BRENDA - Enzyme Database show
show all sequences of 1.1.1.31

Characterization of 3-hydroxyisobutyrate dehydrogenase, HIBADH, as a sperm-motility marker

Tasi, Y.C.; Chao, H.C.; Chung, C.L.; Liu, X.Y.; Lin, Y.M.; Liao, P.C.; Pan, H.A.; Chiang, H.S.; Kuo, P.L.; Lin, Y.H.; J. Assist. Reprod. Genet. 30, 505-512 (2013)

Data extracted from this reference:

Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
mitochondrion
-
Homo sapiens
5739
-
additional information
the enzyme is located at the mid-piece (a specialized development from the mitochondria) of elongating, elongated, and mature sperm
Homo sapiens
-
-
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
3-hydroxy-2-methylpropanoate + NAD+
Homo sapiens
-
2-methyl-3-oxopropanoate + NADH + H+
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Homo sapiens
-
-
-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
cerebellum
-
Homo sapiens
-
heart
-
Homo sapiens
-
kidney
-
Homo sapiens
-
liver
-
Homo sapiens
-
additional information
HIBADH is downregulated in low-motility sperm, and is enriched expressed during human spermiogenesis, quantitative RT-PCR expression analysis, overview
Homo sapiens
-
neuronal cell
-
Homo sapiens
-
placenta
-
Homo sapiens
-
skeletal muscle
-
Homo sapiens
-
sperm
elongating, elongated, and mature sperm
Homo sapiens
-
testis
-
Homo sapiens
-
uterus
-
Homo sapiens
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3-hydroxy-2-methylpropanoate + NAD+
-
722472
Homo sapiens
2-methyl-3-oxopropanoate + NADH + H+
-
-
-
?
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
20
-
assay at
Homo sapiens
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
10
-
assay at
Homo sapiens
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
-
Homo sapiens
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
-
Homo sapiens
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
mitochondrion
-
Homo sapiens
5739
-
additional information
the enzyme is located at the mid-piece (a specialized development from the mitochondria) of elongating, elongated, and mature sperm
Homo sapiens
-
-
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
3-hydroxy-2-methylpropanoate + NAD+
Homo sapiens
-
2-methyl-3-oxopropanoate + NADH + H+
-
-
?
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
cerebellum
-
Homo sapiens
-
heart
-
Homo sapiens
-
kidney
-
Homo sapiens
-
liver
-
Homo sapiens
-
additional information
HIBADH is downregulated in low-motility sperm, and is enriched expressed during human spermiogenesis, quantitative RT-PCR expression analysis, overview
Homo sapiens
-
neuronal cell
-
Homo sapiens
-
placenta
-
Homo sapiens
-
skeletal muscle
-
Homo sapiens
-
sperm
elongating, elongated, and mature sperm
Homo sapiens
-
testis
-
Homo sapiens
-
uterus
-
Homo sapiens
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3-hydroxy-2-methylpropanoate + NAD+
-
722472
Homo sapiens
2-methyl-3-oxopropanoate + NADH + H+
-
-
-
?
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
20
-
assay at
Homo sapiens
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
10
-
assay at
Homo sapiens
Expression
Organism
Commentary
Expression
Homo sapiens
HIBADH is downregulated in low-motility sperm, and is enriched expressed during human spermiogenesis
down
Homo sapiens
HIBADH is downregulated in low-motility sperm, and is enriched expressed during human spermiogenesis
up
General Information
General Information
Commentary
Organism
evolution
3-hydroxyisobutyrate dehydrogenase belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donors with NAD+ or NADP+ acceptors
Homo sapiens
additional information
enzyme activity of HIBADH in spermatozoa from patients with asthenozoospermia is reduced compared to controls
Homo sapiens
physiological function
3-hydroxyisobutyrate dehydrogenase is one of the critical enzymes generating glucose by metabolizing amino acids in the gluconeogenesis pathway. It participates in valine, leucine, and isoleucine degradation and is a central metabolic enzyme in the valine catabolic pathway. The enzyme plays an important role in regulating sperm motility and may serve as a novel sperm-motility marker
Homo sapiens
General Information (protein specific)
General Information
Commentary
Organism
evolution
3-hydroxyisobutyrate dehydrogenase belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donors with NAD+ or NADP+ acceptors
Homo sapiens
additional information
enzyme activity of HIBADH in spermatozoa from patients with asthenozoospermia is reduced compared to controls
Homo sapiens
physiological function
3-hydroxyisobutyrate dehydrogenase is one of the critical enzymes generating glucose by metabolizing amino acids in the gluconeogenesis pathway. It participates in valine, leucine, and isoleucine degradation and is a central metabolic enzyme in the valine catabolic pathway. The enzyme plays an important role in regulating sperm motility and may serve as a novel sperm-motility marker
Homo sapiens
Expression (protein specific)
Organism
Commentary
Expression
Homo sapiens
HIBADH is downregulated in low-motility sperm, and is enriched expressed during human spermiogenesis
down
Homo sapiens
HIBADH is downregulated in low-motility sperm, and is enriched expressed during human spermiogenesis
up
Other publictions for EC 1.1.1.31
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)
737620
Park
Structural and biochemical cha ...
Bacillus cereus
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474
522-527
2016
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1
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1
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2
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1
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737911
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3
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11
5
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2
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3
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11
1
1
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5
1
1
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5
5
722472
Tasi
Characterization of 3-hydroxyi ...
Homo sapiens
J. Assist. Reprod. Genet.
30
505-512
2013
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11
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1
