Enzyme Nomenclature

Continued from EC 2.1.1.251 to EC 2.1.1.307

EC 2.1.2 to EC 2.2.1

Sections

EC 2.1.2 Hydroxymethyl-, Formyl- and Related Transferases
EC 2.1.3 Carboxy- and Carbamoyltransferases
EC 2.1.4 Amidinotransferases

EC 2.2 Transferring Aldehyde or Ketonic Groups
EC 2.2.1 Transketolases and Transaldolases


EC 2.1.2 Hydroxymethyl-, Formyl- and Related Transferases

('Hydroxymethyltransferase', 'formyltransferase', 'formiminotransferase' may be replaced by 'transhydroxymethylase', 'transformylase' and 'trans-formiminase', respectively).

Contents

EC 2.1.2.1 glycine hydroxymethyltransferase
EC 2.1.2.2 phosphoribosylglycinamide formyltransferase
EC 2.1.2.3 phosphoribosylaminoimidazolecarboxamide formyltransferase
EC 2.1.2.4 glycine formiminotransferase
EC 2.1.2.5 glutamate formiminotransferase
EC 2.1.2.6 deleted, included in EC 2.1.2.5
EC 2.1.2.7 D-alanine 2-hydroxymethyltransferase
EC 2.1.2.8 deoxycytidylate 5-hydroxymethyltransferase
EC 2.1.2.9 methionyl-tRNA formyltransferase
EC 2.1.2.10 aminomethyltransferase
EC 2.1.2.11 3-methyl-2-oxobutanoate hydroxymethyltransferase
EC 2.1.2.12 now EC 2.1.1.74
EC 2.1.2.13 UDP-4-amino-4-deoxy-L-arabinose formyltransferase

Entries

EC 2.1.2.1

Accepted name: glycine hydroxymethyltransferase

Reaction: 5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine

For diagram of reaction click here.

Other name(s): serine aldolase; threonine aldolase; serine hydroxymethylase; serine hydroxymethyltransferase; allothreonine aldolase; L-serine hydroxymethyltransferase; L-threonine aldolase; serine hydroxymethyltransferase; serine transhydroxymethylase

Systematic name: 5,10-methylenetetrahydrofolate:glycine hydroxymethyltransferase

Comments: A pyridoxal-phosphate protein. Also catalyses the reaction of glycine with acetaldehyde to form L-threonine, and with 4-trimethylammoniobutanal to form 3-hydroxy-N6,N6,N6-trimethyl-L-lysine.

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9029-83-8

References:

1. Akhtar, M. and El-Obeid, H.A. Inactivation of serine transhydroxymethylase and threonine aldolase activities. Biochim. Biophys. Acta 258 (1972) 791-799. [PMID: 5017703]

2. Blakley, R.L. A spectrophotometric study of the reaction catalysed by serine transhydroxymethylase. Biochem. J. 77 (1960) 459-465.

3. Fujioka, M. Purification and properties of serine hydroxymethylase from soluble and mitochondrial fractions of rabbit liver. Biochim. Biophys. Acta 185 (1969) 338-349. [PMID: 5808700]

4. Kumagai, H., Nagate, T., Yoshida, H. and Yamada, H. Threonine aldolase from Candida humicola. II. Purification, crystallization and properties. Biochim. Biophys. Acta 258 (1972) 779-790. [PMID: 5017702]

5. Schirch, L.V. and Gross, T. Serine transhydroxymethylase. Identification as the threonine and allothreonine aldolases. J. Biol. Chem. 243 (1968) 5651-5655. [PMID: 5699057]

[EC 2.1.2.1 created 1961, modified 1983]

EC 2.1.2.2

Accepted name: phosphoribosylglycinamide formyltransferase

Reaction: 10-formyltetrahydrofolate + N1-(5-phospho-D-ribosyl)glycinamide = tetrahydrofolate + N2-formyl-N1-(5-phospho-D-ribosyl)glycinamide

For reaction pathway click here.

Other name(s): 2-amino-N-ribosylacetamide 5'-phosphate transformylase; GAR formyltransferase; GAR transformylase; glycinamide ribonucleotide transformylase; GAR TFase; 5,10-methenyltetrahydrofolate:2-amino-N-ribosylacetamide ribonucleotide transformylase

Systematic name: 10-formyltetrahydrofolate:5'-phosphoribosylglycinamide N-formyltransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9032-02-4

References:

1. Hartman, S.C. and Buchanan, J.M. Biosynthesis of the purines. XXVI. The identification of the formyl donors of the transformylation reaction. J. Biol. Chem. 234 (1959) 1812-1816.

2. Smith, G.K., Benkovic, P.A. and Benkovic, S.J. L(–)-10-Formyltetrahydrofolate is the cofactor for glycinamide ribonucleotide transformylase from chicken liver. Biochemistry 20 (1981) 4034-4036. [PMID: 7284307]

3. Warren, L. and Buchanan, J.M. Biosynthesis of the purines. XIX. 2-Amino-N-ribosylacetamide 5'-phosphate (glycinamide ribotide) transformylase. J. Biol. Chem. 229 (1957) 613-626.

[EC 2.1.2.2 created 1961, modified 2000]

EC 2.1.2.3

Accepted name: phosphoribosylaminoimidazolecarboxamide formyltransferase

Reaction: 10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide = tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide

For reaction pathway click here.

Other name(s): 5-amino-4-imidazolecarboxamide ribonucleotide transformylase; AICAR transformylase; 10-formyltetrahydrofolate:5'-phosphoribosyl-5-amino-4-imidazolecarboxamide formyltransferase; 5'-phosphoribosyl-5-amino-4-imidazolecarboxamide formyltransferase; 5-amino-1-ribosyl-4-imidazolecarboxamide 5'-phosphate transformylase; 5-amino-4-imidazolecarboxamide ribotide transformylase; AICAR formyltransferase; aminoimidazolecarboxamide ribonucleotide transformylase

Systematic name: 10-formyltetrahydrofolate:5'-phosphoribosyl-5-amino-4-imidazole-carboxamide N-formyltransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9032-03-5

References:

1. Hartman, S.C. and Buchanan, J.M. Biosynthesis of the purines. XXVI. The identification of the formyl donors of the transformylation reaction. J. Biol. Chem. 234 (1959) 1812-1816.

[EC 2.1.2.3 created 1961, modified 2000]

EC 2.1.2.4

Accepted name: glycine formimidoyltransferase

Reaction: 5-formimidoyltetrahydrofolate + glycine = tetrahydrofolate + N-formimidoylglycine

For diagram of reaction click here.

Other name(s): formiminoglycine formiminotransferase; FIG formiminotransferase; glycine formiminotransferase

Systematic name: 5-formimidoyltetrahydrofolate:glycine N-formimidoyltransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9029-84-9

References:

1. Rabinowitz, J.C. and Pricer, W.E. Formiminotetrahydrofolic acid and methenyltetrahydrofolic acid as intermediates in the formation of N10-formyltetrahydrofolic acid. J. Am. Chem. Soc. 78 (1956) 5702-5704.

2. Rabinowitz, J.C. and Pricer, W.E. Formation, isolation and properties of 5-formiminotetrahydrofolic acid. Fed. Proc. 16 (1957) 236 only.

