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EC Tree
IUBMB Comments Also reduces D-galacturonate. May be identical with EC 1.1.1.2 [alcohol dehydrogenase (NADP+)].
The enzyme appears in viruses and cellular organisms
Synonyms
akr1a1, aldehyde reductase ii, hexonate dehydrogenase, glucuronate reductase, d-glucuronate reductase, pcgor, nadp-l-gulonate dehydrogenase, galacturonate oxidoreductase,
more
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aldehyde reductase II
-
-
-
-
D-glucuronate dehydrogenase
-
-
-
-
D-glucuronate reductase
-
-
-
-
D-glucuronic reductase
-
-
-
-
galacturonate oxidoreductase
hexonate dehydrogenase
-
-
-
-
L-glucuronate reductase
-
-
-
-
L-gulonate NAD-3-oxidoreductase
-
-
-
-
L-hexonate:NADP dehydrogenase
-
-
-
-
NADP-L-gulonate dehydrogenase
-
-
-
-
TPN l-hexonate dehydrogenase
TPN-L-gulonate dehydrogenase
-
-
-
-
AKR1A1
-
-
aldehyde reductase
-
-
-
-
galacturonate oxidoreductase
-
galacturonate oxidoreductase
-
-
PcGOR
-
TPN l-hexonate dehydrogenase
-
-
TPN l-hexonate dehydrogenase
-
-
additional information
-
the enzyme belongs to the aldo-keto reductase superfamily
additional information
-
the enzyme belongs to the aldo-keto reductase superfamily
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
L-gulonate + NADP+ = D-glucuronate + NADPH + H+
L-gulonate + NADP+ = D-glucuronate + NADPH + H+
also reduces D-galacturonate
-
-
-
L-gulonate + NADP+ = D-glucuronate + NADPH + H+
may be identical with EC 1.1.1.2 (alcohol dehydrogenase (NADP)) e.g. in
-
-
-
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oxidation
-
-
-
oxidation
-
-
pH dependent reaction mechanism
-
oxidation
-
-
ordered bi bi mechanism
-
reduction
-
-
-
reduction
-
-
pH dependent reaction mechanism
-
reduction
-
-
ordered bi bi mechanism
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
L-gulonate:NADP+ 6-oxidoreductase
Also reduces D-galacturonate. May be identical with EC 1.1.1.2 [alcohol dehydrogenase (NADP+)].
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2-deoxyglucose + NADPH + H+
?
-
-
-
-
r
2-nitrobenzaldehyde + NADPH + H+
2-nitrobenzyl alcohol + NADP+
-
-
-
-
r
3-nitrobenzaldehyde + NADPH + H+
3-nitrobenzyl alcohol + NADP+
-
-
-
-
r
4-nitrobenzaldehyde + NADPH
4-nitrobenzyl alcohol + NADP+
benzaldehyde + NADPH + H+
benzyl alcohol + NADP+
-
-
-
-
r
D-aldose + NADPH
L-alditol + NADP+
D-arabinose + NADPH + H+
D-arabinitol + NADP+
-
-
-
-
r
D-galactose + NADPH + H+
D-galactitol + NADP+
-
-
-
-
r
D-galacturonate + NADH + H+
L-galactonate + NAD+
D-galacturonate + NADPH
?
-
-
-
-
r
D-galacturonate + NADPH + H+
L-galactonate + NADP+
D-glucose + NADPH + H+
D-glucitol + NADP+
-
-
-
-
r
D-glucuronate + NADH + H+
D-gulonate + NADH + H+
D-glucuronate + NADPH
L-gulonate + NADP+
D-glucuronate + NADPH + H+
? + NADP+
-
ALR1
-
-
?
D-glucuronate + NADPH + H+
L-gulonate + NADP+
D-glucurono-3,6-lactone + NADPH + H+
L-gulono-1,4-lactone
D-glucuronolactone + NADPH
L-gulonolactone + NADP+
D-glyceraldehyde + NADPH + H+
glycerol + NADP+
D-ribose + NADPH + H+
D-ribitol + NADP+
-
-
-
-
r
D-xylose + NADPH + H+
D-xylitol + NADP+
-
-
-
-
r
DL-glyceraldehyde + NADPH + H+
glycerol + NADP+
-
-
-
-
r
gamma-hydroxybutyrate + NADP+
succinic semialdehyde + NADPH
gamma-hydroxybutyrate + NADP+
succinic semialdehyde + NADPH + H+
-
-
-
-
r
L-gulonate + NADP+
D-glucuronate + NADPH
L-gulonate + NADP+
D-glucuronate + NADPH + H+
-
-
-
-
r
pyridine-3-aldehyde + NADPH
3-hydroxypyridine + NADP+
additional information
?
