{PDOC00330}
{PS00781; PEPCASE_1}
{PS00393; PEPCASE_2}
{BEGIN}
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* Phosphoenolpyruvate carboxylase active sites *
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Phosphoenolpyruvate  carboxylase   (EC 4.1.1.31)   (PEPcase)   catalyzes   the
irreversible beta-carboxylation of phosphoenolpyruvate by bicarbonate to yield
oxaloacetate and phosphate. The enzyme is found in all plants and in a variety
of microorganisms.  A histidine [1]  and a lysine [2] have  been implicated in
the catalytic mechanism of this enzyme;  the  regions around these active site
residues are highly conserved  in PEPcase  from  various  plants, bacteria and
cyanobacteria and can be used as a signature patterns for this type of enzyme.

-Consensus pattern: [VTI]-x-T-A-H-P-T-[EQ]-x(2)-R-[KRHAQ]
                    [H is an active site residue]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Consensus pattern: [IVLC]-M-[LIVM]-G-Y-S-D-S-x-K-[DF]-[STAG]-G
                    [K is an active site residue]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Last update: December 2004 / Patterns and text revised.

[ 1] Terada K., Izui K.
     "Site-directed mutagenesis of the conserved histidine residue of
     phosphoenolpyruvate carboxylase. His138 is essential for the second
     partial reaction."
     Eur. J. Biochem. 202:797-803(1991).
     PubMed=1765093
[ 2] Jiao J.-A., Podesta F.E., Chollet R., O'Leary M.H., Andreo C.S.
     "Isolation and sequence of an active-site peptide from maize leaf
     phosphoenolpyruvate carboxylase inactivated by pyridoxal
     5'-phosphate."
     Biochim. Biophys. Acta 1041:291-295(1990).
     PubMed=2268676

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