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PROSITE documentation PDOC00167 |
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:
Sequence data reveal that the region around the biocytin (biotin-lysine) residue is well conserved and can be used as a signature pattern.
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 <PDOC00168>).
Last update:December 2001 / Pattern and text revised.
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PROSITE method (with tools and information) covered by this documentation:
1 | Authors | Knowles J.R. |
Title | The mechanism of biotin-dependent enzymes. | |
Source | Annu. Rev. Biochem. 58:195-221(1989). | |
PubMed ID | 2673009 | |
DOI | 10.1146/annurev.bi.58.070189.001211 |
2 | Authors | Samols D. Thornton C.G. Murtif V.L. Kumar G.K. Haase F.C. Wood H.G. |
Title | Evolutionary conservation among biotin enzymes. | |
Source | J. Biol. Chem. 263:6461-6464(1988). | |
PubMed ID | 2896195 |
3 | Authors | Goss N.H. Wood H.G. |
Title | Formation of N epsilon-(biotinyl)lysine in biotin enzymes. | |
Source | Methods Enzymol. 107:261-278(1984). | |
PubMed ID | 6438443 |
4 | Authors | Shenoy B.C. Xie Y. Park V.L. Kumar G.K. Beegen H. Wood H.G. Samols D. |
Title | The importance of methionine residues for the catalysis of the biotin enzyme, transcarboxylase. Analysis by site-directed mutagenesis. | |
Source | J. Biol. Chem. 267:18407-18412(1992). | |
PubMed ID | 1526981 |