Biology:Biotin attachment domain
| Biotin/lipoyl attachment domain | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||||
| Symbol | Biotin_lipoyl | ||||||||||
| Pfam | PF00364 | ||||||||||
| InterPro | IPR000089 | ||||||||||
| PROSITE | PDOC00168 | ||||||||||
| SCOP2 | 1lab / SCOPe / SUPFAM | ||||||||||
| CDD | cd06663 | ||||||||||
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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;
References
- ↑ "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. doi:10.1016/S0021-9258(19)36977-7. PMID 1526981.
- ↑ "Sequence similarities within the family of dihydrolipoamide acyltransferases and discovery of a previously unidentified fungal enzyme". Biochim. Biophys. Acta 1076 (2): 225–232. 1991. doi:10.1016/0167-4838(91)90271-z. PMID 1825611.
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