D-Alanine—D-alanine ligase | |
Ec Number: | 6.3.2.4 |
Cas Number: | 9023-63-6 |
Go Code: | 0008716 |
Symbol: | Dala_Dala_lig_N |
D-ala D-ala ligase N-terminus | |
Pfam: | PF01820 |
Interpro: | IPR011127 |
Scop: | 2dln |
Symbol: | Dala_Dala_lig_C |
D-ala D-ala ligase C-terminus | |
Pfam: | PF07478 |
Pfam Clan: | CL0179 |
Interpro: | IPR011095 |
Scop: | 2dln |
In enzymology, a D-alanine—D-alanine ligase is an enzyme that catalyzes the chemical reaction
ATP + 2 D-alanine
\rightleftharpoons
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 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.[1]
As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes,,,,,,, and .