-
4-nitrobenzaldehyde + NADPH
4-nitrobenzyl alcohol + NADP+
-
2-, and 3-isomer also reduced
-
-
r
4-nitrobenzaldehyde + NADPH
4-nitrobenzyl alcohol + NADP+
-
-
-
-
r
D-aldose + NADPH
L-alditol + NADP+
-
i.e. D-xylose, D-glucose, D-galactose are reduced with 100fold less active than D-glucuronate
-
-
r
D-aldose + NADPH
L-alditol + NADP+
-
-
-
-
r
D-galacturonate + NADH + H+
L-galactonate + NAD+
the enzyme is active on both glucuronic acid and galacturonic acid, with similar substrate specificities (kcat/Km) using the preferred co-substrate NADPH
-
-
?
D-galacturonate + NADH + H+
L-galactonate + NAD+
the enzyme is active on both glucuronic acid and galacturonic acid, with similar substrate specificities (kcat/Km) using the preferred co-substrate NADPH
-
-
?
D-galacturonate + NADPH + H+
L-galactonate + NADP+
the enzyme is active on both glucuronic acid and galacturonic acid, with similar substrate specificities (kcat/Km) using the preferred co-substrate NADPH
-
-
?
D-galacturonate + NADPH + H+
L-galactonate + NADP+
the enzyme is active on both glucuronic acid and galacturonic acid, with similar substrate specificities (kcat/Km) using the preferred co-substrate NADPH
-
-
?
D-glucuronate + NADH + H+
D-gulonate + NADH + H+
the enzyme is active on both glucuronic acid and galacturonic acid, with similar substrate specificities (kcat/Km) using the preferred co-substrate NADPH
-
-
?
D-glucuronate + NADH + H+
D-gulonate + NADH + H+
the enzyme is active on both glucuronic acid and galacturonic acid, with similar substrate specificities (kcat/Km) using the preferred co-substrate NADPH
-
-
?
D-glucuronate + NADPH
L-gulonate + NADP+
-
-
-
-
r
D-glucuronate + NADPH
L-gulonate + NADP+
-
-
-
-
r
D-glucuronate + NADPH
L-gulonate + NADP+
-
catabolism of inositol
-
-
?
D-glucuronate + NADPH
L-gulonate + NADP+
-
-
-
-
r
D-glucuronate + NADPH
L-gulonate + NADP+
-
a step in ascorbic acid biosynthesis, overview
-
-
r
D-glucuronate + NADPH
L-gulonate + NADP+
-
formation of ascorbic acid
-
-
?
D-glucuronate + NADPH + H+
L-gulonate + NADP+
-
-
-
-
r
D-glucuronate + NADPH + H+
L-gulonate + NADP+
-
-
-
-
?
D-glucuronate + NADPH + H+
L-gulonate + NADP+
-
-
-
-
?
D-glucuronate + NADPH + H+
L-gulonate + NADP+
the enzyme is active on both glucuronic acid and galacturonic acid, with similar substrate specificities (kcat/Km) using the preferred co-substrate NADPH
-
-
?
D-glucuronate + NADPH + H+
L-gulonate + NADP+
the enzyme is active on both glucuronic acid and galacturonic acid, with similar substrate specificities (kcat/Km) using the preferred co-substrate NADPH
-
-
?
D-glucurono-3,6-lactone + NADPH + H+
L-gulono-1,4-lactone
-
-
-
?
D-glucurono-3,6-lactone + NADPH + H+
L-gulono-1,4-lactone
-
-
-
?
