N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-glycyl)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase

N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N⁶-glycyl)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase (EC 2.3.2.17, femA (gene)) is an enzyme with systematic name N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N⁶-glycyl)-D-alanyl-D-alanine-ditrans,octacis-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase.^[1]^[2]^[3]^[4] This enzyme catalyses the following chemical reaction

N-acetylmuramoyl-L-alanyl-D-isoglutaminyl-L-lysyl-(N⁶-glycyl)-D-alanyl-D-alanine-diphospho-ditrans,octacis-undecaprenyl-N-acetylglucosamine + 2 glycyl-tRNA

\rightleftharpoons

N-acetylmuramoyl-L-alanyl-D-isoglutaminyl-L-lysyl-(N⁶-triglycyl)-D-alanyl-D-alanine-diphospho-ditrans,octacis-undecaprenyl-N-acetylglucosamine + 2 tRNA

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.

References

↑ Berger-Bachi, B., Barberis-Maino, L., Strassle, A. and Kayser, F.H. (1989). "FemA, a host-mediated factor essential for methicillin resistance in Staphylococcus aureus: molecular cloning and characterization". Mol. Gen. Genet. 219: 263–269. doi:10.1007/bf00261186. PMID 2559314.
↑ Johnson, S., Kruger, D. and Labischinski, H. (1995). "FemA of Staphylococcus aureus: isolation and immunodetection". FEMS Microbiol. Lett. 132: 221–228. doi:10.1111/j.1574-6968.1995.tb07837.x. PMID 7590176.
↑ 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. (2002). "X-ray crystal structure of Staphylococcus aureus FemA". Structure 10: 1107–1115. doi:10.1016/s0969-2126(02)00807-9. PMID 12176388.
↑ Schneider, T., Senn, M.M., Berger-Bachi, B., Tossi, A., Sahl, H.G. and Wiedemann, I. (2004). "In vitro assembly of a complete, pentaglycine interpeptide bridge containing cell wall precursor (lipid II-Gly₅) of Staphylococcus aureus". Mol. Microbiol. 53: 675–685. doi:10.1111/j.1365-2958.2004.04149.x. PMID 15228543.

External links

N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-glycyl)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase at the US National Library of Medicine Medical Subject Headings (MeSH)

Transferases: acyltransferases (EC 2.3)

2.3.1: other than amino-acyl groups	acetyltransferases: Acetyl-Coenzyme A acetyltransferase N-Acetylglutamate synthase Choline acetyltransferase Dihydrolipoyl transacetylase Acetyl-CoA C-acyltransferase Beta-galactoside transacetylase Chloramphenicol acetyltransferase N-acetyltransferase Serotonin N-acetyl transferase HGSNAT ARD1A Histone acetyltransferase P300/CBP NAT2 palmitoyltransferases: Carnitine O-palmitoyltransferase CPT1 CPT2 Serine C-palmitoyltransferase SPTLC1 SPTLC2 other: Acyltransferase like 2 Aminolevulinic acid synthase Beta-ketoacyl-ACP synthase Glyceronephosphate O-acyltransferase Lecithin—cholesterol acyltransferase Glycerol-3-phosphate O-acyltransferase 1-acylglycerol-3-phosphate O-acyltransferase 2-acylglycerol-3-phosphate O-acyltransferase ABHD5

2.3.2: Aminoacyltransferases	Gamma-glutamyl transpeptidase Peptidyl transferase Transglutaminase Tissue transglutaminase Keratinocyte transglutaminase Factor XIII

2.3.3: converted into alkyl on transfer	Citrate synthase ATP citrate lyase HMG-CoA synthase Malate synthase

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

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