PROSITE documentation PDOC00167Biotin-requiring enzymes attachment site
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PURL: https://purl.expasy.org/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:
- 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.
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 |
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