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Literature summary for 1.1.1.298 extracted from

  • Yao, T.; Xu, L.; Ying, H.; Huang, H.; Yan, M.
    The catalytic property of 3-hydroxyisobutyrate dehydrogenase from Bacillus cereus on 3-hydroxypropionate (2009), Appl. Biochem. Biotechnol., 160, 694-703.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli strain BL21 Bacillus cereus
MmsB gene, overexpression in Escherichia coli strain BL21, subcloning in strain DH5alpha Bacillus cereus

Inhibitors

Inhibitors Comment Organism Structure
additional information not inhibitory: EDTA and ethylene glykol, up to 0.2 mM Bacillus cereus
Zn 0.2 mM, 60% inhibition Bacillus cereus
Zn2+ 60% inhibition at 0.2 mM Bacillus cereus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information steady-state kinetics, overview Bacillus cereus
additional information
-
additional information steady-state kinetic analysis, overview Bacillus cereus
0.25
-
NADP+ pH 8.5, 37°C Bacillus cereus
0.25
-
NADP+ pH 8.5, 37°C, recombinant enzyme Bacillus cereus
2.4
-
NAD+ pH 8.5, 37°C Bacillus cereus
2.4
-
NAD+ pH 8.5, 37°C, recombinant enzyme Bacillus cereus
16.8
-
3-hydroxypropionate pH 8.5, 37°C Bacillus cereus
16.8
-
3-hydroxypropanoate pH 8.5, 37°C Bacillus cereus
16.8
-
3-hydroxypropionate pH 8.5, 37°C, recombinant enzyme Bacillus cereus

Metals/Ions

Metals/Ions Comment Organism Structure
additional information no metal ion requirement Bacillus cereus
additional information up to 0.2 mM, no effect on activity: MnSO4, CuSO4, CaCl2, MgSO4, and FeSO4 Bacillus cereus
additional information no metal ion requirement, no effects by 0.2 mM MnSO4, CuSO4, CaCl2, MgSO4, and FeSO4 Bacillus cereus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
32000
-
x * 32000, SDS-PAGE Bacillus cereus
32000
-
x * 32000, recombinant enzyme, SDS-PAGE Bacillus cereus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3-hydroxypropanoate + NADP+ Bacillus cereus
-
3-oxopropanoate + NADPH + H+
-
r
3-hydroxypropanoate + NADP+ Bacillus cereus
-
malonate semialdehyde + NADPH + H+
-
r
additional information Bacillus cereus MmsB from Bacillus cereus exhibits 3-hydroxyisobutyrate dehydrogenase, EC 1.1.1.31, as well as 3-hydroxypropionate dehydrogenase activity ?
-
?
additional information Bacillus cereus the enzyme is a 3-hydroxyisobutyrate dehydrogenase, 3-HIBADH, EC1.1.1.31, that also utilizes 3-hydroxypropionate as substrate. It catalyzes not only the oxidation of 3-hydroxyisobutyrate but also of L-serine, D-threonine, and other 3-hydroxyacid derivatives ?
-
?

Organism

Organism UniProt Comment Textmining
Bacillus cereus
-
gene MmsB
-
Bacillus cereus
-
-
-
Bacillus cereus
-
MmsB gene
-
Bacillus cereus ATCC 14579
-
gene MmsB
-
Bacillus cereus ATCC 14579
-
-
-
Bacillus cereus ATCC 14579
-
MmsB gene
-

Purification (Commentary)

Purification (Comment) Organism
native enzyme 100fold by ammonium sulfate fractionation, and hydrophobic interaction and anion exchange chromatography Bacillus cereus
recombinant enzyme from Escherichia coli strain BL21 96fold by ammonium sulfate fractionation, hydrophobic interaction and anion exchange chromatography, followed by ultrafiltration Bacillus cereus