3. Sagers, R.D., Beck, J.V., Gruber, W. and Gunsalus, I.C. A tetrahydrofolic acid linked formimino transfer enzyme. J. Am. Chem. Soc. 78 (1956) 694-695.

[EC 2.1.2.4 created 1961, modified 2000]

EC 2.1.2.5

Accepted name: glutamate formimidoyltransferase

Reaction: 5-formimidoyltetrahydrofolate + L-glutamate = tetrahydrofolate + N-formimidoyl-L-glutamate

For diagram click here.

Other name(s): glutamate formyltransferase; formiminoglutamic acid transferase; formiminoglutamic formiminotransferase; glutamate formiminotransferase

Systematic name: 5-formimidoyltetrahydrofolate:L-glutamate N-formimidoyltransferase

Comments: A pyridoxal-phosphate protein. Also catalyses formyl transfer from 5-formyltetrahydrofolate to L-glutamate (a reaction formerly listed as EC 2.1.2.6). In eukaryotes, it occurs as a bifunctional enzyme that also has formimidoyltetrahydrofolate cyclodeaminase (EC 4.3.1.4) activity.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9032-83-1

References:

1. Miller, A. and Waelsch, H. Formimino transfer from formamidinoglutaric acid to tetrahydrofolic acid. J. Biol. Chem. 228 (1957) 397-417.

2. Silverman, M., Keresztesy, J.C., Koval, G.J. and Gardiner, R.C. Citrovorium factor and the synthesis of formylglutamic acid. J. Biol. Chem. 226 (1957) 83-94.

3. Tabor, H. and Wyngarden, L. The enzymatic formation of formiminotetrahydrofolic acid, 5,10-methenyltetrahydrofolic acid, and 10-formyltetrahydrofolic acid in the metabolism of formiminoglutamic acid. J. Biol. Chem. 234 (1959) 1830-1849.

[EC 2.1.2.5 created 1961, modified 2000 (EC 2.1.2.6 created 1965, incorporated 1984)]

[EC 2.1.2.6 Deleted entry: glutamate formyltransferase. Now included with EC 2.1.2.5 glutamate formiminotransferase. (EC 2.1.2.6 created 1965, deleted 1984)]

EC 2.1.2.7

Accepted name: D-alanine 2-hydroxymethyltransferase

Reaction: 5,10-methylenetetrahydrofolate + D-alanine + H2O = tetrahydrofolate + 2-methylserine

Other name(s): 2-methylserine hydroxymethyltransferase

Systematic name: 5,10-methylenetetrahydrofolate:D-alanine 2-hydroxymethyltransferase

Comments: Also acts on 2-hydroxymethylserine.

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, CAS registry number: 9075-76-7

References:

1. Wilson, E.M. and Snell, E.E. Metabolism of α-methylserine. I. α-Methylserine hydroxymethyltransferase. J. Biol. Chem. 237 (1962) 3171-3179.

[EC 2.1.2.7 created 1972]

EC 2.1.2.8

Accepted name: deoxycytidylate 5-hydroxymethyltransferase

Reaction: 5,10-methylenetetrahydrofolate + H2O + deoxycytidylate = tetrahydrofolate + 5-hydroxymethyldeoxycytidylate

Other name(s): dCMP hydroxymethylase; d-cytidine 5'-monophosphate hydroxymethylase; deoxyCMP hydroxymethylase; deoxycytidylate hydroxymethylase; deoxycytidylic hydroxymethylase

Systematic name: 5,10-methylenetetrahydrofolate:deoxycytidylate 5-hydroxymethyltransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9012-68-4

References:

1. Mathews, C.K., Brown, F. and Cohen, S.S. Virus-induced acquisition of metabolic function. VII. Biosynthesis de novo of deoxycytidylate hydroxymethylase. J. Biol. Chem. 239 (1964) 2957-2963.

[EC 2.1.2.8 created 1972]

EC 2.1.2.9

Accepted name: methionyl-tRNA formyltransferase

Reaction: 10-formyltetrahydrofolate + L-methionyl-tRNAfMet = tetrahydrofolate + N-formylmethionyl-tRNAfMet

For diagram of reaction click here

Other name(s): N10-formyltetrahydrofolic-methionyl-transfer ribonucleic transformylase; formylmethionyl-transfer ribonucleic synthetase; methionyl ribonucleic formyltransferase; methionyl-tRNA Met formyltransferase; methionyl-tRNA transformylase; methionyl-transfer RNA transformylase; methionyl-transfer ribonucleate methyltransferase; methionyl-transfer ribonucleic transformylase

Systematic name: 10-formyltetrahydrofolate:L-methionyl-tRNA N-formyltransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9015-76-3

References:

1. Dickerman, H.W., Steers, E., Jr., Redfield, B.G. and Weissbach, H. Methionyl soluble ribonucleic acid transformylase. I. Purification and partial characterization. J. Biol. Chem. 242 (1967) 1522-1525. [PMID: 5337045]

[EC 2.1.2.9 created 1972, modified 2002, modified 2012]

EC 2.1.2.10

Accepted name: aminomethyltransferase

Reaction: [protein]-S8-aminomethyldihydrolipoyllysine + tetrahydrofolate = [protein]-dihydrolipoyllysine + 5,10-methylenetetrahydrofolate + NH3

For diagram, click here

Glossary: dihydrolipoyl group

Other name(s): S-aminomethyldihydrolipoylprotein:(6S)-tetrahydrofolate aminomethyltransferase (ammonia-forming); T-protein; glycine synthase; tetrahydrofolate aminomethyltransferase

Systematic name: [protein]-S8-aminomethyldihydrolipoyllysine:tetrahydrofolate aminomethyltransferase (ammonia-forming)

Comments: A component, with EC 1.4.4.2 glycine dehydrogenase (decarboxylating) and EC 1.8.1.4, dihydrolipoyl dehydrogenanse, of the glycine cleavage system, formerly known as glycine synthase. The glycine cleavage system is composed of four components that only loosely associate: the P protein (EC 1.4.4.2), the T protein (EC 2.1.2.10), the L protein (EC 1.8.1.4) and the lipoyl-bearing H protein [3]

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37257-08-2

References:

1. Okamura-Ikeda, J., Fujiwara, K. and Motokawa, Y. Purification and characterization of chicken liver T protein, a component of the glycine cleavage system. J. Biol. Chem. 257 (1982) 135-139.

2. Perham, R.N. Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions. Annu. Rev. Biochem. 69 (2000) 961-1004. [PMID: 10966480]

3. Nesbitt, N.M., Baleanu-Gogonea, C., Cicchillo, R.M., Goodson, K., Iwig, D.F., Broadwater, J.A., Haas, J.A., Fox, B.G. and Booker, S.J. Expression, purification, and physical characterization of Escherichia coli lipoyl(octanoyl)transferase. Protein Expr. Purif. 39 (2005) 269-282. [PMID: 15642479]

[EC 2.1.2.10 created 1972, modified 2003, modified 2006]

EC 2.1.2.11

Accepted name: 3-methyl-2-oxobutanoate hydroxymethyltransferase

Reaction: 5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = tetrahydrofolate + 2-dehydropantoate

For diagram of reaction click here.

