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Biotin attachment domain
A:55-122 A:55-122 A:55-122 B:81-155 A:81-155 B:81-155 A:81-155 :81-155 :81-155 B:186-260 B:186-260 :186-260 B:186-260 :3-76 :3-76 A:4-76 A:207-278 :3-73 :3-73 :3-76 :3-76 A:65-138 A:65-138
Biotin/lipoyl attachment domain has a conserved lysine residue that binds biotin or lipoic acid. Biotin plays a catalytic role in some carboxyl transfer reactions and is covalently attached, via an amide bond, to a lysine residue in enzymes requiring this coenzyme. Lipoamide acyltransferases have an essential cofactor, lipoic acid, which is covalently bound via an amide linkage to a lysine group. The lipoic acid cofactor is found in a variety of proteins.
Human proteins containing this domain
ACACA; ACACB; DBT; DLAT; DLST; DLSTP; MCCC1; PC; PCCA; PDHX;
References
References
- (1992). "The importance of methionine residues for the catalysis of the biotin enzyme, transcarboxylase. Analysis by site-directed mutagenesis". J. Biol. Chem..
- (1991). "Sequence similarities within the family of dihydrolipoamide acyltransferases and discovery of a previously unidentified fungal enzyme". Biochim. Biophys. Acta.
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