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* Residue conservation analysis
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Gene Ontology (GO) functional annotation
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Biological process
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growth
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4 terms
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Biochemical function
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lyase activity
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2 terms
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DOI no:
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FEBS Lett
530:24-30
(2002)
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PubMed id:
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Specificity of substrate recognition by type II dehydroquinases as revealed by binding of polyanions.
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L.D.Evans,
A.W.Roszak,
L.J.Noble,
D.A.Robinson,
P.A.Chalk,
J.L.Matthews,
J.R.Coggins,
N.C.Price,
A.J.Lapthorn.
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ABSTRACT
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The interactions between the polyanionic ligands phosphate and sulphate and the
type II dehydroquinases from Streptomyces coelicolor and Mycobacterium
tuberculosis have been characterised using a combination of structural and
kinetic methods. From both approaches, it is clear that interactions are more
complex in the case of the latter enzyme. The data provide new insights into the
differences between the two enzymes in terms of substrate recognition and
catalytic efficiency and may also explain the relative potencies of rationally
designed inhibitors. An improved route to the synthesis of the substrate
3-dehydroquinic acid (dehydroquinate) is described.
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Selected figure(s)
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Figure 2.
Fig. 2. Stereoviews of an overlay of the Ca backbone trace
of MTDHQase (black)+sulphate anions (labelled S1–S4) and
SCDHQase (grey)+phosphate anion (labelled P1). The figure was
produced using SETOR [23].
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Figure 3.
Fig. 3. Ribbon representations of the active sites of (A)
SCDHQ with phosphate (P1) bound and (B) MTDHQase with two
sulphate ions (S1 and S2) bound. Amino acid residues important
for ligand binding are shown in stick and coloured according to
atom type, hydrogen bonds are shown as dashed lines coloured
magenta. The figure was produced using DINO.
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The above figures are
reprinted
by permission from the Federation of European Biochemical Societies:
FEBS Lett
(2002,
530,
24-30)
copyright 2002.
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Figures were
selected
by an automated process.
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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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C.González-Bello,
and
L.Castedo
(2007).
Progress in type II dehydroquinase inhibitors: from concept to practice.
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Med Res Rev, 27,
177-208.
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M.D.Toscano,
R.J.Payne,
A.Chiba,
O.Kerbarh,
and
C.Abell
(2007).
Nanomolar Inhibition of Type II Dehydroquinase Based on the Enolate Reaction Mechanism.
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ChemMedChem, 2,
101-112.
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V.F.Prazeres,
C.Sánchez-Sixto,
L.Castedo,
A.Canales,
F.J.Cañada,
J.Jiménez-Barbero,
H.Lamb,
A.R.Hawkins,
and
C.González-Bello
(2006).
Determination of the bound conformation of a competitive nanomolar inhibitor of mycobacterium tuberculosis type II dehydroquinase by NMR spectroscopy.
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ChemMedChem, 1,
990-996.
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D.Maes,
L.A.Gonzalez-Ramirez,
J.Lopez-Jaramillo,
B.Yu,
H.De Bondt,
I.Zegers,
E.Afonina,
J.M.Garcia-Ruiz,
and
S.Gulnik
(2004).
Structural study of the type II 3-dehydroquinate dehydratase from Actinobacillus pleuropneumoniae.
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Acta Crystallogr D Biol Crystallogr, 60,
463-471.
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PDB code:
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B.I.Lee,
J.E.Kwak,
and
S.W.Suh
(2003).
Crystal structure of the type II 3-dehydroquinase from Helicobacter pylori.
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Proteins, 51,
616-617.
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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
code is
shown on the right.
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Links
