PROSITE documentation PDOC00167

Biotin-requiring enzymes attachment site




Description

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.

Technical section

PROSITE method (with tools and information) covered by this documentation:

BIOTIN, PS00188; Biotin-requiring enzymes attachment site  (PATTERN)


References

1AuthorsKnowles J.R.
TitleThe mechanism of biotin-dependent enzymes.
SourceAnnu. Rev. Biochem. 58:195-221(1989).
PubMed ID2673009
DOI10.1146/annurev.bi.58.070189.001211

2AuthorsSamols D., Thornton C.G., Murtif V.L., Kumar G.K., Haase F.C., Wood H.G.
TitleEvolutionary conservation among biotin enzymes.
SourceJ. Biol. Chem. 263:6461-6464(1988).
PubMed ID2896195

3AuthorsGoss N.H., Wood H.G.
TitleFormation of N epsilon-(biotinyl)lysine in biotin enzymes.
SourceMethods Enzymol. 107:261-278(1984).
PubMed ID6438443

4AuthorsShenoy B.C., Xie Y., Park V.L., Kumar G.K., Beegen H., Wood H.G., Samols D.
TitleThe importance of methionine residues for the catalysis of the biotin enzyme, transcarboxylase. Analysis by site-directed mutagenesis.
SourceJ. Biol. Chem. 267:18407-18412(1992).
PubMed ID1526981



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