Other name(s): α-ketoisovalerate hydroxymethyltransferase; dehydropantoate hydroxymethyltransferase; ketopantoate hydroxymethyltransferase; oxopantoate hydroxymethyltransferase; 5,10-methylene tetrahydrofolate:α-ketoisovalerate hydroxymethyltransferase

Systematic name: 5,10-methylenetetrahydrofolate:3-methyl-2-oxobutanoate hydroxymethyltransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 56093-17-5

References:

1. Powers, S.G. and Snell, E.E. Ketopantoate hydroxymethyltransferase. II. Physical, catalytic, and regulatory properties. J. Biol. Chem. 251 (1976) 3786-3793. [PMID: 6463]

2. Teller, J.H., Powers, S.G. and Snell, E.E. Ketopantoate hydroxymethyltransferase. I. Purification and role in pantothenate biosynthesis. J. Biol. Chem. 251 (1976) 3780-3785. [PMID: 776976]

[EC 2.1.2.11 created 1982]

[EC 2.1.2.12 Deleted entry: now EC 2.1.1.74 methylenetetrahydrofolate-tRNA-(uracil-5-)-methyltransferase (FADH2-oxidizing) (EC 2.1.2.12 created 1983, deleted 1984)]

EC 2.1.2.13

Accepted name: UDP-4-amino-4-deoxy-L-arabinose formyltransferase

Reaction: 10-formyltetrahydrofolate + UDP-4-amino-4-deoxy-β-L-arabinopyranose = 5,6,7,8-tetrahydrofolate + UDP-4-deoxy-4-formamido-β-L-arabinopyranose

Other name(s): UDP-L-Ara4N formyltransferase; ArnAFT

Systematic name: 10-formyltetrahydrofolate:UDP-4-amino-4-deoxy-β-L-arabinose N-formyltransferase

Comments: The activity is part of a bifunctional enzyme also performing the reaction of EC 1.1.1.305 [UDP-glucuronic acid dehydrogenase (UDP-4-keto-hexauronic acid decarboxylating)].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:

References:

1. Breazeale, S.D., Ribeiro, A.A., McClerren, A.L. and Raetz, C.R.H. A formyltransferase required for polymyxin resistance in Escherichia coli and the modification of lipid A with 4-amino-4-deoxy-L-arabinose. Identification and function of UDP-4-deoxy-4-formamido-L-arabinose. J. Biol. Chem. 280 (2005) 14154-14167. [PMID: 15695810]

2. Gatzeva-Topalova, P.Z., May, A.P. and Sousa, M.C. Crystal structure and mechanism of the Escherichia coli ArnA (PmrI) transformylase domain. An enzyme for lipid A modification with 4-amino-4-deoxy-L-arabinose and polymyxin resistance. Biochemistry 44 (2005) 5328-5338. [PMID: 15807526]

3. Williams, G.J., Breazeale, S.D., Raetz, C.R.H. and Naismith, J.H. Structure and function of both domains of ArnA, a dual function decarboxylase and a formyltransferase, involved in 4-amino-4-deoxy-L-arabinose biosynthesis. J. Biol. Chem. 280 (2005) 23000-23008. [PMID: 15809294]

4. Gatzeva-Topalova, P.Z., May, A.P. and Sousa, M.C. Structure and mechanism of ArnA: conformational change implies ordered dehydrogenase mechanism in key enzyme for polymyxin resistance. Structure 13 (2005) 929-942. [PMID: 15939024]

5. Yan, A., Guan, Z. and Raetz, C.R.H. An undecaprenyl phosphate-aminoarabinose flippase required for polymyxin resistance in Escherichia coli. J. Biol. Chem. 282 (2007) 36077-36089. [PMID: 17928292]

[EC 2.1.2.13 created 2010]

EC 2.1.2.14

Accepted name: tobramycin carbamoyltransferase

Reaction: (1) O-carbamoyladenylate + tobramycin = AMP + nebramycin 5'
(2) O-carbamoyladenylate + kanamycin A = AMP + 6''-O-carbamoylkanamycin A

Glossary: tobramycin = (1S,2S,3R,4S,6R)-4,6-diamino-3-(2,6-diamino-2,3,6-trideoxy-α-D-ribo-hexopyranosyloxy)-2-hydroxycyclohexyl 3-amino-3-deoxy-α-D-glucopyranoside
nebramycin 5' = (1S,2S,3R,4S,6R)-4,6-diamino-3-[(2,6-diamino-2,3,6-trideoxy-α-D-ribo-hexopyranosyl)oxy]-2-hydroxycyclohexyl 3-amino-6-O-carbamoyl-3-deoxy-α-D-glucopyranoside
kanamycin A = (1S,2R,3R,4S,6R)-4,6-diamino-3-(6-amino-6-deoxy--D-glucopyranosyloxy)-2-hydroxycyclohexyl 3-amino-3-deoxy--D-glucopyranoside
6''-O-carbamoylkanamycin A = (1S,2R,3R,4S,6R)-4,6-diamino-3-[(6-amino-6-deoxy-α-D-glucopyranosyl)oxy]-2-hydroxycyclohexyl 3-amino-6-O-carbamoyl-3-deoxy-α-D-glucopyranoside

For diagram of reaction click here.

Other name(s): TobZ (ambiguous)

Systematic name: carbamoyl phosphate:tobramycin 6''-O-carbamoyl-transferase

Comments: Binds iron. The enzyme from the bacterium Streptoalloteichus tenebrarius catalyses the activation of carbamoyl phosphate to O-carbamoyladenylate (see EC 2.1.3.13, ATP carbamoyltransferase), and the subsequent carbamoylation of kanamycin and tobramycin.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Parthier, C., Gorlich, S., Jaenecke, F., Breithaupt, C., Brauer, U., Fandrich, U., Clausnitzer, D., Wehmeier, U.F., Bottcher, C., Scheel, D. and Stubbs, M.T. The O-carbamoyltransferase TobZ catalyzes an ancient enzymatic reaction. Angew. Chem. Int. Ed. Engl. 51 (2012) 4046-4052. [PMID: 22383337]

[EC 2.1.3.14 created 2013]


EC 2.1.3 Carboxy- and Carbamoyltransferases

('Carboxytransferase' and 'carbamoyltransferase' may be replaced by 'transcarboxylase' and 'transcarbamoylase' respectively).