D-glucuronolactone + NADPH
L-gulonolactone + NADP+
-
-
-
-
r
D-glucuronolactone + NADPH
L-gulonolactone + NADP+
-
-
-
-
r
D-glyceraldehyde + NADPH + H+
glycerol + NADP+
-
-
-
-
r
D-glyceraldehyde + NADPH + H+
glycerol + NADP+
-
-
-
-
r
gamma-hydroxybutyrate + NADP+
succinic semialdehyde + NADPH
-
-
-
-
?
gamma-hydroxybutyrate + NADP+
succinic semialdehyde + NADPH
-
preverably in a coupled reaction in vivo with reduction of D-glucuronate
-
-
?
L-gulonate + NADP+
D-glucuronate + NADPH
-
-
-
-
r
L-gulonate + NADP+
D-glucuronate + NADPH
-
-
-
-
r
L-gulonate + NADP+
D-glucuronate + NADPH
-
-
-
-
r
L-gulonate + NADP+
D-glucuronate + NADPH
-
-
-
-
?
L-gulonate + NADP+
D-glucuronate + NADPH
-
-
-
-
r
pyridine-3-aldehyde + NADPH
3-hydroxypyridine + NADP+
-
-
-
-
r
pyridine-3-aldehyde + NADPH
3-hydroxypyridine + NADP+
-
-
-
-
r
additional information
?
-
-
coupled gamma-hydroxybutyrate oxidation and D-glucuronate reduction
-
-
?
additional information
?
-
-
reduction of aldehyde greatly favored compared to oxidation of alcohol
-
-
?
additional information
?
-
-
broad specificity
-
-
?
additional information
?
-
-
no reaction with gamma-lactones of the substrates
-
-
?
additional information
?
-
-
reduction of D-glyceraldehyde: pro-4R hydrogen is transferred from NADPH, i.e. A-specific, attacks re face of carbonyl group of the D-glyceraldehyde
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
D-glucuronate + NADPH
L-gulonate + NADP+
D-glucuronate + NADPH + H+
? + NADP+
-
ALR1
-
-
?
D-glucuronolactone + NADPH
L-gulonolactone + NADP+
gamma-hydroxybutyrate + NADP+
succinic semialdehyde + NADPH
-
preverably in a coupled reaction in vivo with reduction of D-glucuronate
-
-
?
L-gulonate + NADP+
D-glucuronate + NADPH
D-glucuronate + NADPH
L-gulonate + NADP+
-
-
-
-
r
D-glucuronate + NADPH
L-gulonate + NADP+
-
-
-
-
r
D-glucuronate + NADPH
L-gulonate + NADP+
-
catabolism of inositol
-
-
?
D-glucuronate + NADPH
L-gulonate + NADP+
-
-
-
-
r
D-glucuronate + NADPH
L-gulonate + NADP+
-
a step in ascorbic acid biosynthesis, overview
-
-
r
D-glucuronate + NADPH
L-gulonate + NADP+
-
formation of ascorbic acid
-
-
?
D-glucuronolactone + NADPH
L-gulonolactone + NADP+
-
-
-
-
r
D-glucuronolactone + NADPH
L-gulonolactone + NADP+
-
-
-
-
r
L-gulonate + NADP+
D-glucuronate + NADPH
-
-
-
-
r
L-gulonate + NADP+
D-glucuronate + NADPH
-
-
-
-
r
L-gulonate + NADP+
D-glucuronate + NADPH
-
-
-
-
r
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NADH
clear preference for NADPH as cosubstrate
NADP+
-
-
NADPH
-
-
NADPH
-
reduction of D-glyceraldehyde: pro-4R hydrogen is transferred from NADPH, i.e. A-specific, attacks re face of carbonyl group of the D-glyceraldehyde
NADPH
clear preference for NADPH as cosubstrate
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP-ribose
-
competitive versus NADPH
branched alpha-ketoacids
-
D-galacturonate
reaction with galacturonate displays marked substrate inhibition
L-gulonate
competitive inhibitors in reaction with D-glucuronate
L-gulono-1,4-lactone
competitive inhibitors in reaction with D-glucuronate
menadione
-
competitive versus D-glucuronate
2-mercaptoethanol
-
-
2-mercaptoethanol
-
