N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-glycyl)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase
(Redirected from FEMA (gene))
| N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-glycyl)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase | |||||||||
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| Identifiers | |||||||||
| EC no. | 2.3.2.17 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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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 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
[edit]- ^ Berger-Bächi B, Barberis-Maino L, Strässle A, Kayser FH (October 1989). "FemA, a host-mediated factor essential for methicillin resistance in Staphylococcus aureus: molecular cloning and characterization". Molecular & General Genetics. 219 (1–2): 263–9. doi:10.1007/bf00261186. PMID 2559314.
- ^ Johnson S, Krüger D, Labischinski H (October 1995). "FemA of Staphylococcus aureus: isolation and immunodetection". FEMS Microbiology Letters. 132 (3): 221–8. doi:10.1111/j.1574-6968.1995.tb07837.x. PMID 7590176.
- ^ Benson TE, Prince DB, Mutchler VT, Curry KA, Ho AM, Sarver RW, Hagadorn JC, Choi GH, Garlick RL (August 2002). "X-ray crystal structure of Staphylococcus aureus FemA". Structure. 10 (8): 1107–15. doi:10.1016/s0969-2126(02)00807-9. PMID 12176388.
- ^ Schneider T, Senn MM, Berger-Bächi B, Tossi A, Sahl HG, Wiedemann I (July 2004). "In vitro assembly of a complete, pentaglycine interpeptide bridge containing cell wall precursor (lipid II-Gly5) of Staphylococcus aureus". Molecular Microbiology. 53 (2): 675–85. doi:10.1111/j.1365-2958.2004.04149.x. PMID 15228543.
External links
[edit]- N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-glycyl)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine+glycyltransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
