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Information on EC 1.1.1.19 - glucuronate reductase
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EC Tree
1.1.1.19 glucuronate reductaseIUBMB Comments
Also reduces D-galacturonate. May be identical with EC 1.1.1.2 [alcohol dehydrogenase (NADP+)].
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Word Map
- 1.1.1.19
-
aldo-keto
- aldose
- sorbinil
- akr1b1s
- o-quinones
- alrestatin
-
1.1.1.21
- daunorubicinol
-
trans-dihydrodiols
- statil
-
akr7a2
- dl-glyceraldehyde
-
3alpha-hydroxysteroid
-
diol-epoxide
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, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AKR1A1
aldehyde reductase
aldehyde reductase II
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D-glucuronate dehydrogenase
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D-glucuronate reductase
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D-glucuronic reductase
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-
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galacturonate oxidoreductase
hexonate dehydrogenase
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L-glucuronate reductase
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-
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L-gulonate NAD-3-oxidoreductase
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L-hexonate:NADP dehydrogenase
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NADP-L-gulonate dehydrogenase
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PcGOR
TPN l-hexonate dehydrogenase
TPN-L-gulonate dehydrogenase
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additional information
aldehyde reductase
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-
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additional information
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the enzyme belongs to the aldo-keto reductase superfamily
additional information
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the enzyme belongs to the aldo-keto reductase superfamily
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-gulonate + NADP+ = D-glucuronate + NADPH + H+
also reduces D-galacturonate
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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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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
reduction
oxidation
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pH dependent reaction mechanism
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oxidation
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ordered bi bi mechanism
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reduction
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pH dependent reaction mechanism
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reduction
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ordered bi bi mechanism
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
L-gulonate:NADP+ 6-oxidoreductase
Also reduces D-galacturonate. May be identical with EC 1.1.1.2 [alcohol dehydrogenase (NADP+)].
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CAS REGISTRY NUMBER
COMMENTARY
9028-29-9
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-nitrobenzaldehyde + NADPH
4-nitrobenzyl alcohol + NADP+
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2-, and 3-isomer also reduced
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r
D-aldose + NADPH
L-alditol + NADP+
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i.e. D-xylose, D-glucose, D-galactose are reduced with 100fold less active than D-glucuronate
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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
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-
?
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
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-
?
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
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-
?
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
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-
?
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
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-
?
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
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-
?
D-glucuronate + NADPH
L-gulonate + NADP+
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r
D-glucuronate + NADPH
L-gulonate + NADP+
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a step in ascorbic acid biosynthesis, overview
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r
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
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-
?
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
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-
?
D-glucurono-3,6-lactone + NADPH + H+
L-gulono-1,4-lactone
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-
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?
D-glucurono-3,6-lactone + NADPH + H+
L-gulono-1,4-lactone
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-
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?
gamma-hydroxybutyrate + NADP+
succinic semialdehyde + NADPH
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-
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?
gamma-hydroxybutyrate + NADP+
succinic semialdehyde + NADPH
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preverably in a coupled reaction in vivo with reduction of D-glucuronate
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?
L-gulonate + NADP+
D-glucuronate + NADPH
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r
additional information
?
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coupled gamma-hydroxybutyrate oxidation and D-glucuronate reduction
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?
additional information
?
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reduction of aldehyde greatly favored compared to oxidation of alcohol
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?
additional information
?
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no reaction with gamma-lactones of the substrates
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?
additional information
?
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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
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?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
gamma-hydroxybutyrate + NADP+
succinic semialdehyde + NADPH
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preverably in a coupled reaction in vivo with reduction of D-glucuronate
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-
?
D-glucuronate + NADPH
L-gulonate + NADP+
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r
D-glucuronate + NADPH
L-gulonate + NADP+
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a step in ascorbic acid biosynthesis, overview
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r
L-gulonate + NADP+
D-glucuronate + NADPH
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-
-
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r
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADPH
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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
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
2-mercaptoethanol
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preincubation of gamma-hydroxybutyrate reductase revealed no inhibitory effect
dithiothreitol
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preincubation of gamma-hydroxybutyrate reductase revealed no inhibitory effect
N-ethylmaleimide
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no exact differentiation between organisms in the reference
p-chloromercuribenzoate
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no exact differentiation between organisms in the reference
p-chloromercuribenzoate
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no exact differentiation between organisms in the reference
additional information
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potent inhibitors, i.e. carboxylic and sulfonic acids, bind weakly to the free enzyme but strongly to the enzyme-NADP+-binary complex
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additional information
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synthesis and evaluation of acetic acid derivatives of [1,2,4]triazino[4,3-a]benzimidazole, the compounds do not inhibit aldehyde reductase, overview
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
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.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
7.1
D-glucurono-3,6-lactone
pH 7.5, 37°C, cosubstrate: NADPH
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
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no exact differentiation between organisms in the reference
0.0543
D-glucuronate
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no exact differentiation between organisms in the reference
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
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coupled reaction of gamma-hydroxybutyrate oxidation and D-glucuronate reduction, brain and kidney
0.00045
gamma-hydroxybutyrate
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enzyme from brain, D-glucuronate reduction-coupled assay
0.0014
NADP+
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coupled reaction of gamma-hydroxybutyrate oxidation and D-glucuronate reduction