{PDOC00167} {PS00188; BIOTIN} {BEGIN} ******************************************** * Biotin-requiring enzymes attachment site * ******************************************** Biotin, which plays a catalytic role in some carboxyl transfer reactions, is covalently attached, via an amide bond, to a lysine residue in enzymes requiring this coenzyme [1,2,3,4]. Such enzymes are: - Pyruvate carboxylase (EC 6.4.1.1). - Acetyl-CoA carboxylase (EC 6.4.1.2). - Propionyl-CoA carboxylase (EC 6.4.1.3). - Methylcrotonyl-CoA carboxylase (EC 6.4.1.4). - Geranoyl-CoA carboxylase (EC 6.4.1.5). - Urea carboxylase (EC 6.3.4.6). - Oxaloacetate decarboxylase (EC 4.1.1.3). - Methylmalonyl-CoA decarboxylase (EC 4.1.1.41). - Glutaconyl-CoA decarboxylase (EC 4.1.1.70). - Methylmalonyl-CoA carboxyl-transferase (EC 2.1.3.1) (transcarboxylase). Sequence data reveal that the region around the biocytin (biotin-lysine) residue is well conserved and can be used as a signature pattern. -Consensus pattern: [GDN]-[DEQTR]-x-[LIVMFY]-x(2)-[LIVM]-x-[AIV]-M-K-[LVMAT]- x(3)-[LIVM]-x-[SAV] [K is the biotin attachment site] -Sequences known to belong to this class detected by the pattern: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Note: The domain around the biotin-binding lysine residue is evolutionary related to that around the lipoyl-binding lysine residue of 2-oxo acid dehydrogenase acyltransferases (see ). -Last update: December 2001 / Pattern and text revised. [ 1] Knowles J.R. "The mechanism of biotin-dependent enzymes." Annu. Rev. Biochem. 58:195-221(1989). PubMed=2673009; DOI=10.1146/annurev.bi.58.070189.001211 [ 2] Samols D., Thornton C.G., Murtif V.L., Kumar G.K., Haase F.C., Wood H.G. "Evolutionary conservation among biotin enzymes." J. Biol. Chem. 263:6461-6464(1988). PubMed=2896195 [ 3] Goss N.H., Wood H.G. "Formation of N epsilon-(biotinyl)lysine in biotin enzymes." Methods Enzymol. 107:261-278(1984). PubMed=6438443 [ 4] Shenoy B.C., Xie Y., Park V.L., Kumar G.K., Beegen H., Wood H.G., Samols D. "The importance of methionine residues for the catalysis of the biotin enzyme, transcarboxylase. Analysis by site-directed mutagenesis." J. Biol. Chem. 267:18407-18412(1992). PubMed=1526981 -------------------------------------------------------------------------------- PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html -------------------------------------------------------------------------------- {END}