Contents

EC 2.1.3.1 methylmalonyl-CoA carboxyltransferase
EC 2.1.3.2 aspartate carbamoyltransferase
EC 2.1.3.3 ornithine carbamoyltransferase
EC 2.1.3.4 deleted
EC 2.1.3.5 oxamate carbamoyltransferase
EC 2.1.3.6 putrescine carbamoyltransferase
EC 2.1.3.7 3-hydroxymethylcephem carbamoyltransferase
EC 2.1.3.8 lysine carbamoyltransferase
EC 2.1.3.9 N-acetylornithine carbamoyltransferase
EC 2.1.3.10 malonyl-S-ACP:biotin-protein carboxyltransferase
EC 2.1.3.11 N-succinylornithine carbamoyltransferase
EC 2.1.3.12 decarbamoylnovobiocin carbamoyltransferase
EC 2.1.3.13 deleted now covered by EC 6.1.2.2
EC 2.1.3.14 deleted now covered by EC 6.1.2.2


Entries

EC 2.1.3.1

Accepted name: methylmalonyl-CoA carboxytransferase

Reaction: (S)-methylmalonyl-CoA + pyruvate = propanoyl-CoA + oxaloacetate

Other name(s): transcarboxylase; methylmalonyl coenzyme A carboxyltransferase; methylmalonyl-CoA transcarboxylase; oxalacetic transcarboxylase; methylmalonyl-CoA carboxyltransferase; methylmalonyl-CoA carboxyltransferase; (S)-2-methyl-3-oxopropanoyl-CoA:pyruvate carboxyltransferase; (S)-2-methyl-3-oxopropanoyl-CoA:pyruvate carboxytransferase carboxytransferase [incorrect]

Systematic name: (S)-methylmalonyl-CoA:pyruvate carboxytransferase

Comments: A biotinyl-protein, containing cobalt and zinc.

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, UM-BBD, CAS registry number: 9029-86-1

References:

1. Hoffmann, A., Hilpert, W. and Dimroth, P. The carboxyltransferase activity of the sodium-ion-translocating methylmalonyl-CoA decarboxylase of Veillonella alcalescens. Eur. J. Biochem. 179 (1989) 645-650. [PMID: 2920730]

2. Swick, R.W. and Wood, H.G. The role of transcarboxylation in propionic acid fermentation. Proc. Natl. Acad. Sci. USA 46 (1960) 28-41.

[EC 2.1.3.1 created 1961]

EC 2.1.3.2

Accepted name: aspartate carbamoyltransferase

Reaction: carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate

For diagram click here.

Other name(s): carbamylaspartotranskinase; aspartate transcarbamylase; aspartate carbamyltransferase; aspartic acid transcarbamoylase; aspartic carbamyltransferase; aspartic transcarbamylase; carbamylaspartotranskinase; L-aspartate transcarbamoylase; L-aspartate transcarbamylase; carbamoylaspartotranskinase; aspartate transcarbamylase; aspartate transcarbamoylase; ATCase

Systematic name: carbamoyl-phosphate:L-aspartate carbamoyltransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9012-49-1

References:

1. Lowenstein, J.M. and Cohen, P.P. Studies on the biosynthesis of carbamylaspartic acid. J. Biol. Chem. 220 (1956) 57-70.

2. Reichard, P. and Hanshoff, G. Aspartate carbamyl transferase from Escherichia coli. Acta Chem. Scand. 10 (1956) 548-566.

3. Shepherson, M. and Pardee, A.B. Production and crystallization of aspartate transcarbamylase. J. Biol. Chem. 235 (1960) 3233-3237.

[EC 2.1.3.2 created 1961]

EC 2.1.3.3

Accepted name: ornithine carbamoyltransferase

Reaction: carbamoyl phosphate + L-ornithine = phosphate + L-citrulline

For diagram click here.

Other name(s): citrulline phosphorylase; ornithine transcarbamylase; OTC; carbamylphosphate-ornithine transcarbamylase; L-ornithine carbamoyltransferase; L-ornithine carbamyltransferase; L-ornithine transcarbamylase; ornithine carbamyltransferase

Systematic name: carbamoyl-phosphate:L-ornithine carbamoyltransferase

Comments: The plant enzyme also catalyses the reactions of EC 2.1.3.6 putrescine carbamoyltransferase, EC 2.7.2.2 carbamate kinase and EC 3.5.3.12 agmatine deiminase, thus acting as putrescine synthase, converting agmatine [(4-aminobutyl)guanidine] and ornithine into putrescine and citrulline, respectively.

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9001-69-8

References:

1. Bishop, S.H. and Grisolia, S. Crystalline ornithine transcarbamylase. Biochim. Biophys. Acta 139 (1967) 344-348.

2. Marshall, M. and Cohen, P.P. Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. I. Isolation and subunit structure. J. Biol. Chem. 247 (1972) 1641-1653. [PMID: 4622303]

3. Marshall, M. and Cohen, P.P. Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for carbamyl-P and L-norvaline, correlation with steady state kinetics. J. Biol. Chem. 247 (1972) 1654-1668. [PMID: 4622304]

4. Marshall, M. and Cohen, P.P. Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. 3. Effects of chemical modifications of specific residues on ligand binding and enzymatic activity. J. Biol. Chem. 247 (1972) 1669-1682. [PMID: 4622305]

[EC 2.1.3.3 created 1961]

[EC 2.1.3.4 Deleted entry: malonyl-CoA carboxyltransferase. (EC 2.1.3.4 created 1965, deleted 1972)]

EC 2.1.3.5

Accepted name: oxamate carbamoyltransferase

Reaction: carbamoyl phosphate + oxamate = phosphate + oxalureate

For diagram click here.

Other name(s): oxamic transcarbamylase

Systematic name: carbamoyl-phosphate:oxamate carbamoyltransferase

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, CAS registry number: 62213-52-9

References:

1. Bojanowski, R., Gaudy, E., Valentine, R.C. and Wolfe, R.S. Oxamic transcarbamylase of Streptococcus allantoicus. J. Bacteriol. 87 (1964) 75-80.

[EC 2.1.3.5 created 1976]

EC 2.1.3.6

Accepted name: putrescine carbamoyltransferase

Reaction: carbamoyl phosphate + putrescine = phosphate + N-carbamoylputrescine

Other name(s): PTCase; putrescine synthase; putrescine transcarbamylase

Systematic name: carbamoyl-phosphate:putrescine carbamoyltransferase

Comments: The plant enzyme also catalyses the reactions of EC 2.1.3.3 ornithine carbamoyltransferase, EC 2.7.2.2 carbamate kinase and EC 3.5.3.12 agmatine deiminase, thus acting as putrescine synthase, converting agmatine [(4-aminobutyl)guanidine] and ornithine into putrescine and citrulline, respectively.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9076-55-5

References:

1. Roon, R.J. and Barker, H.A. Fermentation of agmatine in Streptococcus faecalis: occurrence of putrescine transcarbamoylase. J. Bacteriol. 109 (1972) 44-50. [PMID: 4621632]

2. Srivenugopal, K.S. and Adiga, P.R. Enzymic conversion of agmatine to putrescine in Lathyrus sativus seedlings. Purification and properties of a multifunctional enzyme (putrescine synthase). J. Biol. Chem. 256 (1981) 9532-9541. [PMID: 6895223]

[EC 2.1.3.6 created 1976]

EC 2.1.3.7

Accepted name: 3-hydroxymethylcephem carbamoyltransferase

Reaction: carbamoyl phosphate + a 3-hydroxymethylceph-3-em-4-carboxylate = phosphate + a 3-carbamoyloxymethylcephem

Systematic name: carbamoyl-phosphate:3-hydroxymethylceph-3-em-4-carboxylate carbamoyltransferase

Comments: Acts on a wide range of 3-hydroxymethylcephems (a subclass of the cephalosporin antibiotics). Activated by ATP.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 74315-96-1

References:

1. Brewer, S.J., Taylor, P.M. and Turner, M.K. An adenosine triphosphate-dependent carbamoylphosphate--3-hydroxymethylcephem O-carbamoyltransferase from Streptomyces clavuligerus. Biochem. J. 185 (1980) 555-564.

