Continued from EC 4.2.3.101-142
[EC 4.2.99.2 Transferred entry: now EC 4.2.3.1, threonine synthase (EC 4.2.99.2 created 1961, deleted 2000)]
[EC 4.2.99.3 Transferred entry: now EC 4.2.2.2 pectate lyase (EC 4.2.99.3 created 1965, deleted 1972)]
[EC 4.2.99.4 Transferred entry: now EC 4.2.2.3 alginate lyase (EC 4.2.99.4 created 1965, deleted 1972)]
[EC 4.2.99.5 Deleted entry: polyglucuronide lyase (EC 4.2.99.5 created 1965, deleted 1972)]
[EC 4.2.99.6 Deleted entry: chondroitin sulfate lyase. Now included with EC 4.2.2.4 (chondroitin ABC lyase) and EC 4.2.2.5 (chondroitin AC lyase) (EC 4.2.99.6 created 1965, deleted 1972)]
[EC 4.2.99.7 Transferred entry: now EC 4.2.3.2, ethanolamine-phosphate phospho-lyase (EC 4.2.99.7 created 1972, deleted 2000)]
[EC 4.2.99.8 Transferred entry: now EC 2.5.1.47, cysteine synthase (EC 4.2.99.8 created 1972, modified 1976, modified 1990, deleted 2002)]
[EC 4.2.99.9 Transferred entry: now EC 2.5.1.48, cystathionine γ-synthase (EC 4.2.99.9 created 1972, deleted 2002)]
[EC 4.2.99.10 Transferred entry: now EC 2.5.1.49, O-acetylhomoserine aminocarboxypropyltransferase (EC 4.2.99.10 created 1972, deleted 2002)]
[EC 4.2.99.11 Transferred entry: now EC 4.2.3.3, methylglyoxal synthase (EC 4.2.99.11 created 1972, deleted 2000)]
Accepted name: carboxymethyloxysuccinate lyase
Reaction: carboxymethyloxysuccinate = fumarate + glycolate
Other name(s): carbon-oxygen lyase; carboxymethyloxysuccinate glycolate-lyase
Systematic name: carboxymethyloxysuccinate glycolate-lyase (fumarate-forming)
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 53167-89-8
References:
1. Peterson, D. and Llaneza, J. Identification of a carbon-oxygen lyase activity cleaving the ether linkage in carboxymethyloxysuccinic acid. Arch. Biochem. Biophys. 162 (1974) 135-146. [PMID: 4831330]
[EC 4.2.99.13 Transferred entry: now EC 2.5.1.50, zeatin 9-aminocarboxyethyltransferase (EC 4.2.99.13 created 1984, deleted 2002)]
[EC 4.2.99.14 Transferred entry: now EC 2.5.1.51, β-pyrazolylalanine synthase (EC 4.2.99.14 created 1989 (EC 4.2.99.17 incorporated 1992), deleted 2002)]
[EC 4.2.99.15 Transferred entry: now EC 2.5.1.52, L-mimosine synthase (EC 4.2.99.15 created 1989, deleted 2002)]
[EC 4.2.99.16 Transferred entry: now EC 2.5.1.53, uracilylalanine synthase (EC 4.2.99.16 created 1990, deleted 2002)]
[EC 4.2.99.17 Deleted entry: listed as EC 4.2.99.14 β-pyrazolylalanine synthase (acetylserine) (EC 4.2.99.17 created 1992, deleted 1992)]
Accepted name: DNA-(apurinic or apyrimidinic site) lyase
Reaction: The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a β-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate
Other name(s): AP lyase; AP endonuclease class I; endodeoxyribonuclease (apurinic or apyrimidinic); deoxyribonuclease (apurinic or apyrimidinic); E. coli endonuclease III; phage-T4 UV endonuclease; Micrococcus luteus UV endonuclease; AP site-DNA 5'-phosphomonoester-lyase; X-ray endonuclease III
Systematic name: DNA-(apurinic or apyrimidinic site) 5'-phosphomonoester-lyase
Comments: 'Nicking' of the phosphodiester bond is due to a lyase-type reaction, not hydrolysis. This group of enzymes was previously listed as endonucleases, under EC 3.1.25.2.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 61811-29-8
References:
1. Bailly, V., Sente, B. and Verly, W.G. Bacteriophage-T4 and Micrococcus luteus UV endonucleases are not endonucleases but β-elimination and sometimes βδ-elimination catalysts. Biochem. J. 259 (1989) 751-759. [PMID: 2471512]
2. Bailly, V. and Verly, W.G. Escherichia coli endonuclease III is not an endonuclease but a β-elimination catalyst. Biochem. J. 242 (1987) 565-572. [PMID: 2439070]
3. Bailly, V. and Verly, W.G. AP endonucleases and AP lyases. Nucleic Acids Res. 17 (1989) 3617-3618. [PMID: 2471157]
4. Manoharan, M., Mazumder, A., Ransom, S.C., Gerlt, J.A. and Bolton, P.H. Mechanism of UV endonuclease-V cleavage of abasic sites in DNA determined by C-13 labeling. J. Am. Chem. Soc. 110 (1988) 2690-2691.
[EC 4.2.99.19 Transferred entry: Now EC 4.4.1.23, 2-hydroxypropyl-CoM lyase. The enzyme was incorrectly classified as acting on a C-O bond rather than a C-S bond (EC 4.2.99.19 created 2001, deleted 2005)]
Accepted name: 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase
Reaction: 5-enolpyruvoyl-6-hydroxy-2-succinylcyclohex-3-ene-1-carboxylate = (1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate + pyruvate
For diagram of reaction, click here.
Other name(s): 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylic acid synthase; 6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate synthase; SHCHC synthase; MenH; YfbB
Systematic name: 5-enolpyruvoyl-6-hydroxy-2-succinylcyclohex-3-ene-1-carboxylate pyruvate-lyase [(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate-forming)
Comments: 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 reactions carried out by this enzyme and EC 2.2.1.9, 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase, were carried out by a single enzyme but this has since been disproved [2].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 122007-88-9
References:
1. Jiang, M., Chen, X., Guo, Z.F., Cao, Y., Chen, M. and Guo, Z. Identification and characterization of (1R,6R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase in the menaquinone biosynthesis of Escherichia coli. Biochemistry 47 (2008) 3426-3434. [PMID: 18284213]
2. 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]
Accepted name: isochorismate lyase
Reaction: isochorismate = salicylate + pyruvate
Other name(s): salicylate biosynthesis protein pchB; pyochelin biosynthetic protein PchB; isochorismate pyruvate lyase
Systematic name: isochorismate pyruvate-lyase (salicylate-forming)
Comments: This enzyme is part of the pathway of salicylate formation from chorismate, and forms an integral part of pathways that produce salicylate-derived siderophores, such as pyochelin and yersiniabactin.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Serino, L., Reimmann, C., Baur, H., Beyeler, M., Visca, P. and Haas, D. Structural genes for salicylate biosynthesis from chorismate in Pseudomonas aeruginosa. Mol. Gen. Genet. 249 (1995) 217-228. [PMID: 7500944]
2. Kerbarh, O., Ciulli, A., Howard, N.I. and Abell, C. Salicylate biosynthesis: overexpression, purification, and characterization of Irp9, a bifunctional salicylate synthase from Yersinia enterocolitica. J. Bacteriol. 187 (2005) 5061-5066. [PMID: 16030197]