Diaminobutyrate acetyltransferase

In enzymology, a diaminobutyrate acetyltransferase (EC 2.3.1.178) is an enzyme that catalyzes the chemical reaction

acetyl-CoA + L-2,4-diaminobutanoate CoA + N4-acetyl-L-2,4-diaminobutanoate
Diaminobutyrate acetyltransferase
Identifiers
EC no.2.3.1.178
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
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PMCarticles
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NCBIproteins

Thus, the two substrates of this enzyme are acetyl-CoA and L-2,4-diaminobutanoate, whereas its two products are CoA and N4-acetyl-L-2,4-diaminobutanoate.

This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl-CoA:L-2,4-diaminobutanoate N4-acetyltransferase. Other names in common use include L-2,4-diaminobutyrate acetyltransferase, L-2,4-diaminobutanoate acetyltransferase, EctA, diaminobutyric acid acetyltransferase, DABA acetyltransferase, 2,4-diaminobutanoate acetyltransferase, DAB acetyltransferase, DABAcT, and acetyl-CoA:L-2,4-diaminobutanoate 4-N-acetyltransferase. This enzyme participates in glycine, serine and threonine metabolism.

References


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