[EC 2.1.3.7 created 1983]

EC 2.1.3.8

Accepted name: lysine carbamoyltransferase

Reaction: carbamoyl phosphate + L-lysine = phosphate + L-homocitrulline

Other name(s): lysine transcarbamylase

Systematic name: carbamoyl-phosphate:L-lysine carbamoyltransferase

Comments: Not identical with EC 2.1.3.3 ornithine carbamoyltransferase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 86352-19-4

References:

1. Hommes, F.A., Eller, A.G., Scott, D.F. and Carter, A.L. Separation of ornithine and lysine activities of the ornithine-transcarbamylase-catalyzed reaction. Enzyme 29 (1983) 271-277. [PMID: 6409607]

[EC 2.1.3.8 created 1986]

EC 2.1.3.9

Accepted name: N-acetylornithine carbamoyltransferase

Reaction: carbamoyl phosphate + N2-acetyl-L-ornithine = phosphate + N-acetyl-L-citrulline

Glossary: N-acetyl-L-citrulline = N5-acetylcarbamoyl-L-ornithine

Other name(s): acetylornithine transcarbamylase; N-acetylornithine transcarbamylase; AOTC

Systematic name: carbamoyl-phosphate:N2-acetyl-L-ornithine carbamoyltransferase

Comments: Differs from EC 2.1.3.3, ornithine carbamoyltransferase. This enzyme replaces EC 2.1.3.3 in the canonic arginine biosynthetic pathway of several Eubacteria and has no catalytic activity with L-ornithine as substrate.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 890853-54-0

References:

1. Shi, D., Morizono, H., Yu, X., Roth, L., Caldovic, L., Allewell, N.M., Malamy, M.H. and Tuchman, M. Crystal structure of N-acetylornithine transcarbamylase from Xanthomonas campestris: a novel enzyme in a new arginine biosynthetic pathway found in several Eubacteria. J. Biol. Chem. 280 (2005) 14366-14369. [PMID: 15731101]

2. Morizono, H., Cabrera-Luque, J., Shi, D., Gallegos, R., Yamaguchi, S., Yu, X., Allewell, N.M., Malamy, M.H. and Tuchman, M. Acetylornithine transcarbamylase: a novel enzyme in arginine biosynthesis. J. Bacteriol. 188 (2006) 2974-2982. [PMID: 16585758]

[EC 2.1.3.9 created 2005]

EC 2.1.3.10

Accepted name: malonyl-S-ACP:biotin-protein carboxyltransferase

Reaction: a malonyl-[acyl-carrier protein] + a biotinyl-[protein] = an acetyl-[acyl-carrier protein] + a carboxybiotinyl-[protein]

For diagram of the reaction click here

Other name(s): malonyl-S-acyl-carrier protein:biotin-protein carboxyltransferase; MadC/MadD; MadC,D; malonyl-[acyl-carrier protein]:biotinyl-[protein] carboxyltransferase

Systematic name: malonyl-[acyl-carrier protein]:biotinyl-[protein] carboxytransferase

Comments: Derived from the components MadC and MadD of the anaerobic bacterium Malonomonas rubra, this enzyme is a component of EC 4.1.1.89, biotin-dependent malonate decarboxylase. The carboxy group is transferred from malonate to the prosthetic group of the biotin protein (MadF) with retention of configuration [2]. Similar to EC 4.1.1.87, malonyl-S-ACP decarboxylase, which forms part of the biotin-independent malonate decarboxylase (EC 4.1.1.88), this enzyme also follows on from EC 2.3.1.187, acetyl-S-ACP:malonate ACP transferase, and results in the regeneration of the acetyl-[acyl-carrier protein] [3].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Berg, M., Hilbi, H. and Dimroth, P. Sequence of a gene cluster from Malonomonas rubra encoding components of the malonate decarboxylase Na+ pump and evidence for their function. Eur. J. Biochem. 245 (1997) 103-115. [PMID: 9128730]

2. Micklefield, J., Harris, K.J., Gröger, S., Mocek, U., Hilbi, H., Dimroth, P. and Floss, H.G. Stereochemical course of malonate decarboxylase in Malonomonas rubra has biotin decarboxylation with retention. J. Am. Chem. Soc. 117 (1995) 1153-1154.

3. Dimroth, P. and Hilbi, H. Enzymic and genetic basis for bacterial growth on malonate. Mol. Microbiol. 25 (1997) 3-10. [PMID: 11902724]

[EC 2.1.3.10 created 2008]

EC 2.1.3.11

Accepted name: N-succinylornithine carbamoyltransferase

Reaction: carbamoyl phosphate + N2-succinyl-L-ornithine = phosphate + N-succinyl-L-citrulline

Glossary: N-acetyl-L-citrulline = N5-acetylcarbamoyl-L-ornithine

Other name(s): succinylornithine transcarbamylase; N-succinyl-L-ornithine transcarbamylase; SOTCase

Systematic name: carbamoyl phosphate:N2-succinyl-L-ornithine carbamoyltransferase

Comments: This enzyme is specific for N-succinyl-L-ornithine and cannot use either L-ornithine (see EC 2.1.3.3, ornithine carbamoyltransferase) or N-acetyl-L-ornithine (see EC 2.1.3.9, N-acetylornithine carbamoyltransferase) as substrate. However, a single amino-acid substitution (Pro90 → Glu90) is sufficient to switch the enzyme to one that uses N-acetyl-L-ornithine as substrate. It is essential for de novo arginine biosynthesis in the obligate anaerobe Bacteroides fragilis, suggesting that this organism uses an alternative pathway for synthesizing arginine.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Shi, D., Morizono, H., Cabrera-Luque, J., Yu, X., Roth, L., Malamy, M.H., Allewell, N.M. and Tuchman, M. Structure and catalytic mechanism of a novel N-succinyl-L-ornithine transcarbamylase in arginine biosynthesis of Bacteroides fragilis. J. Biol. Chem. 281 (2006) 20623-20631. [PMID: 16704984]

2. Shi, D., Yu, X., Cabrera-Luque, J., Chen, T.Y., Roth, L., Morizono, H., Allewell, N.M. and Tuchman, M. A single mutation in the active site swaps the substrate specificity of N-acetyl-L-ornithine transcarbamylase and N-succinyl-L-ornithine transcarbamylase. <>Protein Sci. 16 (2007) 1689-1699. [PMID: 17600144]

[EC 2.1.3.11 created 2008]

EC 2.1.3.12

Accepted name: decarbamoylnovobiocin carbamoyltransferase

Reaction: carbamoyl phosphate + decarbamoylnovobiocin = phosphate + novobiocin

Glossary: decarbamoylnovobiocin = N-{7-[(6-deoxy-5-methyl-4-O-methyl-β-D-gulopyranosyl)oxy]4-hydroxy-8-methyl-2-oxo-2H-chromen-3-yl}-4-hydroxy-3-(3-methyl-2-buten-1-yl)benzamide

Other name(s): novN (gene name)

Systematic name: carbamoyl phosphate:decarbamoylnovobiocin 3''-O-carbamoyltransferase

Comments: The enzyme catalyses the last step in the biosynthesis of the aminocoumarin antibiotic novobiocin. The reaction is activated by ATP [1].

