EC 2.3.2.16 lipid II:glycine glycyltransferase
EC 2.3.2.17 N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-glycyl)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase
EC 2.3.2.18 N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-triglycine)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase
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: a (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid
Other name(s): glutamyl transpeptidase; α-glutamyl transpeptidase; γ-glutamyl peptidyltransferase; γ-glutamyl transpeptidase (ambiguous); γ-GPT; γ-GT; γ-GTP; L-γ-glutamyl transpeptidase; L-γ-glutamyltransferase; L-glutamyltransferase; GGT (ambiguous); γ-glutamyltranspeptidase (ambiguous)
Systematic name: (5-L-glutamyl)-peptide:amino-acid 5-glutamyltransferase
Comments: The mammlian enzyme is part of the cell antioxidant defense mechanism. It initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracelular GSH levels. The protein also has EC 3.4.19.13 (glutathione hydrolase) activity [3-4]. The enzyme consists of two chains that are created by the proteolytic cleavage of a single precursor polypeptide. The N-terminal L-threonine of the C-terminal subunit functions as the active site for both the cleavage and the hydrolysis reactions [3-4].
Links to other databases: BRENDA, EXPASY, KEGG, PDB, 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. [PMID: 5698023]
3. Okada, T., Suzuki, H., Wada, K., Kumagai, H. and Fukuyama, K. Crystal structures of γ-glutamyltranspeptidase from Escherichia coli, a key enzyme in glutathione metabolism, and its reaction intermediate. Proc. Natl. Acad. Sci. USA 103 (2006) 6471-6476. [PMID: 16618936]
4. Boanca, G., Sand, A., Okada, T., Suzuki, H., Kumagai, H., Fukuyama, K. and Barycki, J.J. Autoprocessing of Helicobacter pylori γ-glutamyltranspeptidase leads to the formation of a threonine-threonine catalytic dyad. J. Biol. Chem. 282 (2007) 534-541. [PMID: 17107958]
5. Wickham, S., West, M.B., Cook, P.F. and Hanigan, M.H. Gamma-glutamyl compounds: substrate specificity of γ-glutamyl transpeptidase enzymes. Anal. Biochem. 414 (2011) 208-214. [PMID: 21447318]
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: The enzyme is a ribozyme. Two non-equivlant ribonucleoprotein subunits operate in non-concerted fashion in peptide elongation. The small subunit forms the mRNA-binding machinery and decoding center, the large subunit performs the main ribosomal catalytic function in the peptidyl-transferase center.
Links to other databases: BRENDA, EXPASY, KEGG, PDB, 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.
4. Voorhees, R.M., Weixlbaumer, A., Loakes, D., Kelley, A.C. and Ramakrishnan, V. Insights into substrate stabilization from snapshots of the peptidyl transferase center of the intact 70S ribosome. Nat. Struct. Mol. Biol. 16 (2009) 528-533. [PMID: 19363482]
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.
Accepted name: lipid II:glycine glycyltransferase
Reaction: N-acetylmuramoyl-L-alanyl-D-isoglutaminyl-L-lysyl-D-alanyl-D-alanine-diphospho-ditrans,octacis-undecaprenyl-N-acetylglucosamine + glycyl-tRNA = N-acetylmuramoyl-L-alanyl-D-isoglutaminyl-L-lysyl-(N6-glycyl)-D-alanyl-D-alanine-diphospho-ditrans,octacis-undecaprenyl-N-acetylglucosamine + tRNA
Other name(s): N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:N6-glycine transferase; femX (gene name)
Systematic name: alanyl-D-alanine-diphospho-ditrans,octacis-undecaprenyl-N-acetylglucosamine:glycine N6-glycyltransferase
Comments: The enzyme from Staphylococcus aureus catalyses the transfer of glycine from a charged tRNA to N-acetylmuramoyl-L-alanyl-D-isoglutaminyl-L-lysyl-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine (lipid II), attaching it to the N6 of the L-lysine at position 3 of the pentapeptide. This is the first step in the synthesis of the pentaglycine interpeptide bridge that is used in S. aureus for the crosslinking of different glycan strands to each other. Four additional glycine residues are subsequently attached by EC 2.3.2.17 (N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-glycyl)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase) and EC 2.3.2.18 (N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-triglycine)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase).
