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show all sequences of 1.1.1.24

Purification and characterization of quinate (shikimate) dehydrogenase, an enzyme in the inducible quinic acid catabolic pathway of Neurospora crassa

Barea, J.L.; Giles, N.H.; Biochim. Biophys. Acta 524, 1-14 (1978)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
dithiothreitol
-
Neurospora crassa
General Stability
General Stability
Organism
high ionic strength, such as 0.1 M (NH4)2SO4, NaCl or phosphate buffer or the presence of 0.1 M quinate or shikimate protects against thermal inactivation
Neurospora crassa
Inhibitors
Inhibitors
Commentary
Organism
Structure
p-chloromercuribenzoate
-
Neurospora crassa
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.32
0.37
quinate
-
Neurospora crassa
1.18
-
shikimate
-
Neurospora crassa
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
41000
-
1 * 41000, SDS-PAGE in presence of urea or electrophoresis in presence of cetyltrimethyl ammonium bromide
Neurospora crassa
42000
-
sucrose density gradient centrifugation
Neurospora crassa
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
quinate + NAD+
Neurospora crassa
first reaction in inducible quinic acid catabolic pathway
5-dehydroquinate + NADH + H+
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Neurospora crassa
-
bifunctional enzyme: quinate (shikimate) dehydrogenase
-
Purification (Commentary)
Commentary
Organism
bifunctional enzyme: quinate (shikimate) dehydrogenase
Neurospora crassa
Source Tissue
Source Tissue
Commentary
Organism
Textmining
mycelium
-
Neurospora crassa
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
86.87
-
-
Neurospora crassa
Storage Stability
Storage Stability
Organism
-20°C, 0.1 M NaCl, half-life 40 days
Neurospora crassa
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
quinate + NAD+
-
286356
Neurospora crassa
5-dehydroquinate + NADH + H+
-
-
-
-
quinate + NAD+
first reaction in inducible quinic acid catabolic pathway
286356
Neurospora crassa
5-dehydroquinate + NADH + H+
-
-
-
-
shikimate + NAD+
-
286356
Neurospora crassa
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
monomer
1 * 41000, SDS-PAGE in presence of urea or electrophoresis in presence of cetyltrimethyl ammonium bromide
Neurospora crassa
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
40
-
half-life of unprotected enzyme: 20 min, 180 min in presence of NaCl, completely stable in presence of quinate, shikimate or NADH
Neurospora crassa
pH Stability
pH Stability
pH Stability Maximum
Commentary
Organism
7.5
-
-20°C, highest stability
Neurospora crassa
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
specific for NAD+
Neurospora crassa
NADH
specific for NAD+
Neurospora crassa
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
dithiothreitol
-
Neurospora crassa
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
specific for NAD+
Neurospora crassa
NADH
specific for NAD+
Neurospora crassa
General Stability (protein specific)
General Stability
Organism
high ionic strength, such as 0.1 M (NH4)2SO4, NaCl or phosphate buffer or the presence of 0.1 M quinate or shikimate protects against thermal inactivation
Neurospora crassa
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
p-chloromercuribenzoate
-
Neurospora crassa
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.32
0.37
quinate
-
Neurospora crassa
1.18
-
shikimate
-
Neurospora crassa
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
41000
-
1 * 41000, SDS-PAGE in presence of urea or electrophoresis in presence of cetyltrimethyl ammonium bromide
Neurospora crassa
42000
-
sucrose density gradient centrifugation
Neurospora crassa
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
quinate + NAD+
Neurospora crassa
first reaction in inducible quinic acid catabolic pathway
5-dehydroquinate + NADH + H+
-
-
-
Purification (Commentary) (protein specific)
Commentary
Organism
bifunctional enzyme: quinate (shikimate) dehydrogenase
Neurospora crassa
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
mycelium
-
Neurospora crassa
-
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
86.87
-
-
Neurospora crassa
Storage Stability (protein specific)
Storage Stability
Organism
-20°C, 0.1 M NaCl, half-life 40 days
Neurospora crassa
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
quinate + NAD+
-
286356
Neurospora crassa
5-dehydroquinate + NADH + H+
-
-
-
-
quinate + NAD+
first reaction in inducible quinic acid catabolic pathway
286356
Neurospora crassa
5-dehydroquinate + NADH + H+
-
-
-
-
shikimate + NAD+
-
286356
Neurospora crassa
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
monomer
1 * 41000, SDS-PAGE in presence of urea or electrophoresis in presence of cetyltrimethyl ammonium bromide
Neurospora crassa
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
40
-
half-life of unprotected enzyme: 20 min, 180 min in presence of NaCl, completely stable in presence of quinate, shikimate or NADH
Neurospora crassa
pH Stability (protein specific)
pH Stability
pH Stability Maximum
Commentary
Organism
7.5
-
-20°C, highest stability
Neurospora crassa
Other publictions for EC 1.1.1.24
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
727115
Höppner
Enzyme-substrate complexes of ...
Corynebacterium glutamicum, Corynebacterium glutamicum ATCC 13032
Biol. Chem.
394
1505-1516
2013
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1
1
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8
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2
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4
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1
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6
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1
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8
2
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6
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1
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8
2
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8
8
698068
Marsh
Changes in quinic acid metabol ...
Actinidia arguta, Actinidia arguta var. arguta, Actinidia chinensis, Actinidia deliciosa, Actinidia deliciosa var. deliciosa
Funct. Plant Biol.
36
463-470
2009
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5
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3
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5
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1
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5
3
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3
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3
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684153
Schoepe
1.6 A structure of an NAD(+)-d ...
Corynebacterium glutamicum
Acta Crystallogr. Sect. D
64
803-809
2008
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1
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2
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2
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2
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4
1
1
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2
2
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657345
Shein
-
The content of phenolic compou ...
Pinus sylvestris
Russ. J. Plant Physiol.
50
516-521
2003
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1
1
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286364
Ossipov
-
Broad-specificity quinate (shi ...
Daucus carota, Pinus taeda
Plant Physiol.
38
923-928
2000
-
-
-
-
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4
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1
2
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2
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1
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1
1
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3
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2
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2
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4
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1
2
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1
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1
1
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3
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286363
Grund
Utilization of quinate and p-h ...
Pseudonocardia sp., Rhodococcus rhodochrous, Streptomyces sp.
J. Basic Microbiol.
38
241-255
1998
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3
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6
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286362
Kang
-
Subcellular localization of qu ...
Vigna radiata var. radiata
Z. Naturforsch. C
49
415-420
1994
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1
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5487
Hawkins
Characterization of the 3-dehy ...
Aspergillus nidulans
Biochem. J.
296
451-457
1993
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286365
Kang
-
Purification and characterizat ...
Vigna radiata var. radiata
Phytochemistry
33
769-773
1993
3
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2
8
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2
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1
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3
1
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286359
Graziana
-
The reversible association of ...
Daucus carota
FEBS Lett.
163
306-311
1983
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286356
Barea
Purification and characterizat ...
Neurospora crassa
Biochim. Biophys. Acta
524
1-14
1978
1
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286357
Cain
The identity of shikimate dehy ...
Aspergillus niger
Biochem. J.
127
15P
1972
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1
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2
6
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684945
Cain
Metabolism of shikimate and qu ...
Aspergillus niger
Biochem. J.
127
15P-16P
1972
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286358
Gamborg
-
Aromatic metabolism in plants ...
Vigna radiata var. radiata
Biochim. Biophys. Acta
128
483-491
1966
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7
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286360
Davies
-
Enzymes of aromatic biosynthes ...
Enterobacter aerogenes
Methods Enzymol.
2
307-311
1955
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