Links to other databases: BRENDA, EXPASY, KEGG Metacyc, CAS registry number:

References:

1. Freel Meyers, C.L., Oberthur, M., Xu, H., Heide, L., Kahne, D. and Walsh, C.T. Characterization of NovP and NovN: completion of novobiocin biosynthesis by sequential tailoring of the noviosyl ring. Angew. Chem. Int. Ed. Engl. 43 (2004) 67-70. [PMID: 14694473]

2. Gomez Garcia, I., Freel Meyers, C.L., Walsh, C.T. and Lawson, D.M. Crystallization and preliminary X-ray analysis of the O-carbamoyltransferase NovN from the novobiocin-biosynthetic cluster of Streptomyces spheroides. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 64 (2008) 1000-1002. [PMID: 18997325]

[EC 2.1.3.12 created 2013]

[EC 2.1.3.13 Deleted entry: ATP carbamoyltransferase. The enzyme has been replaced by EC 6.1.2.2, nebramycin 5' synthase (EC 2.1.3.13 created 2013, deleted 2014)]

[EC 2.1.3.14 Deleted entry: tobramycin carbamoyltransferase. The enzyme has been replaced by EC 6.1.2.2, nebramycin 5' synthase (EC 2.1.3.14 created 2013, deleted 2014)]


EC 2.1.4 Amidinotransferases

('Amidinotransferase' may be replaced by 'transamidinase')

Contents

EC 2.1.4.1 glycine amidinotransferase
EC 2.1.4.2 scyllo-inosamine-4-phosphate amidinotransferase


Entries

EC 2.1.4.1

Accepted name: glycine amidinotransferase

Reaction: L-arginine + glycine = L-ornithine + guanidinoacetate

For diagram of reaction click here.

Other name(s): arginine-glycine amidinotransferase; arginine-glycine transamidinase; glycine transamidinase

Systematic name: L-arginine:glycine amidinotransferase

Comments: Canavanine can act instead of arginine. Formerly EC 2.6.2.1.

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9027-35-4

References:

1. Borsook, H. and Dubnoff, J.W. The formation of glycocyamine in animal tissues. J. Biol. Chem. 138 (1941) 389-403.

2. Conconi, F. and Grazi, E. Transamidinase of hog kidney. I. Purification and properties. J. Biol. Chem. 240 (1965) 2461-2464.

3. McGuire, D.M., Tormanen, C.D., Segal, I.S. and van Pilsum, J.F. The effect of growth hormone and thyroxine on the amount of L-arginine:glycine amidinotransferase in kidneys of hypophysectomized rats, purification and some properties of rat kidney transamidinase. J. Biol. Chem. 255 (1980) 1152-1159.

4. Ratner, S. Transamidination. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd ed., vol. 6, Academic Press, New York, 1962, pp. 267-275.

5. Ratner, S. and Rochovansky, O. Biosynthesis of guanidinoacetic acid. I. Purification and properties of transamidinase. Arch. Biochem. Biophys. 63 (1956) 277-295.

6. Ratner, S. and Rochovansky, O. Biosynthesis of guanidinoacetic acid. II. Mechanism of amidine group transfer. Arch. Biochem. Biophys. 63 (1956) 296-315.

7. Walker, J.B. Biosynthesis of arginine from canavanine and ornithine in kidney. J. Biol. Chem. 218 (1956) 549-556.

8. Walker, J.B. Studies on the mechanism of action of kidney transamidinase. J. Biol. Chem. 224 (1957) 57-66.

[EC 2.1.4.1 created 1961 as EC 2.6.2.1, transferred 1965 to EC 2.1.4.1]

EC 2.1.4.2

Accepted name: scyllo-inosamine-4-phosphate amidinotransferase

Reaction: L-arginine + 1-amino-1-deoxy-scyllo-inositol 4-phosphate = L-ornithine + 1-guanidino-1-deoxy-scyllo-inositol 4-phosphate

Other name(s): L-arginine:inosamine-P-amidinotransferase; inosamine-P amidinotransferase; L-arginine:inosamine phosphate amidinotransferase; inosamine-phosphate amidinotransferase

Systematic name: L-arginine:1-amino-1-deoxy-scyllo-inositol-4-phosphate amidinotransferase

Comments: 1D-1-Guanidino-3-amino-1,3-dideoxy-scyllo-inositol 6-phosphate, streptamine phosphate and 2-deoxystreptamine phosphate can also act as acceptors; canavanine can act as donor.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 52227-63-1

References:

1. Walker, M.S. and Walker, J.B. Enzymic studies on the biosynthesis of streptomycin, transamidation of inosamine and streptamine derivatives. J. Biol. Chem. 241 (1966) 1262-1269.

[EC 2.1.4.2 created 1976, modified 2001]


EC 2.2 Transferring Aldehyde or Ketonic Groups

EC 2.2.1 Transketolases and Transaldolases

Contents

EC 2.2.1.1 transketolase
EC 2.2.1.2 transaldolase
EC 2.2.1.3 formaldehyde transketolase
EC 2.2.1.4 acetoin—ribose-5-phosphate transaldolase
EC 2.2.1.5 2-hydroxy-3-oxoadipate synthase
EC 2.2.1.6 acetolactate synthase
EC 2.2.1.7 1-deoxy-D-xylulose-5-phosphate synthase
EC 2.2.1.8 fluorothreonine transaldolase
EC 2.2.1.9 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase
EC 2.2.1.10 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthase
EC 2.2.1.11 6-deoxy-5-ketofructose 1-phosphate synthase


Entries

EC 2.2.1.1

Accepted name: transketolase

Reaction: sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate

For diagram click here (mechanism), another example click here or here.

Glossary: thiamine diphosphate

Other name(s): glycolaldehydetransferase

Systematic name: sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate glycolaldehydetransferase

Comments: A thiamine-diphosphate protein. Wide specificity for both reactants, e.g. converts hydroxypyruvate and R-CHO into CO2 and R-CHOH-CO-CH2OH. Transketolase from Alkaligenes faecalis shows high activity with D-erythrose as acceptor.

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9014-48-6

References:

1. de la Haba, G., Leder, I.G. and Racker, E. Crystalline transketolase from bakers' yeast: isolation and properties. J. Biol. Chem. 214 (1955) 409-426.

2. Domagk, G.F. and Horecker, B.L. Fructose and erythrose metabolism in Alcaligenes faecalis. Arch. Biochem. Biophys. 109 (1965) 342-349.

3. Horecker, B.L., Smyrniotis, P.Z. and Hurwitz, J. The role of xylulose 5-phosphate in the transketolase reaction. J. Biol. Chem. 223 (1956) 1009-1019.

4. Racker, E. Transketolase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd ed., vol. 5, Academic Press, New York, 1961, pp. 397-412.

[EC 2.2.1.1 created 1961]

EC 2.2.1.2

Accepted name: transaldolase

Reaction: sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate

For diagram of reaction click here (mechanism), another example click here.

Other name(s): dihydroxyacetonetransferase; dihydroxyacetone synthase; formaldehyde transketolase

Systematic name: sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate glyceronetransferase

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9014-46-4

References:

1. Horecker, B.L. and Smyrniotis, P.Z. Purification and properties of yeast transaldolase. J. Biol. Chem. 212 (1955) 811-825.

