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* Residue conservation analysis
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Enzyme class:
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E.C.5.3.1.6
- Ribose-5-phosphate isomerase.
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Reaction:
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D-ribose 5-phosphate = D-ribulose 5-phosphate
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D-ribose 5-phosphate
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=
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D-ribulose 5-phosphate
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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Gene Ontology (GO) functional annotation
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Cellular component
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cytoplasm
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2 terms
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Biological process
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pyridoxine biosynthetic process
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3 terms
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Biochemical function
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protein binding
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4 terms
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DOI no:
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Biochimie
87:763-769
(2005)
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PubMed id:
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Crystal structure of the S. cerevisiae D-ribose-5-phosphate isomerase: comparison with the archaeal and bacterial enzymes.
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M.Graille,
P.Meyer,
N.Leulliot,
I.Sorel,
J.Janin,
H.Van Tilbeurgh,
S.Quevillon-Cheruel.
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ABSTRACT
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Ribose-5-phosphate isomerase A has an important role in sugar metabolism by
interconverting ribose-5-phosphate and ribulose-5-phosphate. This enzyme is
ubiquitous and highly conserved among the three kingdoms of life. We have solved
the 2.1 A resolution crystal structure of the Saccharomyces cerevisiae enzyme by
molecular replacement. This protein adopts the same fold as its archaeal and
bacterial orthologs with two alpha/beta domains tightly packed together. Mapping
of conserved residues at the surface of the protein reveals strong invariability
of the active site pocket, suggesting a common ligand binding mode and a similar
catalytic mechanism. The yeast enzyme associates as a homotetramer similarly to
the archaeal protein. The effect of an inactivating mutation (Arg189 to Lys) is
discussed in view of the information brought by this structure.
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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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J.Jung,
J.K.Kim,
S.J.Yeom,
Y.J.Ahn,
D.K.Oh,
and
L.W.Kang
(2011).
Crystal structure of Clostridium thermocellum ribose-5-phosphate isomerase B reveals properties critical for fast enzyme kinetics.
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Appl Microbiol Biotechnol, 90,
517-527.
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PDB codes:
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T.G.Kim,
T.H.Kwon,
K.Min,
M.S.Dong,
Y.I.Park,
and
C.Ban
(2009).
Crystal structures of substrate and inhibitor complexes of ribose 5-phosphate isomerase A from Vibrio vulnificus YJ016.
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Mol Cells, 27,
99.
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PDB codes:
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M.M.Wamelink,
E.A.Struys,
and
C.Jakobs
(2008).
The biochemistry, metabolism and inherited defects of the pentose phosphate pathway: a review.
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J Inherit Metab Dis, 31,
703-717.
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K.I.Minard,
C.A.Carroll,
S.T.Weintraub,
and
L.Mc-Alister-Henn
(2007).
Changes in disulfide bond content of proteins in a yeast strain lacking major sources of NADPH.
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Free Radic Biol Med, 42,
106-117.
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M.A.Holmes,
F.S.Buckner,
W.C.Van Voorhis,
C.L.Verlinde,
C.Mehlin,
E.Boni,
G.DeTitta,
J.Luft,
A.Lauricella,
L.Anderson,
O.Kalyuzhniy,
F.Zucker,
L.W.Schoenfeld,
T.N.Earnest,
W.G.Hol,
and
E.A.Merritt
(2006).
Structure of ribose 5-phosphate isomerase from Plasmodium falciparum.
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Acta Crystallogr Sect F Struct Biol Cryst Commun, 62,
427-431.
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PDB code:
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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.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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Links
