Biotin attachment domain

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Biotin-requiring enzyme
Identifiers
Symbol Biotin_lipoyl
Pfam PF00364
InterPro IPR000089
PROSITE PDOC00168
SCOP 1lab
SUPERFAMILY 1lab
TCDB 3.B.1
CDD cd06663

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[edit]

ACACA; ACACB; DBT; DLAT; DLST; DLSTP; MCCC1; PC; PCCA; PDHX;

References[edit]

  1. ^ Kumar GK, Shenoy BC, Wood HG, Samols D, Xie Y, Park VL, Beegen H (1992). "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. PMID 1526981. 
  2. ^ Guest JR, Russell GC (1991). "Sequence similarities within the family of dihydrolipoamide acyltransferases and discovery of a previously unidentified fungal enzyme". Biochim. Biophys. Acta 1076 (2): 225–232. doi:10.1016/0167-4838(91)90271-z. PMID 1825611. 

This article incorporates text from the public domain Pfam and InterPro IPR000089