BRENDA - Enzyme Database show
show all sequences of 1.1.1.24

The identity of shikimate dehydrogenase and quinate dehydrogenase in Aspergillus niger

Cain, R.B.; Biochem. J. 127, 15P (1972)

Data extracted from this reference:

Engineering
Amino acid exchange
Commentary
Organism
additional information
enzyme knockout results in loss of the ability to grow on quinate and/or shikimate
Aspergillus niger
Inhibitors
Inhibitors
Commentary
Organism
Structure
chloromercuribenzene 4-sulfonate
inhibits both activities of the enzyme
Aspergillus niger
additional information
the enzyme is strongly repressed by D-glucose
Aspergillus niger
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.031
-
NAD+
-
Aspergillus niger
0.26
-
NAD+
+ quinate
Aspergillus niger
0.32
0.37
quinate
-
Aspergillus niger
0.42
-
NAD+
+ shikimate
Aspergillus niger
6.25
-
quinate
-
Aspergillus niger
11.5
-
shikimate
-
Aspergillus niger
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
23000
-
gel filtration
Aspergillus niger
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-quinate + NAD+
Aspergillus niger
-
3-dehydroquinate + NADH + H+
-
-
r
additional information
Aspergillus niger
addition of either shikimate or quinate to the assay does not increase the reaction rate when the other substrate is present alone
?
-
-
-
shikimate + NAD+
Aspergillus niger
-
3-dehydroshikimate + NADH + H+
-
-
r
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Aspergillus niger
-
; bifunctional enzyme: quinate (shikimate) dehydrogenase, different from EC 1.1.1.25
-
Purification (Commentary)
Commentary
Organism
separation from NADP+-linked shikimate dehydrogenase, EC 1.1.1.25, gel filtration
Aspergillus niger
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-quinate + NAD+
-
286357
Aspergillus niger
3-dehydroquinate + NADH + H+
-
-
-
r
additional information
addition of either shikimate or quinate to the assay does not increase the reaction rate when the other substrate is present alone
286357
Aspergillus niger
?
-
-
-
-
additional information
the bifunctional enzyme shows quinate and shikimate dehydrogenase activities
286357
Aspergillus niger
?
-
-
-
-
quinate + NAD+
-
286357
Aspergillus niger
5-dehydroquinate + NADH + H+
-
-
-
-
shikimate + NAD+
-
286357
Aspergillus niger
?
-
-
-
-
shikimate + NAD+
-
286357
Aspergillus niger
3-dehydroshikimate + NADH + H+
-
-
-
r
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
47
-
inactivation, kinetics vary in presence of quinate or shikimate, respectively
Aspergillus niger
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
additional information
-
different pH optima for shikimate and quinate
Aspergillus niger
Cofactor
Cofactor
Commentary
Organism
Structure
additional information
no activity with NADP(H)
Aspergillus niger
NAD+
-
Aspergillus niger
NADH
-
Aspergillus niger
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
additional information
no activity with NADP(H)
Aspergillus niger
NAD+
-
Aspergillus niger
NADH
-
Aspergillus niger
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
additional information
enzyme knockout results in loss of the ability to grow on quinate and/or shikimate
Aspergillus niger
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
chloromercuribenzene 4-sulfonate
inhibits both activities of the enzyme
Aspergillus niger
additional information
the enzyme is strongly repressed by D-glucose
Aspergillus niger
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.031
-
NAD+
-
Aspergillus niger
0.26
-
NAD+
+ quinate
Aspergillus niger
0.32
0.37
quinate
-
Aspergillus niger
0.42
-
NAD+
+ shikimate
Aspergillus niger
6.25
-
quinate
-
Aspergillus niger
11.5
-
shikimate
-
Aspergillus niger
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
23000
-
gel filtration
Aspergillus niger
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-quinate + NAD+
Aspergillus niger
-
3-dehydroquinate + NADH + H+
-
-
r
additional information
Aspergillus niger
addition of either shikimate or quinate to the assay does not increase the reaction rate when the other substrate is present alone
?
-
-
-
shikimate + NAD+
Aspergillus niger
-
3-dehydroshikimate + NADH + H+
-
-
r
Purification (Commentary) (protein specific)
Commentary
Organism
separation from NADP+-linked shikimate dehydrogenase, EC 1.1.1.25, gel filtration
Aspergillus niger
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-quinate + NAD+
-
286357
Aspergillus niger
3-dehydroquinate + NADH + H+
-
-
-
r
additional information
addition of either shikimate or quinate to the assay does not increase the reaction rate when the other substrate is present alone
286357
Aspergillus niger
?
-
-
-
-
additional information
the bifunctional enzyme shows quinate and shikimate dehydrogenase activities
286357
Aspergillus niger
?
-
-
-
-
quinate + NAD+
-
286357
Aspergillus niger
5-dehydroquinate + NADH + H+
-
-
-
-
shikimate + NAD+
-
286357
Aspergillus niger
?
-
-
-
-
shikimate + NAD+
-
286357
Aspergillus niger
3-dehydroshikimate + NADH + H+
-
-
-
r
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
47
-
inactivation, kinetics vary in presence of quinate or shikimate, respectively
Aspergillus niger
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
additional information
-
different pH optima for shikimate and quinate
Aspergillus niger
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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2
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1
2
1
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8
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2
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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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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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-
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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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6
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5
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3
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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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2
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1
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2
1
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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
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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
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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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5
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3
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5
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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
2
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1
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3
1
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8
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2
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1
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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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2
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286356
Barea
Purification and characterizat ...
Neurospora crassa
Biochim. Biophys. Acta
524
1-14
1978
1
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1
1
2
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1
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1
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3
1
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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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1
3
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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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