preincubation of gamma-hydroxybutyrate reductase revealed no inhibitory effect
acetoacetate
-
-
Al 1576
-
-
AL-1567
-
-
alpha-ketoglutarate
-
-
branched alpha-ketoacids
-
-
-
branched alpha-ketoacids
-
-
-
dithiothreitol
-
-
dithiothreitol
-
preincubation of gamma-hydroxybutyrate reductase revealed no inhibitory effect
DL-beta-hydroxybutyrate
-
-
DL-beta-hydroxybutyrate
-
-
hydroxylamine
-
-
iodoacetic acid
-
-
N-ethylmaleimide
-
no exact differentiation between organisms in the reference
N-ethylmaleimide
-
no exact differentiation between organisms in the reference
NaF
-
-
p-chloromercuribenzoate
-
no exact differentiation between organisms in the reference
p-chloromercuribenzoate
-
no exact differentiation between organisms in the reference
p-chloromercuribenzoate
-
-
Phenobarbital
-
-
phenylacetate
-
-
ponalrestat
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
Salicylates
-
-
-
sorbinil
-
-
Tolrestat
-
-
additional information
-
potent inhibitors, i.e. carboxylic and sulfonic acids, bind weakly to the free enzyme but strongly to the enzyme-NADP+-binary complex
-
additional information
-
synthesis and evaluation of acetic acid derivatives of [1,2,4]triazino[4,3-a]benzimidazole, the compounds do not inhibit aldehyde reductase, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Acute Kidney Injury
Metabolic reprogramming by the S-nitroso-CoA reductase system protects against kidney injury.
Anemia
Association between the genetic polymorphisms of the pharmacokinetics of anthracycline drug and myelosuppression in a patient with breast cancer with anthracycline-based chemotherapy.
Ascorbic Acid Deficiency
A novel osteoporosis model with ascorbic acid deficiency in Akr1A1 gene knockout mice.
Astrocytoma
The role of aldehyde reductase AKR1A1 in the metabolism of gamma-hydroxybutyrate in 1321N1 human astrocytoma cells.
Astrocytoma
[Effect of AKR1A1 knock-down on H2;O2; and 4-hydroxynonenal-induced cytotoxicity in human 1321N1 astrocytoma cells].
Breast Neoplasms
Association between the genetic polymorphisms of the pharmacokinetics of anthracycline drug and myelosuppression in a patient with breast cancer with anthracycline-based chemotherapy.
Carcinoma, Hepatocellular
Metabolism of gamma hydroxybutyrate in human hepatoma HepG2 cells by the aldo-keto reductase AKR1A1.
Diabetes Mellitus, Type 2
Activities of aldose reductase, ATPases, and nucleotide concentrations of erythrocytes in patients with type 2 (non-insulin-dependent) diabetes mellitus.
Laryngeal Neoplasms
Increased aldehyde reductase expression mediates acquired radioresistance of laryngeal cancer cells via modulating p53.
Liver Diseases, Alcoholic
Major differences exist in the function and tissue-specific expression of human aflatoxin B1 aldehyde reductase and the principal human aldo-keto reductase AKR1 family members.
Lymphoma, Non-Hodgkin
Genetic Polymorphisms in Oxidative Stress Pathway Genes and Modification of BMI and Risk of Non-Hodgkin Lymphoma.
Neoplasms
Quantitative analysis of the human AKR family members in cancer cell lines using the mTRAQ/MRM approach.
Neoplasms
The role of cytochromes p450 and aldo-keto reductases in prognosis of breast carcinoma patients.
