Accepted name: D-glutamyltransferase
Reaction: L(or D)-glutamine + D-glutamyl-peptide = NH3 + 5-glutamyl-D-glutamyl-peptide
Other name(s): D-glutamyl transpeptidase; D-γ-glutamyl transpeptidase
Systematic name: glutamine:D-glutamyl-peptide 5-glutamyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 9030-02-8
References:
1. Williams, W.J., Litwin, J. and Thorne, C.B. Further studies on the biosynthesis of γ-glutamyl peptides by transfer reactions. J. Biol. Chem. 212 (1955) 427-438.
Accepted name: γ-glutamyltransferase
Reaction: (5-L-glutamyl)-peptide + an amino acid = peptide + 5-L-glutamyl amino acid
Other name(s): glutamyl transpeptidase; α-glutamyl transpeptidase; γ-glutamyl peptidyltransferase; γ-glutamyl transpeptidase; γ-GPT; γ-GT; γ-GTP; L-γ-glutamyl transpeptidase; L-γ-glutamyltransferase; L-glutamyltransferase
Systematic name: (5-L-glutamyl)-peptide:amino-acid 5-glutamyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 9046-27-9
References:
1. Goore, M.Y. and Thompson, J.F. γ-Glutamyl transpeptidase from kidney bean fruit. I. Purification and mechanism of action. Biochim. Biophys. Acta 132 (1967) 15-26. [PMID: 6030345]
2. Leibach, F.H. and Binkley, F. γ-Glutamyl transferase of swine kidney. Arch. Biochem. Biophys. 127 (1968) 292-301.
Accepted name: lysyltransferase
Reaction: L-lysyl-tRNA + phosphatidylglycerol = tRNA + 3-phosphatidyl-1'-(3'-O-L-lysyl)glycerol
Systematic name: L-lysyl-tRNA:phosphatidylglycerol 3-O-lysyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 37257-20-8
References:
1. Lennarz, W.J., Bonsen, P.P.M. and van Deenan, L.L.M. Substrate specificity of O-L-lysylphosphatidylglycerol synthetase. Enzymatic studies on the structure of O-L-lysylphosphatidylglycerol. Biochemistry 6 (1967) 2307-2312. [PMID: 6049461]
Accepted name: γ-glutamylcyclotransferase
Reaction: (&gmma;-L-glutamyl)-L-amino acid = 5-oxoproline + L-amino acid
Other name(s): γ-glutamyl-amino acid cyclotransferase; γ-L-glutamylcyclotransferase; L-glutamic cyclase; (5-L-glutamyl)-L-amino-acid 5-glutamyltransferase (cyclizing)
Systematic name: (γ-L-glutamyl)-L-amino-acid γ-glutamyltransferase (cyclizing)
Comments: The enzyme acts on derivatives of L-glutamate, L-2-aminobutanoate, L-alanine and glycine.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 9045-44-7
References:
1. Bodnaryk, R.P. and McGirr, L. Purification, properties and function of a unique γ-glutamyl cyclotransferase from the housefly, Musca domestica L. Biochim. Biophys. Acta 315 (1973) 352-362.
2. Orlowski, M., Richman, P.G. and Meister, A. Isolation and properties of γ-L-glutamylcyclotransferase from human brain. Biochemistry 8 (1969) 1048-1055. [PMID: 5781001]
Accepted name: glutaminyl-peptide cyclotransferase
Reaction: L-glutaminyl-peptide = 5-oxoprolyl-peptide + NH3
Other name(s): glutaminyl-tRNA cyclotransferase; glutaminyl cyclase; glutaminyl-transfer ribonucleate cyclotransferase
Systematic name: L-glutaminyl-peptide γ-glutamyltransferase (cyclizing)
Comments: Involved in the formation of thyrotropin-releasing hormone and other biologically active peptides containing N-terminal pyroglutamyl residues. The enzyme from papaya also acts on glutaminyl-tRNA.
Links to other databases: BRENDA, EXPASY, KEGG, PDB, CAS registry number: 37257-21-9
References:
1. Busby, W.H., Quackenbush, G.E., Humm, J., Youngblood, W.W. and Kizer, J.S. An enzyme(s) that converts glutaminyl-peptides into pyroglutamyl-peptides. Presence in pituitary, brain, adrenal medulla, and lymphocytes. J. Biol. Chem. 262 (1987) 8532-8536. [PMID: 3597387]
2. Fischer, W.H. and Spiess, J. Identification of a mammalian glutaminyl cyclase converting glutaminyl into pyroglutamyl peptides. Proc. Natl. Acad. Sci. USA 84 (1987) 3628-3632. [PMID: 3473473]
3. Messer, M. and Ottesen, M. Isolation and properties of glutamine cyclotransferase of dried papaya latex. C.R. Trav. Lab. Carlsberg 35 (1965) 1-24.
