UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diamino-pimelate ligase

Search
PMC	articles
PubMed	articles
NCBI	proteins

UDP-N-acetylmuramoyl-L-alanyl-D-glutamate—2,6-diaminopimelate ligase
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate—2,6-diaminopimelate ligase
Identifiers
EC no.	6.3.2.13
CAS no.	2620865
Databases
BRENDA	enzyme data
ExPASy	NiceZyme view
KEGG	enzyme entry
MetaCyc	metabolic pathway
Rhea	reactions
PDB structures	RCSB PDB PDBe PDBsum
PMC
Search
PMC	articles
PubMed	articles
NCBI	proteins

UDP-N-acetylmuramoyl-L-alanyl-D-glutamate—2,6-diaminopimelate ligase (EC 6.3.2.13, MurE synthetase, UDP-N-acetylmuramoyl-L-alanyl-D-glutamate:meso-2,6-diamino-heptanedioate ligase (ADP-forming), UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelate synthetase, UDP-N-acetylmuramoylalanyl-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

ATP + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate + meso-2,6-diaminoheptanedioate

\rightleftharpoons

ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-meso-2,6-diaminoheptanedioate

This enzyme takes part in synthesis of a cell-wall peptide.

References

↑ Mizuno Y, Ito E (May 1968). "Purification and properties of uridine diphosphate N-acetylmuramyl-L-alanyl-D-glutamate:meso-2,6-diaminopimelate ligase". The Journal of Biological Chemistry. 243 (10): 2665–72. doi:10.1016/S0021-9258(18)93424-1. PMID 4967958.
↑ van Heijenoort J (October 2001). "Recent advances in the formation of the bacterial peptidoglycan monomer unit". Natural Product Reports. 18 (5): 503–19. doi:10.1039/a804532a. PMID 11699883.

External links

UDP-N-acetylmuramoyl-L-alanyl-D-glutamate—2,6-diaminopimelate+ligase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

[1] Mizuno Y, Ito E (May 1968). "Purification and properties of uridine diphosphate N-acetylmuramyl-L-alanyl-D-glutamate:meso-2,6-diaminopimelate ligase". The Journal of Biological Chemistry. 243 (10): 2665–72. doi:10.1016/S0021-9258(18)93424-1. PMID 4967958.

[2] van Heijenoort J (October 2001). "Recent advances in the formation of the bacterial peptidoglycan monomer unit". Natural Product Reports. 18 (5): 503–19. doi:10.1039/a804532a. PMID 11699883.

v t e Enzymes: CO CS and CN ligases (EC 6.1-6.3)
6.1: Carbon-Oxygen	Aminoacyl tRNA synthetase Alanine Arginine Asparagine Aspartate Cysteine D-Alanine—poly(phosphoribitol) ligase Glutamate Glutamine Glycine Histidine Isoleucine Leucine Lysine Methionine Phenylalanine Proline Serine Threonine Tryptophan Tyrosine Valine
6.2: Carbon-Sulfur	(2,2,3-trimethyl-5-oxocyclopent-3-enyl)acetyl-CoA synthase 2-furoate—CoA ligase 3-alpha,7-alpha-dihydroxy-5-beta-cholestanate—CoA ligase 3-hydroxybenzoate—CoA ligase 3-hydroxypropionyl-CoA synthase 4-chlorobenzoate—CoA ligase 4-Coumarate-CoA ligase 4-hydroxybenzoate—CoA ligase 6-carboxyhexanoate—CoA ligase Acetate—ACP ligase Acetate—CoA ligase (ADP-forming) Acetoacetate—CoA ligase Acetyl—CoA synthetase Acid—CoA ligase (GDP-forming) Anthranilate—CoA ligase Arachidonate—CoA ligase Benzoate—CoA ligase Biotin—CoA ligase (butirosin acyl-carrier protein)—L-glutamate ligase Butyrate—CoA ligase Cholate—CoA ligase Citrate—CoA ligase (citrate (pro-3S)-lyase) ligase Dicarboxylate—CoA ligase Glutarate—CoA ligase Long-chain-fatty-acid—ACP ligase Long-chain-fatty-acid—CoA ligase Malate—CoA ligase Malonate—CoA ligase o-Succinylbenzoate—CoA ligase Oxalate—CoA ligase Phenylacetate—CoA ligase Phytanate—CoA ligase Propionate—CoA ligase Succinate—CoA ligase (ADP-forming) Succinate—CoA ligase (GDP-forming) Succinyl—CoA synthetase trans-Feruloyl—CoA synthase
6.3: Carbon-Nitrogen	Glutamine synthetase Ubiquitin ligase Cullin Von Hippel–Lindau tumor suppressor UBE3A Mdm2 Anaphase-promoting complex UBR1 Glutathione synthetase CTP synthetase Adenylosuccinate synthase Argininosuccinate synthase Holocarboxylase synthetase GMP synthase Asparagine synthetase Carbamoyl phosphate synthetase I II Glutamate–cysteine ligase

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)