Osteoporosis
A novel osteoporosis model with ascorbic acid deficiency in Akr1A1 gene knockout mice.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.769
2-nitrobenzaldehyde
-
-
0.526
3-Nitrobenzaldehyde
-
-
0.133 - 0.35
4-nitrobenzaldehyde
0.57 - 3.15
D-galacturonate
0.0543 - 9.1
D-glucuronate
7.1
D-glucurono-3,6-lactone
pH 7.5, 37°C, cosubstrate: NADPH
0.69
D-glucuronolactone
-
-
1.671
DL-glyceraldehyde
-
-
0.00045 - 0.0025
gamma-hydroxybutyrate
0.4
NADH
pH 7.5, 37°C, cosubstrate: D-glucuronate
2.6
Pyridine-3-aldehyde
-
-
0.133
4-nitrobenzaldehyde
-
-
0.35
4-nitrobenzaldehyde
-
-
0.57
D-galacturonate
pH 7.5, 37°C, cosubstrate: NADPH, spectrometric assay
0.95
D-galacturonate
pH 7.5, 37°C, cosubstrate: NADPH, HPLC assay
1.96
D-galacturonate
pH 7.5, 37°C, cosubstrate: NADH, spectrometric assay
3.15
D-galacturonate
pH 7.5, 37°C, cosubstrate: NADH, HPLC assay
0.0543
D-glucuronate
-
no exact differentiation between organisms in the reference
0.0543
D-glucuronate
-
no exact differentiation between organisms in the reference
0.0543
D-glucuronate
-
defined as D-glucuronate reductase
0.0543
D-glucuronate
-
defined as D-glucuronate reductase
0.097
D-glucuronate
pH 7.5, 37°C, cosubstrate: NADPH, spectrometric assay
3.34
D-glucuronate
pH 7.5, 37°C, cosubstrate: NADPH, HPLC assay
6.3
D-glucuronate
pH 7.5, 37°C, cosubstrate: NADH, HPLC assay
6.48
D-glucuronate
pH 7.5, 37°C, cosubstrate: NADH, spectrometric assay
0.00045
gamma-hydroxybutyrate
-
coupled reaction of gamma-hydroxybutyrate oxidation and D-glucuronate reduction, brain and kidney
0.00045
gamma-hydroxybutyrate
-
enzyme from brain, D-glucuronate reduction-coupled assay
0.0022
gamma-hydroxybutyrate
-
kidney
0.0022
gamma-hydroxybutyrate
-
enzyme from kidney, uncoupled assay
0.0025
gamma-hydroxybutyrate
-
brain
0.0025
gamma-hydroxybutyrate
-
enzyme from brain, uncoupled assay
2.1
L-gulonate
-
-
0.0014
NADP+
-
coupled reaction of gamma-hydroxybutyrate oxidation and D-glucuronate reduction
0.02
NADP+
-
uncoupled reaction
0.02
NADP+
-
uncoupled reaction
0.0058
NADPH
pH 7.5, 37°C, cosubstrate: D-glucuronate
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
4.5 - 18.5
D-galacturonate
2.3
D-glucurono-3,6-lactone
pH 7.5, 37°C, cosubstrate: NADPH
7.4
NADH
pH 7.5, 37°C, cosubstrate: D-glucuronate
9.6
NADPH
pH 7.5, 37°C, cosubstrate: D-glucuronate
additional information
additional information
-
4.5
D-galacturonate
pH 7.5, 37°C, cosubstrate: NADH, spectrometric assay
8.9
D-galacturonate
pH 7.5, 37°C, cosubstrate: NADPH, spectrometric assay
13.6
D-galacturonate
pH 7.5, 37°C, cosubstrate: NADPH, HPLC assay
18.5
D-galacturonate
pH 7.5, 37°C, cosubstrate: NADH, HPLC assay
1.26
D-glucuronate
pH 7.5, 37°C, cosubstrate: NADH, spectrometric assay
7.6
D-glucuronate
pH 7.5, 37°C, cosubstrate: NADH, HPLC assay
11.9
D-glucuronate
pH 7.5, 37°C, cosubstrate: NADPH, spectrometric assay
13
D-glucuronate
pH 7.5, 37°C, cosubstrate: NADPH, HPLC assay
additional information
additional information
-
0.119 per mM * s, L-gulonate, steady state kinetic
-
additional information
additional information
-
10.82 per mM * s, D-glucuronate, steady state kinetic
-
additional information
additional information
-
1124 per mM * s, NADPH, steady state kinetic
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.19 - 12.3
D-glucuronate
0.32
D-glucurono-3,6-lactone
pH 7.5, 37°C, cosubstrate: NADPH
19
NADH
pH 7.5, 37°C, cosubstrate: D-glucuronate
1655
NADPH
pH 7.5, 37°C, cosubstrate: D-glucuronate
2.3
D-galacturonate
pH 7.5, 37°C, cosubstrate: NADH, spectrometric assay
5.87
D-galacturonate
pH 7.5, 37°C, cosubstrate: NADH, HPLC assay
14.3
D-galacturonate
pH 7.5, 37°C, cosubstrate: NADPH, HPLC assay
16
D-galacturonate
pH 7.5, 37°C, cosubstrate: NADPH, spectrometric assay
0.19
D-glucuronate
pH 7.5, 37°C, cosubstrate: NADH, spectrometric assay
1.2
D-glucuronate
pH 7.5, 37°C, cosubstrate: NADH, HPLC assay
3.89
D-glucuronate
pH 7.5, 37°C, cosubstrate: NADPH, HPLC assay
12.3
D-glucuronate
pH 7.5, 37°C, cosubstrate: NADPH, spectrometric assay
