D-alanine—D-alanine ligase

This enzyme belongs to the family of ATP-grasp ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases (peptide synthases). The systematic name of this enzyme class is D-alanine:D-alanine ligase (ADP-forming). Other names in common use include alanine:alanine ligase (ADP-forming), and alanylalanine synthetase. This enzyme participates in d-alanine metabolism and peptidoglycan biosynthesis. Phosphinate and D-cycloserine are known to inhibit this enzyme.

The N-terminal region of the D-alanine—D-alanine ligase is thought to be involved in substrate binding, while the C-terminus is thought to be a catalytic domain.

Structural studies

As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes 1EHI, 1IOV, 1IOW, 2DLN, 2FB9, 2I80, 2I87, and 2I8C.

References

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 domain Pfam and InterPro: IPR011127

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	Succinyl coenzyme A synthetase Acetyl—CoA synthetase Long-chain-fatty-acid—CoA ligase
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)

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Structural studies

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