{PDOC50991}
{PS50991; PYR_CT}
{BEGIN}
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* Pyruvate carboxyltransferase domain profile *
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Pyruvate  carboxylase  (EC  6.4.1.1)  (PC),  a  member of the biotin-dependent
enzyme   family,   is   involved  in  the  gluconeogenesis  by  mediating  the
carboxylation   of  pyruvate  to  oxaloacetate.  Biotin-dependent  carboxylase
enzymes perform a two step reaction. Enzyme-bound biotin is first carboxylated
by  bicarbonate  and ATP and the carboxyl group temporarily bound to biotin is
subsequently transferred to an acceptor substrate such as pyruvate [1]. PC has
three  functional domains: a biotin carboxylase (BC) domain (see <PDOC50979>),
a  carboxyltransferase  (CT)  domain  which  perform  the  second  part of the
reaction and a biotinyl domain (see <PDOC50968>) [2,3]. The mechanism by which
the carboxyl group is transferred from the carboxybiotin to the pyruvate is not
well understood.

The  pyruvate  carboxyltransferase  domain  is  also  found  in other pyruvate
binding  enzymes  and acetyl-CoA dependent enzymes suggesting that this domain
can be associated with different enzymatic activities:

 - 2-isopropylmalate synthase (EC 2.3.3.13).
 - (R)-citramalate synthase (EC 2.3.3.-).
 - Homocitrate synthase (EC 2.3.3.14).
 - Hydroxymethylglutaryl-CoA lyase (EC 4.1.3.4) (HMGL).
 - 4-hydroxy-2-oxovalerate aldolase (EC 4.1.3.39) (HOA).
 - Oxaloacetate decarboxylase (EC 4.1.1.3).

The profile we developed spans the entire carboxyltransferase domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: May 2004 / First entry.

[ 1] Attwood P.V., Wallace J.C.
     "Chemical and catalytic mechanisms of carboxyl transfer reactions in
     biotin-dependent enzymes."
     Acc. Chem. Res. 35:113-120(2002).
     PubMed=11851389
[ 2] Attwood P.V.
     "The structure and the mechanism of action of pyruvate carboxylase."
     Int. J. Biochem. Cell Biol. 27:231-249(1995).
     PubMed=7780827
[ 3] Jitrapakdee S., Wallace J.C.
     "Structure, function and regulation of pyruvate carboxylase."
     Biochem. J. 340:1-16(1999).
     PubMed=10229653

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