BRENDA - Enzyme Database show
show all sequences of 1.1.1.24

The reversible association of quinate:NAD+ oxidoreductase from carrot cells with a putative regulatory subunit depends on light conditions

Graziana, A.; Ranjeva, R.; Salimath, B.P.; Boudet, A.M.; FEBS Lett. 163, 306-311 (1983)
No PubMed abstract available

Data extracted from this reference:

Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
additional information
-
transfer of carrot enzyme from dark to light conditions shifts MW from 42000 Da to 110000 Da, probably due to association of a regulatory subunit which may be a calciprotein
Daucus carota
40000
-
1 * 40000 + 1 * 60000-63000, SDS-PAGE
Daucus carota
110000
-
gel filtration
Daucus carota
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
3-dehydroquinate + NADH
Daucus carota
-
quinate + NAD+
-
-
r
quinate + NAD+
Daucus carota
-
5-dehydroquinate + NADH + H+
-
-
r
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Daucus carota
-
carrot
-
Purification (Commentary)
Commentary
Organism
-
Daucus carota
Source Tissue
Source Tissue
Commentary
Organism
Textmining
cell suspension culture
-
Daucus carota
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3-dehydroquinate + NADH
-
286359
Daucus carota
quinate + NAD+
-
-
-
r
quinate + NAD+
-
286359
Daucus carota
5-dehydroquinate + NADH + H+
-
-
-
-
quinate + NAD+
-
286359
Daucus carota
5-dehydroquinate + NADH + H+
-
-
-
r
Subunits
Subunits
Commentary
Organism
dimer
1 * 40000 + 1 * 60000-63000, SDS-PAGE
Daucus carota
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
additional information
-
transfer of carrot enzyme from dark to light conditions shifts MW from 42000 Da to 110000 Da, probably due to association of a regulatory subunit which may be a calciprotein
Daucus carota
40000
-
1 * 40000 + 1 * 60000-63000, SDS-PAGE
Daucus carota
110000
-
gel filtration
Daucus carota
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
3-dehydroquinate + NADH
Daucus carota
-
quinate + NAD+
-
-
r
quinate + NAD+
Daucus carota
-
5-dehydroquinate + NADH + H+
-
-
r
Purification (Commentary) (protein specific)
Commentary
Organism
-
Daucus carota
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
cell suspension culture
-
Daucus carota
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3-dehydroquinate + NADH
-
286359
Daucus carota
quinate + NAD+
-
-
-
r
quinate + NAD+
-
286359
Daucus carota
5-dehydroquinate + NADH + H+
-
-
-
-
quinate + NAD+
-
286359
Daucus carota
5-dehydroquinate + NADH + H+
-
-
-
r
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
1 * 40000 + 1 * 60000-63000, SDS-PAGE
Daucus carota
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
Hppner
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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1
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2
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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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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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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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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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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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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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8
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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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3
2
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1
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1
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286356
Barea
Purification and characterizat ...
Neurospora crassa
Biochim. Biophys. Acta
524
1-14
1978
1
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3
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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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2
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6
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1
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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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3
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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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