D-alanine—D-alanine ligase

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D-alanine—D-alanine ligase
Identifiers
EC no.6.3.2.4
CAS no.9023-63-6
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
D-ala D-ala ligase N-terminus
PDB 1iow EBI.jpg
complex of y216f d-ala:d-ala ligase with adp and a phosphoryl phosphinate
Identifiers
SymbolDala_Dala_lig_N
PfamPF01820
InterProIPR011127
SCOP22dln / SCOPe / SUPFAM
D-ala D-ala ligase C-terminus
PDB 1iow EBI.jpg
complex of y216f d-ala:d-ala ligase with adp and a phosphoryl phosphinate
Identifiers
SymbolDala_Dala_lig_C
PfamPF07478
Pfam clanCL0179
InterProIPR011095
SCOP22dln / SCOPe / SUPFAM

In enzymology, a D-alanine—D-alanine ligase (EC 6.3.2.4) is an enzyme that catalyzes the chemical reaction

ATP + 2 D-alanine ADP + phosphate + D-alanyl-D-alanine

Thus, the two substrates of this enzyme are ATP and D-alanine, whereas its 3 products are ADP, phosphate, and D-alanyl-D-alanine.

This enzyme belongs to the family of 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.[1]

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

  1. ^ 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.

Further reading

This article incorporates text from the public domain Pfam and InterPro: IPR011127