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Schneider, T., Senn, M.M., Berger-Bachi, B., Tossi, A., Sahl, H.G. and Wiedemann, I. In vitro assembly of a complete, pentaglycine interpeptide bridge containing cell wall precursor (lipid II-Gly5) of Staphylococcus aureus. Mol. Microbiol. 53 (2004) 675-685. [PMID: 15228543]
Accepted name: N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-glycyl)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase
Reaction: N-acetylmuramoyl-L-alanyl-D-isoglutaminyl-L-lysyl-(N6-glycyl)-D-alanyl-D-alanine-diphospho-ditrans,octacis-undecaprenyl-N-acetylglucosamine + 2 glycyl-tRNA = N-acetylmuramoyl-L-alanyl-D-isoglutaminyl-L-lysyl-(N6-triglycyl)-D-alanyl-D-alanine-diphospho-ditrans,octacis-undecaprenyl-N-acetylglucosamine + 2 tRNA
Other name(s): femA (gene name)
Systematic name: N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-glycyl)-D-alanyl-D-alanine-ditrans,octacis-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase
Comments: This enzyme catalyses the successive transfer of two glycine moieties from charged tRNAs to N-acetylmuramoyl-L-alanyl-D-isoglutaminyl-L-lysyl-(N6-glycyl)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine, attaching them to a glycine residue previously attached by EC 2.3.2.16 (lipid II:glycine glycyltransferase) to the N6 of the L-lysine at position 3 of the pentapeptide. This is the second step in the synthesis of the pentaglycine interpeptide bridge that is used by Staphylococcus aureus for the crosslinking of different glycan strands to each other. The next step is catalysed by EC 2.3.2.18 (FemB). This enzyme is essential for methicillin resistance [1].
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Berger-Bachi, B., Barberis-Maino, L., Strassle, A. and Kayser, F.H. FemA, a host-mediated factor essential for methicillin resistance in Staphylococcus aureus: molecular cloning and characterization. Mol. Gen. Genet. 219 (1989) 263-269. [PMID: 2559314]
2. Johnson, S., Kruger, D. and Labischinski, H. FemA of Staphylococcus aureus: isolation and immunodetection. FEMS Microbiol. Lett. 132 (1995) 221-228. [PMID: 7590176]
3. Benson, T.E., Prince, D.B., Mutchler, V.T., Curry, K.A., Ho, A.M., Sarver, R.W., Hagadorn, J.C., Choi, G.H. and Garlick, R.L. X-ray crystal structure of Staphylococcus aureus FemA. Structure 10 (2002) 1107-1115. [PMID: 12176388]
4. Schneider, T., Senn, M.M., Berger-Bachi, B., Tossi, A., Sahl, H.G. and Wiedemann, I. In vitro assembly of a complete, pentaglycine interpeptide bridge containing cell wall precursor (lipid II-Gly5) of Staphylococcus aureus. Mol. Microbiol. 53 (2004) 675-685. [PMID: 15228543]
Accepted name: N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-triglycine)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase
Reaction: N-acetylmuramoyl-L-alanyl-D-isoglutaminyl-L-lysyl-(N6-triglycyl)-D-alanyl-D-alanine-diphospho-ditrans,octacis-undecaprenyl-N-acetylglucosamine + 2 glycyl-tRNA = N-acetylmuramoyl-L-alanyl-D-isoglutaminyl-L-lysyl-(N6-pentaglycyl)-D-alanyl-D-alanine-diphospho-ditrans,octacis-undecaprenyl-N-acetylglucosamine + 2 tRNA
Other name(s): femB (gene name)
Systematic name: N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-triglycine)-D-alanyl-D-alanine-ditrans,octacis-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase
Comments: This Staphylococcus aureus enzyme catalyses the successive transfer of two glycine moieties from charged tRNAs to N-acetylmuramoyl-L-alanyl-D-isoglutaminyl-L-lysyl-(N6-triglycyl)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine, attaching them to the three glycine molecules that were previously attached to the N6 of the L-lysine at position 3 of the pentapeptide by EC 2.3.2.16 (lipid II:glycine glycyltransferase) and EC 2.3.2.17 (N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-glycyl)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase). This is the last step in the synthesis of the pentaglycine interpeptide bridge that is used in this organism for the crosslinking of different glycan strands to each other.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Ehlert, K., Schroder, W. and Labischinski, H. Specificities of FemA and FemB for different glycine residues: FemB cannot substitute for FemA in staphylococcal peptidoglycan pentaglycine side chain formation. J. Bacteriol. 179 (1997) 7573-7576. [PMID: 9393725]
2. Rohrer, S. and Berger-Bachi, B. Application of a bacterial two-hybrid system for the analysis of protein-protein interactions between FemABX family proteins. Microbiology 149 (2003) 2733-2738. [PMID: 14523106]
3. Schneider, T., Senn, M.M., Berger-Bachi, B., Tossi, A., Sahl, H.G. and Wiedemann, I. In vitro assembly of a complete, pentaglycine interpeptide bridge containing cell wall precursor (lipid II-Gly5) of Staphylococcus aureus. Mol. Microbiol. 53 (2004) 675-685. [PMID: 15228543]