{PDOC00167}
{PS00188; BIOTIN}
{BEGIN}
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* Biotin-requiring enzymes attachment site *
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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 <PDOC00168>).
-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
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