2. Racker, E. Transaldolase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd ed., vol. 5, Academic Press, New York, 1961, pp. 407-412.

3. Tsolas, O. and Horecker, B.L. Transaldolase. In: Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 7, Academic Press, New York, 1972, pp. 259-280.

[EC 2.2.1.2 created 1961]

EC 2.2.1.3

Accepted name: formaldehyde transketolase

Reaction: D-xylulose 5-phosphate + formaldehyde = D-glyceraldehyde 3-phosphate + glycerone

For diagram click here.

Glossary: thiamine diphosphate

Other name(s): dihydroxyacetone synthase

Systematic name: D-xylulose-5-phosphate:formaldehyde glycolaldehydetransferase

Comments: A thiamine-diphosphate protein. Not identical with EC 2.2.1.1 transketolase. Also converts hydroxypyruvate and formaldehyde into glycerone and CO2.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 124566-23-0

References:

1. Bystrykh, L.V., Sokolov, A.P. and Trotsenko, Yu.A. Separation of transketolase and dihydroxyacetone synthase from methylotrophic yeasts. Dokl. Akad. Nauk S.S.S.R. 258 (1981) 499-501 [in Russian].

2. Kato, N., Higuchi, T., Sakazawa, C., Nishizawa, T., Tani, Y. and Yamada, H. Purification and properties of a transketolase responsible for formaldehyde fixation in a methanol-utilizing yeast, Candida boidinii (Kloeckera sp.) No. 2201. Biochim. Biophys. Acta 715 (1982) 143-150.

3. Waites, M.J. and Quayle, J.R. The interrelation between transketolase and dihydroxyacetone synthase activities in the methylotrophic yeast Candida boidinii. J. Gen. Microbiol. 124 (1981) 309-316.

[EC 2.2.1.3 created 1984]

EC 2.2.1.4

Accepted name: acetoin—ribose-5-phosphate transaldolase

Reaction: 3-hydroxybutan-2-one + D-ribose 5-phosphate = acetaldehyde + 1-deoxy-D-altro-heptulose 7-phosphate

For diagram click here.

Glossary: thiamine diphosphate

Other name(s): 1-deoxy-D-altro-heptulose-7-phosphate synthetase; 1-deoxy-D-altro-heptulose-7-phosphate synthase; 3-hydroxybutan-2-one:D-ribose-5-phosphate aldehydetransferase [wrong substrate name]

Systematic name: 3-hydroxybutan-2-one:D-ribose-5-phosphate aldehydetransferase

Comments: A thiamine-diphosphate protein.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 87843-76-3

References:

1. Yokota, A. and Sasajima, K. Enzymatic formation of a new monosaccharide, 1-deoxy-D-altro-heptulose phosphate, from DL-acetoin and D-ribose 5-phosphate by a transketolase mutant of Bacillus pumilus. Agric. Biol. Chem. 47 (1983) 1545-1553.

[EC 2.2.1.4 created 1989]

EC 2.2.1.5

Accepted name: 2-hydroxy-3-oxoadipate synthase

Reaction: 2-oxoglutarate + glyoxylate = 2-hydroxy-3-oxoadipate + CO2

For diagram click here.

Glossary: thiamine diphosphate

Other name(s): 2-hydroxy-3-oxoadipate glyoxylate-lyase (carboxylating); α-ketoglutaric-glyoxylic carboligase; oxoglutarate: glyoxylate carboligase

Systematic name: 2-oxoglutarate:glyoxylate succinaldehydetransferase (decarboxylating)

Comments: The bacterial enzyme requires thiamine diphosphate. The product decarboxylates to 5-hydroxy-4-oxopentanoate. The enzyme can decarboxylate 2-oxoglutarate. Acetaldehyde can replace glyoxylate.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9054-72-2

References:

1. Schlossberg, M.A., Bloom, R.J., Richert, D.A. and Westerfield, W.W. Carboligase activity of α-ketoglutarate dehydrogenase. Biochemistry 9 (1970) 1148-1153. [PMID: 5418712]

2. Schlossberg, M.A., Richert, D.A., Bloom, R.J. and Westerfield, W.W. Isolation and identification of 5-hydroxy-4-ketovaleric acid as a product of α-ketoglutarate: glyoxylate carboligase. Biochemistry 7 (1968) 333-337. [PMID: 4320439]

3. Stewart, P.R. and Quayle, J.R. The synergistic decarboxylation of glyoxalate and 2-oxoglutarate by an enzyme system from pig-liver mitochondria. Biochem. J. 102 (1967) 885-897.

[EC 2.2.1.5 created 1972 as EC 4.1.3.15, transferred 2002 to EC 2.2.1.5]

EC 2.2.1.6

Accepted name: acetolactate synthase

Reaction: 2 pyruvate = 2-acetolactate + CO2

For diagram click here.

Glossary: thiamine diphosphate

Other name(s): α-acetohydroxy acid synthetase; α-acetohydroxyacid synthase; α-acetolactate synthase; α-acetolactate synthetase; acetohydroxy acid synthetase; acetohydroxyacid synthase; acetolactate pyruvate-lyase (carboxylating); acetolactic synthetase

Systematic name: pyruvate:pyruvate acetaldehydetransferase (decarboxylating)

Comments: This enzyme requires thiamine diphosphate. The reaction shown is in the pathway of biosynthesis of valine; the enzyme can also transfer the acetaldehyde from pyruvate to 2-oxobutanoate, forming 2-ethyl-2-hydroxy-3-oxobutanoate, also known as 2-aceto-2-hydroxybutanoate, a reaction in the biosynthesis of isoleucine.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9027-45-6

References:

1. Bauerle, R.H., Freundlich, M., Størmer, F.C. and Umbarger, H.E. Control of isoleucine, valine and leucine biosynthesis. II. Endproduct inhibition by valine of acetohydroxy acid synthetase in Salmonella typhimurium. Biochim. Biophys. Acta 92 (1964) 142-149.

2. Huseby, N.E., Christensen, T.B., Olsen, B.R. and Størmer, F.C. The pH 6 acetolactate-forming enzyme from Aerobacter aerogenes. Subunit structure. Eur. J. Biochem. 20 (1971) 209-214. [PMID: 5560406]

3. Størmer, F.C., Solberg, Y. and Hovig, T. The pH 6 acetolactate-forming enzyme from Aerobacter aerogenes. Molecular properties. Eur. J. Biochem. 10 (1969) 251-260. [PMID: 5823101]

4. Barak, Z., Chipman, D.M. and Gollop, N. Physiological implications of the specificity of acetohydroxy acid synthase isozymes of enteric bacteria. J. Bacteriol. 169 (1987) 3750-3756. [PMID: 3301814]

[EC 2.2.1.6 created 1972 as EC 4.1.3.18, transferred 2002 to EC 2.2.1.6]

EC 2.2.1.7

Accepted name: 1-deoxy-D-xylulose-5-phosphate synthase

Reaction: pyruvate + D-glyceraldehyde 3-phosphate = 1-deoxy-D-xylulose 5-phosphate + CO2