Accepted name: leucyltransferase
Reaction: L-leucyl-tRNA + protein = tRNA + L-leucyl-protein
Other name(s): leucyl, phenylalanine-tRNA-protein transferase; leucyl-phenylalanine-transfer ribonucleate-protein aminoacyltransferase; leucyl-phenylalanine-transfer ribonucleate-protein transferase
Systematic name: L-leucyl-tRNA:protein leucyltransferase
Comments: Also transfers phenylalanyl groups. Requires a univalent cation. Peptides and proteins containing an N-terminal arginine, lysine or histidine residue can act as acceptors.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 37257-22-0
References:
1. Leibowitz, M.J. and Soffer, R.L. A soluble enzyme from Escherichia coli which catalyzes the transfer of leucine and phenylalanine from tRNA to acceptor proteins. Biochem. Biophys. Res. Commun. 36 (1969) 47-53. [PMID: 4894363]
2. Leibowitz, M.J. and Soffer, R.L. Enzymatic modification of proteins. 3. Purification and properties of a leucyl, phenylalanyl transfer ribonucleic acid protein transferase from Escherichia coli. J. Biol. Chem. 245 (1970) 2066-2073. [PMID: 4909560]
3. Soffer, R.L. Peptide acceptors in the leucine, phenylalanine transfer reaction. J. Biol. Chem. 248 (1973) 8424-8428. [PMID: 4587124]
Accepted name: aspartyltransferase
Reaction: L-asparagine + hydroxylamine = NH3 + β-L-aspartylhydroxamate
Other name(s): β-aspartyl transferase; aspartotransferase
Systematic name: L-asparagine:hydroxylamine γ-aspartyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 37257-23-1
References:
1. Jayaram, H.N., Ramakrishnan, T. and Vaidyanathan, C.S. Aspartotransferase from Mycobacterium tuberculosis H37Ra. Indian J. Biochem. 6 (1969) 106-110.
Accepted name: arginyltransferase
Reaction: L-arginyl-tRNA + protein = tRNA + L-arginyl-protein
Other name(s): arginine transferase; arginyl-transfer ribonucleate-protein aminoacyltransferase; arginyl-transfer ribonucleate-protein transferase; arginyl-tRNA protein transferase
Systematic name: L-arginyl-tRNA:protein arginyltransferase
Comments: Requires mercaptoethanol and a univalent cation. Peptides and proteins containing an N-terminal glutamate, aspartate or cystine residue can act as acceptors.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 37257-24-2
References:
1. Soffer, R.L. Enzymatic modification of proteins. II. Purification and properties of the arginyl transfer ribonucleic acid-protein transferase from rabbit liver cytoplasm. J. Biol. Chem. 245 (1970) 731-737. [PMID: 5416661]
2. Soffer, R.L. Peptide acceptors in the arginine transfer reaction. J. Biol. Chem. 248 (1973) 2918-2921. [PMID: 4572514]
3. Soffer, R.L. and Horinishi, H. Enzymic modification of proteins. I. General characteristics of the arginine-transfer reaction in rabbit liver cytoplasm. J. Mol. Biol. 43 (1969) 163-175. [PMID: 5811819]
Accepted name: agaritine γ-glutamyltransferase
Reaction: agaritine + acceptor = 4-hydroxymethylphenylhydrazine + γ-L-glutamyl-acceptor
Other name(s): (γ-L-glutamyl)-N1-(4-hydroxymethylphenyl)hydrazine:(acceptor) γ-glutamyltransferase
Systematic name: (γ-L-glutamyl)-N1-(4-hydroxymethylphenyl)hydrazine:acceptor γ-glutamyltransferase
Comments: 4-Hydroxyaniline, cyclohexylamine, 1-naphthylhydrazine and similar compounds can act as acceptors; the enzyme also catalyses the hydrolysis of agaritine.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 37257-25-3
References:
1. Gigliotti, H.J. and Levenberg, B. Studies on the γ-glutamyltransferase of Agaricus bisporus. J. Biol. Chem. 239 (1964) 2274-2284.
Accepted name: UDP-N-acetylmuramoylpentapeptide-lysine N6-alanyltransferase
Reaction: L-alanyl-tRNA + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine = tRNA + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-N6-(L-alanyl)-L-lysyl-D-alanyl-D-alanine
Other name(s): alanyl-transfer ribonucleate-uridine diphosphoacetylmuramoylpentapeptide transferase; UDP-N-acetylmuramoylpentapeptide lysine N6-alanyltransferase; uridine diphosphoacetylmuramoylpentapeptide lysine N6-alanyltransferase
Systematic name: L-alanyl-tRNA:UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine N6-alanyltransferase
Comments: Also acts on L-seryl-tRNA.
Links to other databases: BRENDA, EXPASY, KEGG, PDB, CAS registry number: 37257-26-4
References:
1. Plapp, R. and Strominger, J.L. Biosynthesis of the peptidoglycan of bacterial cell walls. 18. Purification and properties of L-alanyl transfer ribonucleic acid-uridine diphosphate-N-acetylmuramyl-pentapeptide transferase from Lactobacillus viridescens. J. Biol. Chem. 245 (1970) 3675-3682. [PMID: 4248527]
Accepted name: alanylphosphatidylglycerol synthase
Reaction: L-alanyl-tRNA + phosphatidylglycerol = tRNA + 3-O-L-alanyl-1-O-phosphatidylglycerol
Other name(s): O-alanylphosphatidylglycerol synthase; alanyl phosphatidylglycerol synthetase
Systematic name: L-alanyl-tRNA:phosphatidylglycerol alanyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 37257-27-5
References:
1. Gould, R.M., Thornton, M.P., Liepkalns, V. and Lennarz, W.J. Participation of aminoacyl transfer ribonucleic acid in aminoacyl phosphatidylglycerol synthesis. II. Specificity of alanyl phosphatidylglycerol synthetase. J. Biol. Chem. 243 (1968) 3096-3104.
