Information on EC 1.1.1.59 - 3-hydroxypropionate dehydrogenase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
1.1.1.59
-
RECOMMENDED NAME
GeneOntology No.
3-hydroxypropionate dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
3-hydroxypropanoate + NAD+ = 3-oxopropanoate + NADH + H+
show the reaction diagram
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
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reduction
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
acrylate degradation
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-
beta-alanine biosynthesis II
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propanoyl-CoA degradation II
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alanine metabolism
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beta-Alanine metabolism
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Propanoate metabolism
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
3-hydroxypropanoate:NAD+ oxidoreductase
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CAS REGISTRY NUMBER
COMMENTARY hide
9028-59-5
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
; MmsB gene
-
-
Manually annotated by BRENDA team
MmsB gene
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
no activity in Desulfovibrio carbinolicus
-
-
-
Manually annotated by BRENDA team
no activity in Desulfovibrio fructosovorans
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-hydroxyisobutyrate + NAD+
methylmalonate semialdehyde + NADH + H+
show the reaction diagram
-
-
-
-
r
3-hydroxypropanoate + NAD+
3-oxopropanoate + NADH + H+
show the reaction diagram
3-hydroxypropanoate + NAD+
malonate semialdehyde + NADH + H+
show the reaction diagram
-
-
-
-
r
3-hydroxypropanoate + NADP+
malonate semialdehyde + NADPH + H+
show the reaction diagram
-
-
-
-
r
additional information
?
-
-
MmsB from Bacillus cereus exhibits 3-hydroxyisobutyrate dehydrogenase, EC 1.1.1.31, as well as 3-hydroxypropionate dehydrogenase activity
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-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3-hydroxypropanoate + NAD+
3-oxopropanoate + NADH + H+
show the reaction diagram
additional information
?
-
-
MmsB from Bacillus cereus exhibits 3-hydroxyisobutyrate dehydrogenase, EC 1.1.1.31, as well as 3-hydroxypropionate dehydrogenase activity
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
no metal ion requirement
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ZnCl2
-
0.2 mM, 60% inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
16.8 - 20
3-hydroxypropanoate
0.34 - 2.4
NAD+
0.25
NADP+
-
pH 8.5, 37C
additional information
additional information
-
steady-state kinetic analysis, overview
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.21
3-hydroxypropanoate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0125
3-hydroxypropanoate
4480
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.77
-
pH 8.5, 37C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.8 - 9
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 10
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; activity range
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35 - 45
-
90% of maximal activity within this range
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
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-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
-
30 min, purified enzyme, completely stable; stable at 45C for 30 min, about 40% activity after 3 min at 55C
55
-
3 min, purified enzyme, significant denaturation and inactivation
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
several weeks, frozen
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, hydrophobic interaction chromatography (Phenyl-Sepharose), anion exchange chromatography; native enzyme 100fold by ammonium sulfate fractionation, and hydrophobic interaction and anion exchange chromatography
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partially
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 (DE3); MmsB gene, overexpression in Escherichia coli strain BL21, subcloning in strain DH5alpha
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