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D-alanine—D-alanine ligase
Enzyme belonging to the ligase family / From Wikipedia, the free encyclopedia
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
D-Alanine—D-alanine ligase | |||||||||
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Identifiers | |||||||||
EC no. | 6.3.2.4 | ||||||||
CAS no. | 9023-63-6 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
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 N-terminus | |||||||||
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![]() complex of y216f d-ala:d-ala ligase with adp and a phosphoryl phosphinate | |||||||||
Identifiers | |||||||||
Symbol | Dala_Dala_lig_N | ||||||||
Pfam | PF01820 | ||||||||
InterPro | IPR011127 | ||||||||
SCOP2 | 2dln / SCOPe / SUPFAM | ||||||||
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D-ala D-ala ligase C-terminus | |||||||||
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![]() complex of y216f d-ala:d-ala ligase with adp and a phosphoryl phosphinate | |||||||||
Identifiers | |||||||||
Symbol | Dala_Dala_lig_C | ||||||||
Pfam | PF07478 | ||||||||
Pfam clan | CL0179 | ||||||||
InterPro | IPR011095 | ||||||||
SCOP2 | 2dln / SCOPe / SUPFAM | ||||||||
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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]