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Oxidoreductase
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PDB id
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1crw
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Contents |
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* Residue conservation analysis
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Enzyme class:
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E.C.1.2.1.12
- Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating).
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Pathway:
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Glyceraldehyde-3-phosphate Dehydrogenase (phosphorylating)
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Reaction:
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D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH
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D-glyceraldehyde 3-phosphate
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+
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phosphate
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+
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NAD(+)
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=
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3-phospho-D-glyceroyl phosphate
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+
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NADH
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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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1 term
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Biological process
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oxidation-reduction process
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3 terms
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Biochemical function
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nucleotide binding
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6 terms
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DOI no:
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J Struct Biol
130:1-9
(2000)
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PubMed id:
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Structure of apo-glyceraldehyde-3-phosphate dehydrogenase from Palinurus versicolor.
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Y.Q.Shen,
J.Li,
S.Y.Song,
Z.J.Lin.
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ABSTRACT
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d-Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) shows cooperative properties
for binding coenzymes. The structure of apo-GAPDH from Palinurus versicolor has
been solved at 2.0 A resolution by X-ray crystallography. The final model gives
a crystallographic R factor of 0.178 in the resolution range 8 to 2 A. The
structural comparison with holo-GAPDH from the same species reveals a
conformational change induced by coenzyme binding similar to that observed in
Bacillus stearothermophilus GAPDH but to a lesser extent. The differences in
magnitude during the apo-holo transition between these two enzymes were analyzed
with respect to the change of the amino acid composition in the coenzyme binding
pocket. In the crystalline state of apo-GAPDH, the overall structures of the
subunits are similar to each other; however, significant differences in
temperature factors and minor differences in domain rotation upon coenzyme
binding were observed for different subunits. These structural features are
discussed in relation to the environmental asymmetry of crystallographically
independent subunits.
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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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D.A.Butterfield,
S.S.Hardas,
and
M.L.Lange
(2010).
Oxidatively modified glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and Alzheimer's disease: many pathways to neurodegeneration.
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J Alzheimers Dis, 20,
369-393.
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F.Ferreira-da-Silva,
P.J.Pereira,
L.Gales,
M.Roessle,
D.I.Svergun,
P.Moradas-Ferreira,
and
A.M.Damas
(2006).
The crystal and solution structures of glyceraldehyde-3-phosphate dehydrogenase reveal different quaternary structures.
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J Biol Chem, 281,
33433-33440.
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PDB code:
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J.L.Jenkins,
and
J.J.Tanner
(2006).
High-resolution structure of human D-glyceraldehyde-3-phosphate dehydrogenase.
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Acta Crystallogr D Biol Crystallogr, 62,
290-301.
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PDB codes:
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V.F.Waingeh,
C.D.Gustafson,
E.I.Kozliak,
S.L.Lowe,
H.R.Knull,
and
K.A.Thomasson
(2006).
Glycolytic enzyme interactions with yeast and skeletal muscle F-actin.
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Biophys J, 90,
1371-1384.
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S.W.Cowan-Jacob,
M.Kaufmann,
A.N.Anselmo,
W.Stark,
and
M.G.Grütter
(2003).
Structure of rabbit-muscle glyceraldehyde-3-phosphate dehydrogenase.
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Acta Crystallogr D Biol Crystallogr, 59,
2218-2227.
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PDB code:
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Y.Q.Shen,
S.Y.Song,
and
Z.J.Lin
(2002).
Structures of D-glyceraldehyde-3-phosphate dehydrogenase complexed with coenzyme analogues.
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Acta Crystallogr D Biol Crystallogr, 58,
1287-1297.
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PDB codes:
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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
code is
shown on the right.
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