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
8.7
-
pH 8.5, 37°C Bacillus cereus
8.8
-
purified recombinant enzyme, pH 8.5, 37°C Bacillus cereus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-hydroxypropanoate + NAD+
-
Bacillus cereus malonate semialdehyde + NADH + H+
-
r
3-hydroxypropanoate + NAD+
-
Bacillus cereus malonate-semialdehyde + NADH + H+
-
?
3-hydroxypropanoate + NADP+ 3-hydroxyisobutyrate dehydrogenase, EC 1.1.1.31, additionally exhibits 3-hydroxypropionate dehydrogenase activity Bacillus cereus malonate-semialdehyde + NADPH + H+
-
?
3-hydroxypropanoate + NADP+
-
Bacillus cereus 3-oxopropanoate + NADPH + H+
-
r
3-hydroxypropanoate + NADP+
-
Bacillus cereus malonate semialdehyde + NADPH + H+
-
r
3-hydroxypropanoate + NADP+
-
Bacillus cereus malonate semialdehyde + NADPH + H+ spectrophotometric product determination r
additional information MmsB from Bacillus cereus exhibits 3-hydroxyisobutyrate dehydrogenase, EC 1.1.1.31, as well as 3-hydroxypropionate dehydrogenase activity Bacillus cereus ?
-
?
additional information the enzyme is a 3-hydroxyisobutyrate dehydrogenase, 3-HIBADH, EC1.1.1.31, that also utilizes 3-hydroxypropionate as substrate. It catalyzes not only the oxidation of 3-hydroxyisobutyrate but also of L-serine, D-threonine, and other 3-hydroxyacid derivatives Bacillus cereus ?
-
?

Subunits

Subunits Comment Organism
? x * 32000, SDS-PAGE Bacillus cereus
? x * 32000, recombinant enzyme, SDS-PAGE Bacillus cereus

Synonyms

Synonyms Comment Organism
3-HIBADH
-
Bacillus cereus
3-hydroxyisobutyrate dehydrogenase
-
Bacillus cereus
3-hydroxypropionate dehydrogenase
-
Bacillus cereus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
-
Bacillus cereus
37
-
assay at Bacillus cereus

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
35 45 90% of maximal activity within this range Bacillus cereus
35 45 activity range Bacillus cereus
35 45 more than 90% of maximum activity Bacillus cereus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
37 45 purified enzyme, over 90% activity remaining after 30 min Bacillus cereus
45
-
30 min, stable Bacillus cereus
45
-
30 min, purified enzyme, completely stable Bacillus cereus
55
-
3 min, about 40% residual activity Bacillus cereus
55
-
3 min, purified enzyme, significant denaturation and inactivation Bacillus cereus
55
-
purified enzyme, 30 min, partial denaturation Bacillus cereus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.21
-
3-hydroxypropionate pH 8.5, 37°C Bacillus cereus
0.21
-
3-hydroxypropanoate pH 8.5, 37°C Bacillus cereus
0.21
-
3-hydroxypropionate pH 8.5, 37°C, recombinant enzyme Bacillus cereus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.8
-
-
Bacillus cereus
8.8 9
-
Bacillus cereus

pH Range

pH Minimum pH Maximum Comment Organism
7 10 activity range Bacillus cereus
8.2
-
about 30% of maximum acticity Bacillus cereus
9
-
about 65% of maximum activity Bacillus cereus

Cofactor

Cofactor Comment Organism Structure
NAD+ NADP+ is preferred over NAD+ Bacillus cereus
NAD+ more active with NADP+ than NAD+ Bacillus cereus
NADH
-
Bacillus cereus
NADP+
-
Bacillus cereus
NADP+ NADP+ is preferred over NAD+ Bacillus cereus
NADP+ more active with NADP+ than NAD+ Bacillus cereus
NADPH
-
Bacillus cereus

General Information

General Information Comment Organism
physiological function the enzyme is a 3-hydroxyisobutyrate dehydrogenase, 3-HIBADH, EC1.1.1.31, that also utilizes 3-hydroxypropionate as substrate. It catalyzes not only the oxidation of 3-hydroxyisobutyrate but also of L-serine, D-threonine, and other 3-hydroxyacid derivatives. 3-HIBADH may have the similar function to 3-hydroxypropionate dehydrogenase in vivo and be the key enzyme in an autotrophic CO2 fixation pathway, the 3-hydroxypropionate cycle Bacillus cereus

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.0125
-
3-hydroxypropionate pH 8.5, 37°C Bacillus cereus
0.0125
-
3-hydroxypropanoate pH 8.5, 37°C Bacillus cereus
0.0125
-
3-hydroxypropionate pH 8.5, 37°C, recombinant enzyme Bacillus cereus