For diagram click here and mechanism here

Glossary: thiamine diphosphate

Other name(s): 1-deoxy-D-xylulose-5-phosphate pyruvate-lyase (carboxylating); DXP-synthase

Systematic name: pyruvate:D-glyceraldehyde-3-phosphate acetaldehydetransferase (decarboxylating)

Comments: Requires thiamine diphosphate. The enzyme forms part of an alternative nonmevalonate pathway for terpenoid biosynthesis (for diagram, click here).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 202218-79-9

References:

1. Sprenger, G.A., Schörken, U., Weigert, T., Grolle, S., deGraaf, A.A., Taylor, S.V., Begley, T.P., Bringer-Meyer, S. and Sahm, H. Identification of a thiamin-dependent synthase in Escherichia coli required for the formation of the 1-deoxy-D-xylulose 5-phosphate precursor to isoprenoids, thiamin, and pyridoxol. Proc. Natl. Acad. Sci. USA 94 (1997) 12857-12862. [PMID: 9371765]

2. Kuzuyama, T., Takagi, M., Takahashi, S. and Seto, H. Cloning and characterization of 1-deoxy-D-xylulose 5-phosphate synthase from Streptomyces sp. strain CL190, which uses both the mevalonate and nonmevalonate pathways for isopentenyl diphosphate biosynthesis. J. Bacteriol. 182 (2000) 891-897. [PMID: 10648511]

[EC 2.2.1.7 created 2001 as EC 4.1.3.37 transferred 2002 to EC 2.2.1.7]

EC 2.2.1.8

Accepted name: fluorothreonine transaldolase

Reaction: L-threonine + fluoroacetaldehyde = acetaldehyde + 4-fluoro-L-threonine

Systematic name: fluoroacetaldehyde:L-threonine aldehydetransferase

Comments: A pyridoxal phosphate protein. Can also convert chloroacetaldehyde into 4-chloro-L-threonine. Unlike EC 2.1.2.1, glycine hydroxymethyltransferase, does not use glycine as a substrate.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 403503-13-9

References:

1. Murphy, C.D., O'Hagan, D. and Schaffrath, C. Identification of a PLP-dependent threonine transaldolase: a novel enzyme involved in 4-fluorothreonine biosynthesis in Streptomyces cattleya. Angew. Chem. Int. Ed. Engl. 40 (2001) 4479-4481. [PMID: 12404452]

2. Murphy, C.D., Schaffrath, C. and O'Hagan, D. Fluorinated natural products: the biosynthesis of fluoroacetate and 4-fluorothreonine in Streptomyces cattleya. Chemosphere 52 (2003) 455-461. [PMID: 12738270]

[EC 2.2.1.8 created 2003]

EC 2.2.1.9

Accepted name: 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase

Reaction: isochorismate + 2-oxoglutarate = 5-enolpyruvoyl-6-hydroxy-2-succinylcyclohex-3-ene-1-carboxylate + CO2

For diagram of reaction, click here.

Other name(s): SEPHCHC synthase; MenD

Systematic name: isochorismate:2-oxoglutarate 4-oxopentanoatetransferase (decarboxylating)

Comments: Requires Mg2+ for maximal activity. This enzyme is involved in the biosynthesis of vitamin K2 (menaquinone). In most anaerobes and all Gram-positive aerobes, menaquinone is the sole electron transporter in the respiratory chain and is essential for their survival. It had previously been thought that the products of the reaction were (1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate (SHCHC), pyruvate and CO2 but it is now known that two separate enzymes are involved: this enzyme and EC 4.2.99.20, 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase. Under basic conditions, the product can spontaneously lose pyruvate to form SHCHC.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 1112282-73-1

References:

1. Jiang, M., Cao, Y., Guo, Z.F., Chen, M., Chen, X. and Guo, Z. Menaquinone biosynthesis in Escherichia coli: identification of 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate as a novel intermediate and re-evaluation of MenD activity. Biochemistry 46 (2007) 10979-10989. [PMID: 17760421]

[EC 2.2.1.9 created 2008 (EC 2.5.1.64 created 2003, part-incorporated 2008)]

EC 2.2.1.10

Accepted name: 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthase

Reaction: L-aspartate 4-semialdehyde + 1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate = 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate + 2,3-dioxopropyl phosphate

For diagram of reaction click here.

Glossary: 1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate = 6-deoxy-5-ketofructose 1-phosphate
2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate = 2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate

Other name(s): ADH synthase; ADHS; MJ0400 (gene name)

Systematic name: L-aspartate 4-semialdehyde:1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate methylglyoxaltransferase

Comments: The enzyme plays a key role in an alternative pathway of the biosynthesis of 3-dehydroquinate (DHQ), which is involved in the canonical pathway for the biosynthesis of aromatic amino acids. The enzyme can also catalyse the reaction of EC 4.1.2.13, fructose-bisphosphate aldolase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:

References:

1. White, R.H. L-Aspartate semialdehyde and a 6-deoxy-5-ketohexose 1-phosphate are the precursors to the aromatic amino acids in Methanocaldococcus jannaschii. Biochemistry 43 (2004) 7618-7627. [PMID: 15182204]

2. Samland, A.K., Wang, M. and Sprenger, G.A. MJ0400 from Methanocaldococcus jannaschii exhibits fructose-1,6-bisphosphate aldolase activity. FEMS Microbiol. Lett. 281 (2008) 36-41. [PMID: 18318840]

3. Morar, M., White, R.H. and Ealick, S.E. Structure of 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid synthase, a catalyst in the archaeal pathway for the biosynthesis of aromatic amino acids. Biochemistry 46 (2007) 10562-10571. [PMID: 17713928]

[EC 2.2.1.10 created 2012]

EC 2.2.1.11

Accepted name: 6-deoxy-5-ketofructose 1-phosphate synthase

Reaction: (1) methylglyoxal + D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + 1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate
(2) methylglyoxal + D-fructose 1-phosphate = D-glyceraldehyde + 1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate

For diagram of reaction click here.

Glossary: methylglyoxal = 2-oxopropanal
1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate = 6-deoxy-5-ketofructose 1-phosphate

Other name(s): DKFP synthase; MJ1585 (gene name)

Systematic name: 2-oxopropanal:D-fructose 1,6-bisphosphate glycerone-phosphotransferase

Comments: The enzyme plays a key role in an alternative pathway of the biosynthesis of 3-dehydroquinate (DHQ), which is involved in the canonical pathway for the biosynthesis of aromatic amino acids. The enzyme can also catalyse the reaction of EC 4.1.2.13, fructose-bisphosphate aldolase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. White, R.H. and Xu, H. Methylglyoxal is an intermediate in the biosynthesis of 6-deoxy-5-ketofructose-1-phosphate: a precursor for aromatic amino acid biosynthesis in Methanocaldococcus jannaschii. Biochemistry 45 (2006) 12366-12379. [PMID: 17014089]

2. Samland, A.K., Wang, M. and Sprenger, G.A. MJ0400 from Methanocaldococcus jannaschii exhibits fructose-1,6-bisphosphate aldolase activity. FEMS Microbiol. Lett. 281 (2008) 36-41. [PMID: 18318840]

[EC 2.2.1.11 created 2012]


Continued with EC 2.3.1.1 to EC 2.3.1.50
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