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PDBsum entry 1qb4
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* Residue conservation analysis
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Enzyme class:
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E.C.4.1.1.31
- phosphoenolpyruvate carboxylase.
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Reaction:
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oxaloacetate + phosphate = phosphoenolpyruvate + hydrogencarbonate
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oxaloacetate
Bound ligand (Het Group name = )
matches with 80.00% similarity
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+
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phosphate
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=
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phosphoenolpyruvate
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+
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hydrogencarbonate
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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Febs Lett
458:93-96
(1999)
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PubMed id:
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Plausible phosphoenolpyruvate binding site revealed by 2.6 A structure of Mn2+-bound phosphoenolpyruvate carboxylase from Escherichia coli.
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H.Matsumura,
M.Terada,
S.Shirakata,
T.Inoue,
T.Yoshinaga,
K.Izui,
Y.Kai.
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ABSTRACT
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We have determined the crystal structure of Mn2+-bound Escherichia coli
phosphoenolpyruvate carboxylase (PEPC) using X-ray diffraction at 2.6 A
resolution, and specified the location of enzyme-bound Mn2+, which is essential
for catalytic activity. The electron density map reveals that Mn2+ is bound to
the side chain oxygens of Glu-506 and Asp-543, and located at the top of the
alpha/beta barrel in PEPC. The coordination sphere of Mn2+ observed in E. coli
PEPC is similar to that of Mn2+ found in the pyruvate kinase structure. The
model study of Mn2+-bound PEPC complexed with phosphoenolpyruvate (PEP) reveals
that the side chains of Arg-396, Arg-581 and Arg-713 could interact with PEP.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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W.Xu,
S.Ahmed,
H.Moriyama,
and
R.Chollet
(2006).
The importance of the strictly conserved, C-terminal glycine residue in phosphoenolpyruvate carboxylase for overall catalysis: mutagenesis and truncation of GLY-961 in the sorghum C4 leaf isoform.
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J Biol Chem,
281,
17238-17245.
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U.Sauer,
and
B.J.Eikmanns
(2005).
The PEP-pyruvate-oxaloacetate node as the switch point for carbon flux distribution in bacteria.
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FEMS Microbiol Rev,
29,
765-794.
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K.Izui,
H.Matsumura,
T.Furumoto,
and
Y.Kai
(2004).
Phosphoenolpyruvate carboxylase: a new era of structural biology.
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Annu Rev Plant Biol,
55,
69-84.
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T.J.Ettema,
K.S.Makarova,
G.L.Jellema,
H.J.Gierman,
E.V.Koonin,
M.A.Huynen,
W.M.de Vos,
and
J.van der Oost
(2004).
Identification and functional verification of archaeal-type phosphoenolpyruvate carboxylase, a missing link in archaeal central carbohydrate metabolism.
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J Bacteriol,
186,
7754-7762.
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D.G.Kehres,
and
M.E.Maguire
(2003).
Emerging themes in manganese transport, biochemistry and pathogenesis in bacteria.
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FEMS Microbiol Rev,
27,
263-290.
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F.Schmitzberger,
A.G.Smith,
C.Abell,
and
T.L.Blundell
(2003).
Comparative analysis of the Escherichia coli ketopantoate hydroxymethyltransferase crystal structure confirms that it is a member of the (betaalpha)8 phosphoenolpyruvate/pyruvate superfamily.
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J Bacteriol,
185,
4163-4171.
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J.Mima,
G.Jung,
T.Onizuka,
H.Ueno,
and
R.Hayashi
(2002).
Amphipathic property of free thiol group contributes to an increase in the catalytic efficiency of carboxypeptidase Y.
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Eur J Biochem,
269,
3220-3225.
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L.F.García-Alles,
and
B.Erni
(2002).
Synthesis of phosphoenol pyruvate (PEP) analogues and evaluation as inhibitors of PEP-utilizing enzymes.
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Eur J Biochem,
269,
3226-3236.
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L.F.Garcia-Alles,
K.Flükiger,
J.Hewel,
R.Gutknecht,
C.Siebold,
S.Schürch,
and
B.Erni
(2002).
Mechanism-based inhibition of enzyme I of the Escherichia coli phosphotransferase system. Cysteine 502 is an essential residue.
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J Biol Chem,
277,
6934-6942.
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S.Akhter,
A.Vignini,
Z.Wen,
A.English,
P.G.Wang,
and
B.Mutus
(2002).
Evidence for S-nitrosothiol-dependent changes in fibrinogen that do not involve transnitrosation or thiolation.
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Proc Natl Acad Sci U S A,
99,
9172-9177.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
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Links