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1.339
-
highly purified enzyme, substrate NADPH
0.0025
-
substrate D-glucuronate, defined as D-glucuronate reductase
0.0025
-
no exact differentiation between organisms in the reference
0.0025
-
substrate D-glucuronate, defined as D-glucuronate reductase
0.0025
-
no exact differentiation between organisms in the reference
additional information
-
-
additional information
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
6 - 7
-
DL-glyceraldehyde
6.2 - 6.6
-
D-glucuronate
7
-
shifted pH-optimum for the coupled reaction of oxidation of gamma-hydroxybutyrate and reduction of D-glucuronate in vitro
8.5
-
substrate L-gulonate or D-glucuronate
9
-
substrate gamma-hydroxybutyrate, at pH 7.0 activity is reduced by 50%
7.5
-
no exact differentiation between organisms in the reference
7.5
-
in vivo for coupled reaction of gamma-hydroxybutyrate oxidation and D-glucuronate reduction
7.5
-
no exact differentiation between organisms in the reference
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
7 - 10
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
38
-
no exact differentiation between organisms in the reference
38
-
no exact differentiation between organisms in the reference
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
UniProt
brenda
-
UniProt
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
albino rats
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
brenda
-
low activity
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
cortex
brenda
-
high activity. Expression is limited to the proximal tubules. Enzyme is present in the 9 week old fetal kidney
brenda
-
high activity. Expression is limited to the proximal tubules and parietal epithelium of Bowman's capsule. the intensity of staining increases with age
brenda
-
-
brenda
-
cortex
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
low activity
brenda
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
brenda
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
36700
-
1 * 36700, SDS-PAGE
33000
-
SDS-PAGE, gel filtration
33000
-
1 * 33000, SDS-PAGE
36000
-
gel filtration
36000
-
2 * 36000, SDS-PAGE, no exact differentiation between organisms in the reference
36000
-
2 * 36000, SDS-PAGE, no exact differentiation between organisms in the reference
60000 - 70000
-
no exact differentiation between organisms in the reference, gel filtration
60000 - 70000
-
no exact differentiation between organisms in the reference, gel filtration
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
dimer
-
2 * 36000, SDS-PAGE, no exact differentiation between organisms in the reference
dimer
-
2 * 36000, SDS-PAGE, no exact differentiation between organisms in the reference
monomer
-
-
monomer
-
1 * 39000, SDS-PAGE
monomer
-
1 * 33000, SDS-PAGE
monomer
-
1 * 36700, SDS-PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
5 - 10.5
-
irreversible loss of activity below pH 5.0 and above pH 11
286149
8
-
no exact differentiation between organisms in the reference
286146
8
-
rapid decrease of activity above pH 8.0
286146
8
-
no exact differentiation between organisms in the reference
286146
8
-
rapid decrease of activity above pH 8.0
286146
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
50
-
15 min, complete inactivation, ammonium sulfate fraction
40
1 h, complete unfolding
40
-
15 min, 50% loss of activity, ammonium sulfate fraction
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EDTA 1 mM protects against heat denaturation at 40°C
-
lyophilization destroys activity
-
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
no exact differentiation between organisms in the reference
-
-
no exact differentiation between organisms in the reference
-
no exact differentiation between organisms in the reference
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
expression in Escherichia coli
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Flynn, T.G.; Cromlish, J.A.; Davidson, W.S.
Aldehyde reductase (L-hexonate: NADP dehydrogenase) from pig kidney
Methods Enzymol.