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1
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1
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2
3
3
2
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739465
Zhou
Cloning, expression and charac ...
Pseudomonas denitrificans, Pseudomonas denitrificans ATCC 13867
PLoS ONE
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3
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1
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8
6
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2
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6
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1
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10
1
1
1
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6
1
1
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1
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3
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1
1
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8
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6
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2
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1
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10
1
1
1
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6
1
1
-
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-
-
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6
6
695710
Yao
The catalytic property of 3-hy ...
Bacillus cereus, Bacillus cereus ATCC 14579, Bacillus cereus ATCC14579
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694-703
2009
1
1
1
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-
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3
3
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1
1
9
-
10
-
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1
-
-
-
3
1
18
1
1
1
1
1
2
1
-
6
-
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1
1
1
6
-
-
-
-
3
-
3
-
1
1
9
-
-
-
1
-
-
3
1
18
1
1
1
1
1
2
1
-
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-
1
1
-
1
1
688515
Murin
Expression of 3-hydroxyisobuty ...
Rattus norvegicus
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670284
Loupatty
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Homo sapiens
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1
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655051
Chowdhury
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Pseudomonas putida, Pseudomonas putida E23
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2
1
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286550
Hawes
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2
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2
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3
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1
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2
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286551
Chowdhury
3-Hydroxyisobutyrate dehydroge ...
Candida rugosa, Oryctolagus cuniculus, Pseudomonas putida, Pseudomonas putida E23
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60
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7
10
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4
3
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7
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1
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1
2
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10
3
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3
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3
3
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3
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7
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10
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4
3
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1
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1
2
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10
3
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3
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3
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286552
Hawes
Structural and mechanistic asp ...
Rattus norvegicus
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8
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8
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1
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286544
Rougraff
Purification and characterizat ...
Oryctolagus cuniculus
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1988
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2
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3
1
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1
1
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2
1
1
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286523
Worral
3-Hydroxyisobutyrate dehydroge ...
Rhodobacter sphaeroides
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2
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4
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286546
Hasegawa
-
Distribution in organisms and ...
Bos taurus, Candida parapsilosis, Candida rugosa, Corynebacterium hydrocarbons, Endomyces reessii, Micrococcus flavus, Micrococcus luteus, Nocardia lyena, Oryctolagus cuniculus, Pseudomonas aeruginosa, Pseudomonas dacunhae, Rhodotorula mucilaginosa, Sus scrofa, Trichosporon aculeatum, Tsukamurella paurometabola
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16
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16
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16
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286547
Hasegawa
-
Purification, crystallization ...
Candida rugosa
Agric. Biol. Chem.
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1981
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1
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286548
De Paul Marshall
Regulation of valine catabolis ...
Pseudomonas putida
J. Bacteriol.
110
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1972
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286549
Robinson
The purification and propertie ...
Sus scrofa
J. Biol. Chem.
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1956
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2
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1
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