D-alanine—D-alanine ligase

D-alanine—D-alanine ligase
Identifiers
EC number 6.3.2.4
CAS number 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 / EGO
D-ala D-ala ligase N-terminus

complex of y216f d-ala:d-ala ligase with adp and a phosphoryl phosphinate
Identifiers
Symbol Dala_Dala_lig_N
Pfam PF01820
InterPro IPR011127
SCOP 2dln
SUPERFAMILY 2dln
D-ala D-ala ligase C-terminus

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
SCOP 2dln
SUPERFAMILY 2dln

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 \rightleftharpoons 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

Further reading

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

This article is issued from Wikipedia - version of the Tuesday, February 09, 2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.