D-alanine—D-alanine ligase
D-Alanine—D-alanine ligase | |||||||||
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Identifiers | |||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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D-ala D-ala ligase SCOP2 | 2dln / SCOPe / SUPFAM | ||||||||
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D-ala D-ala ligase C-terminus | |||||||||
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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
.This enzyme belongs to the family of
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
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
- PMID 10908650.
Further reading
- 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. .
- 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. PMID 11699883.