Biotin attachment domain explained

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.^[1] Lipoamide acyltransferases have an essential cofactor, lipoic acid, which is covalently bound via an amide linkage to a lysine group.^[2] 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;

Notes and References

1. Kumar GK, Shenoy BC, Wood HG, Samols D, Xie Y, Park VL, Beegen H . The importance of methionine residues for the catalysis of the biotin enzyme, transcarboxylase. Analysis by site-directed mutagenesis . J. Biol. Chem. . 267 . 26 . 18407–18412 . 1992 . 10.1016/S0021-9258(19)36977-7 . 1526981. free .
2. Guest JR, Russell GC . Sequence similarities within the family of dihydrolipoamide acyltransferases and discovery of a previously unidentified fungal enzyme . Biochim. Biophys. Acta . 1076 . 2 . 225–232 . 1991 . 1825611 . 10.1016/0167-4838(91)90271-z.