Accepted name: peptidyltransferase
Reaction: peptidyl-tRNA1 + aminoacyl-tRNA2 = tRNA1 + peptidyl(aminoacyl-tRNA2)
Other name(s): transpeptidase; ribosomal peptidyltransferase
Systematic name: peptidyl-tRNA:aminoacyl-tRNA N-peptidyltransferase
Comments: An enzyme found in ribosomes.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 9059-29-4
References:
1. Rychlik, I. Release of lysine peptides by puromycin from polylysyl-transfer ribonucleic acid in the presence of ribosomes. Biochim. Biophys. Acta 114 (1966) 425-427. [PMID: 5329275]
2. Rychlik, I., Cerná, J., Chládek, S., Zemlicka, J. and Haladová, Z. Substrate specificity of ribosomal peptidyl transferase: 2'(3')-O-aminoacyl nucleosides as acceptors of the peptide chain on the amino acid site. J. Mol. Biol. 43 (1969) 13-24. [PMID: 4897787]
3. Traut, R.R. and Monro, R.E. The puromycin reaction and its relation to protein synthesis. J. Mol. Biol. 10 (1964) 63-72.
Accepted name: protein-glutamine γ-glutamyltransferase
Reaction: protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
Other name(s): transglutaminase; Factor XIIIa; fibrinoligase; fibrin stabilizing factor; glutaminylpeptide γ-glutamyltransferase; polyamine transglutaminase; tissue transglutaminase; R-glutaminyl-peptide:amine γ-glutamyl transferase
Systematic name: protein-glutamine:amine γ-glutamyltransferase
Comments: Requires Ca2+. The γ-carboxamide groups of peptide-bound glutamine residues act as acyl donors, and the 6-amino-groups of protein- and peptide-bound lysine residues act as acceptors, to give intra- and inter-molecular N6-(5-glutamyl)-lysine crosslinks. Formed by proteolytic cleavage from plasma Factor XIII
Links to other databases: BRENDA, EXPASY, KEGG, PDB, CAS registry number: 80146-85-6
References:
1. Folk, J.E. and Chung, S.I. Molecular and catalytic properties of transglutaminases. Adv. Enzymol. Relat. Areas Mol. Biol. 38 (1973) 109-191. [PMID: 4151471]
2. Folk, J.E. and Cole, P.W. Mechanism of action of guinea pig liver transglutaminase. I. Purification and properties of the enzyme: identification of a functional cysteine essential for activity. J. Biol. Chem. 241 (1966) 5518-5525. [PMID: 5928192]
3. Folk, J.E. and Finlayson, J.S.The ε-γ-(glutamyl)lysine crosslink and the catalytic role of transglutaminases. Adv. Protein Chem. 31 (1977) 1-133. [PMID: 73346]
4. Takahashi, N., Takahashi, Y. and Putnam, F.W. Primary structure of blood coagulation factor XIIIa (fibrinoligase, transglutaminase) from human placenta. Proc. Natl. Acad. Sci. USA 83 (1986) 8019-8023. [PMID: 2877456]
Accepted name: D-alanine γ-glutamyltransferase
Reaction: L-glutamine + D-alanine = NH3 + γ-L-glutamyl-D-alanine
Systematic name: L-glutamine:D-alanine γ-glutamyltransferase
Comments: D-Phenylalanine and D-2-aminobutyrate can also act as acceptors, but more slowly. The enzyme also catalyses some of the reactions of EC 2.3.2.2 (γ-glutamyltransferase).
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 9046-27-9
References:
1. Kawasaki, Y., Ogawa, T. and Sasaoka, K. Occurrence and some properties of a novel γ-glutamyltransferase responsible for the synthesis of γ-L-glutamyl-D-alanine in pea-seedlings. Biochim. Biophys. Acta 716 (1982) 194-200.
Accepted name: glutathione γ-glutamylcysteinyltransferase
Reaction: glutathione + [Glu(-Cys)]n-Gly = Gly + [Glu(-Cys)]n+1-Gly
Other name(s): phytochelatin synthase; γ-glutamylcysteine dipeptidyl transpeptidase
Systematic name: glutathione:poly(4-glutamyl-cysteinyl)glycine 4-glutamylcysteinyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 125390-02-5
References:
1. Grill, E., Löffler, S., Winnacker, E.-L. and Zenk, M.H. Phytochelatins, the heavy-metal-binding peptides of plants, are synthesized from glutathione by a specific γ-glutamylcysteine dipeptidyl transpeptidase (phytochelatin synthase). Proc. Natl. Acad. Sci. USA 86 (1989) 6838-6842.