89
501-506
1982
Sus scrofa
brenda
Bublitz, C.; Lehninger, A.L.
Ascorbic acid synthesis in animal tissue I. TPN-L-gulonate dehydrogenase
Methods Enzymol.
6
334-337
1963
Sus scrofa
-
brenda
York, J.L.; Grollman, A.P.; Bublitz, C.
TPN-L-gulonate dehydrogenase
Biochim. Biophys. Acta
47
298-306
1961
Sus scrofa
brenda
Kaufman, E.E.; Nelson, T.
Kinetics of coupled gamma-hydroxybutyrate oxidation and D-glucuronate reduction by an NADP+-dependent oxidoreductase
J. Biol. Chem.
256
6890-6894
1981
Mesocricetus auratus
brenda
Tulsiani, D.R.P.; Touster, O.
Resolution and partial characterization of two aldehyde reductases of mammalian liver
J. Biol. Chem.
252
2545-2550
1977
Mus musculus
brenda
Sivak, A.; Hoffmann-Ostenhof, O.
Enzymes of meso-inositol catabolism in the yeast Schwanniomyces occidentalis
Biochim. Biophys. Acta
53
426-428
1961
Schwanniomyces occidentalis
brenda
Poulsom, R.
Inhibition of hexonate dehydrogenase and aldose reductase from bovine retina by sorbinil, statil, M79175 and valproate
Biochem. Pharmacol.
35
2955-2959
1986
Bos taurus
brenda
Goode, D.; Lewis, M.E.; Crabbe, M.J.C.
Accumulation of xylitol in the mammalian lens is realted to glucoronate metabolism
FEBS Lett.
395
174-178
1996
Bos taurus, Homo sapiens, Rattus norvegicus
brenda
Kaufman, E.E.; Nelson, T.
An overview of gamma-hydroxybutyrate catabolism: the role of the cytosolic NADP+-dependent oxidoreductase EC 1.1.1.19 and of a mitochondrial hydroxyacid-oxoacid transhydrogenase in the initial, rate-limiting step in this pathway
Neurochem. Res.
16
965-974
1991
Homo sapiens, Mesocricetus auratus, Rattus norvegicus
brenda
Sato, S.; Kador, P.F.
Human kidney aldose and aldehyde reductases
J. Diabetes Complicat.
7
179-187
1993
Canis lupus familiaris, Homo sapiens, Rattus norvegicus
brenda
Bhatnagar, A.; Das, B.; Liu, S.Q.; Srivastava, S.K.
Human liver aldehyde reductase: pH dependence of steady-state kinetic parameters
Arch. Biochem. Biophys.
287
329-336
1991
Homo sapiens
brenda
Shinoda, M.; Mori, S.; Shintani, S.; Ishikura, S.; Hara, A.
Inhibition of human aldehyde reductase by drugs for testing the function of liver and kidney
Biol. Pharm. Bull.
22
741-744
1999
Homo sapiens
brenda
Barski, O.A.; Papusha, V.Z.; Ivanova, M.M.; Rudman, D.M.; Finegold, M.J.
Developmental expression and function of aldehyde reductase in proximal tubules of the kidney
Am. J. Physiol. Renal Physiol.
289
F200-F207
2005
Homo sapiens, Mus musculus
brenda
Linster, C.L.; Van Schaftingen, E.
Vitamin C. Biosynthesis, recycling and degradation in mammals
FEBS J.
274
1-22
2007
Homo sapiens, Rattus norvegicus
brenda
Sahoo, P.K.; Behera, P.
Synthesis and biological evaluation of [1,2,4]triazino[4,3-a] benzimidazole acetic acid derivatives as selective aldose reductase inhibitors
Eur. J. Med. Chem.
45
909-914
2010
Rattus norvegicus
brenda
Wagschal, K.; Jordan, D.B.; Hart-Cooper, W.M.; Chan, V.J.
Penicillium camemberti galacturonate reductase C-1 oxidation/reduction of uronic acids and substrate inhibition mitigation by aldonic acids
Int. J. Biol. Macromol.
153
1090-1098
2020
Penicillium camemberti (A0A0G4NUS2), Penicillium camemberti, Penicillium camemberti FM 013 (A0A0G4NUS2)
brenda
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