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This enzyme belongs to the family ofATP-grasp ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases (peptide synthases). Thesystematic name of this enzyme class isD-alanine:D-alanine ligase (ADP-forming). Other names in common use includealanine:alanine ligase (ADP-forming), andalanylalanine synthetase. This enzyme participates ind-alanine metabolism andpeptidoglycan biosynthesis.Phosphinate andD-cycloserine are known toinhibit this enzyme.

The N-terminal region of the D-alanine—D-alanine ligase is thought to be involved insubstrate binding, while the C-terminus is thought to be acatalytic domain.^[1]

Structural studies

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As of late 2007, 8structures have been solved for this class of enzymes, withPDB accession codes1IOV,1IOW,2DLN,2FB9,2I80,2I87, and2I8C.

References

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^Roper DI, Huyton T, Vagin A, Dodson G (August 2000)."The molecular basis of vancomycin resistance in clinically relevant Enterococci: crystal structure of D-alanyl-D-lactate ligase (VanA)".Proc. Natl. Acad. Sci. U.S.A.97 (16):8921–5.Bibcode:2000PNAS...97.8921R.doi:10.1073/pnas.150116497.PMC 16797.PMID 10908650.

Ito, E; Strominger JL (1962)."Enzymatic synthesis of the peptide in bacterial uridine nucleotides II. Enzymatic synthesis and addition of D-alanyl-D-alanine".J. Biol. Chem.237:2696–2703.doi:10.1016/S0021-9258(19)73809-5.
Neuhaus FC (1962). "Kinetic studies on D-Ala-D-Ala synthetase".Fed. Proc.21: 229.
van Heijenoort J (2001). "Recent advances in the formation of the bacterial peptidoglycan monomer unit".Nat. Prod. Rep.18 (5):503–19.doi:10.1039/a804532a.PMID 11699883.

This article incorporates text from the public domainPfam andInterPro:IPR011127

v t e Enzymes: CO CS and CNligases (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	EC1Oxidoreductases (list) EC2Transferases (list) EC3Hydrolases (list) EC4Lyases (list) EC5Isomerases (list) EC6Ligases (list) EC7Translocases (list)

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