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

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N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-glycyl)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase
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EC no. 2.3.2.17
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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.

Related Research Articles

<i>N</i>-Acetylmuramic acid Chemical compound

N-Acetylmuramic acid is an organic compound with the chemical formula C
11H
19NO
8. It is a monomer of peptidoglycan in most bacterial cell walls, which is built from alternating units of N-acetylglucosamine (GlcNAc) and N-acetylmuramic acid, cross-linked by oligopeptides at the lactic acid residue of MurNAc.

<span class="mw-page-title-main">Glycine—tRNA ligase</span> Protein-coding gene in the species Homo sapiens

Glycine—tRNA ligase also known as glycyl–tRNA synthetase is an enzyme that in humans is encoded by the GARS1 gene.

In enzymology, a UDP-N-acetylmuramoyl-L-alanine—D-glutamate ligase is an enzyme that catalyzes the chemical reaction

In enzymology, a UDP-N-acetylmuramoyl-L-alanyl-D-glutamate—L-lysine ligase is an enzyme that catalyzes the chemical reaction

In enzymology, a UDP-N-acetylmuramoyl-tripeptide—D-alanyl-D-alanine ligase is an enzyme that catalyzes the chemical reaction

In enzymology, an UDP-N-acetylmuramoylpentapeptide-lysine N6-alanyltransferase (EC 2.3.2.10) is an enzyme that catalyzes the chemical reaction

Lipid II:glycine glycyltransferase (EC 2.3.2.16, N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:N6-glycine transferase, femX (gene)) is an enzyme with systematic name alanyl-D-alanine-diphospho-ditrans, octacis-undecaprenyl-N-acetylglucosamine:glycine N6-glycyltransferase. This enzyme catalyses the following chemical reaction

N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-triglycine)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase (EC 2.3.2.18, femB (gene)) is an enzyme with systematic name N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-triglycine)-D-alanyl-D-alanine-ditrans,octacis-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase. This enzyme catalyses the following chemical reaction

FEMB may refer to:

GlcA-beta-(1->2)-D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphospho-ditrans,octacis-undecaprenol 4-beta-mannosyltransferase is an enzyme with systematic name GDP-mannose:GlcA-beta-(1->2)-D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphospho-ditrans,octacis-undecaprenol 4-beta-mannosyltransferase. This enzyme catalyses the following chemical reaction

GDP-mannose:cellobiosyl-diphosphopolyprenol alpha-mannosyltransferase is an enzyme with systematic name GDP-mannose:D-Glc-beta-(1->4)-Glc-alpha-1-diphospho-ditrans,octacis-undecaprenol 3-alpha-mannosyltransferase . This enzyme catalyses the following chemical reaction

Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase is an enzyme with systematic name UDP-4-amino-4-deoxy-alpha-L-arabinose:ditrans,octacis-undecaprenyl phosphate 4-amino-4-deoxy-alpha-L-arabinosyltransferase. This enzyme catalyses the following chemical reaction

Undecaprenyl-phosphate glucose phosphotransferase is an enzyme with systematic name UDP-glucose:ditrans,octacis-undecaprenyl-phosphate glucose phosphotransferase. This enzyme catalyses the following chemical reaction

UDP-N-acetylglucosamine—undecaprenyl-phosphate N-acetylglucosaminephosphotransferase is an enzyme with systematic name UDP-N-acetyl-alpha-D-glucosamine:ditrans,octacis-undecaprenyl phosphate N-acetyl-alpha-D-glucosaminephosphotransferase. This enzyme catalyses the following chemical reaction

UDP-N-acetylglucosamine---decaprenyl-phosphate N-acetylglucosaminephosphotransferase is an enzyme with systematic name UDP-N-acetyl-alpha-D-glucosamine:trans,octacis-decaprenyl-phosphate N-acetylglucosaminephosphotransferase. This enzyme catalyses the following chemical reaction

Muramoylpentapeptide carboxypeptidase is an enzyme. This enzyme catalyses the following chemical reaction.

UDP-N-acetylmuramoyl-L-alanyl-D-glutamate—2,6-diaminopimelate ligase is an enzyme with systematic name UDP-N-acetylmuramoyl-L-alanyl-D-glutamate:meso-2,6-diaminoheptanedioate gamma-ligase (ADP-forming). This enzyme catalyses the following chemical reaction

UDP-N-acetylmuramoyl-L-alanyl-D-glutamate—D-lysine ligase is an enzyme with systematic name UDP-N-acetylmuramoyl-L-alanyl-D-glutamate:D-lysine alpha-ligase (ADP-forming). This enzyme catalyses the following chemical reaction

<span class="mw-page-title-main">Methyltransferase/kinase WbdD</span>

Methyltransferase/kinase WbdD EC 2.1.1.294 and EC 2.7.1.181WbdD is a bifunctional enzyme that regulates the length of the LPS O-antigen polysaccharide chain. Stops the polymerization of the chain by phosphorylating and then methylating the phosphate on the terminal sugar. This terminal modification is essential for export of the O-antigen across the inner membrane. WbdD is also required for correct localization of the WbdA mannosyltransferase.

References

  1. ↑ 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.
  2. ↑ 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.
  3. ↑ 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.
  4. ↑ 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.
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