BRENDA - Enzyme Database show
show all sequences of 1.1.1.61

Metabolite profiling reveals YihU as a novel hydroxybutyrate dehydrogenase for alternative succinic semialdehyde metabolism in Escherichia coli

Saito, N.; Robert, M.; Kochi, H.; Matsuo, G.; Kakazu, Y.; Soga, T.; Tomita, M.; J. Biol. Chem. 284, 16442-16451 (2009)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expressed as a histidine-tagged recombinant protein in Escherichia coli
Escherichia coli
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1
-
3-hydroxypropane sulfonate
; in 100 mM Tris-HCl buffer (pH 8.8), at 37°C
Escherichia coli
4.3
-
Succinic semialdehyde
; in 100 mM MOPS-KOH buffer (pH 7.2), at 37°C
Escherichia coli
9
-
methylglyoxal
; in 100 mM Tris-HCl buffer (pH 8.8), at 37°C
Escherichia coli
102
-
4-hydroxybutyrate
-
Escherichia coli
102
-
gamma-hydroxybutyrate
in 100 mM Tris-HCl buffer (pH 8.8), at 37°C
Escherichia coli
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
additional information
no significant differences in the activity are observed when using different divalent metals (Mg2+, Mn2+, Ca2+, Co2+, and Zn2+)
Escherichia coli
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
31154
-
4 * 31154, calculated from amino acid sequence
Escherichia coli
143000
-
gel filtration; gel filtration
Escherichia coli
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
gamma-hydroxybutyrate + NAD+
Escherichia coli
-
succinic semialdehyde + NADH + H+
-
-
r
succinic semialdehyde + NADH + H+
Escherichia coli
succinic semialdehyde is the preferred substrate
gamma-hydroxybutyrate + NAD+
-
-
r
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
-
-
-
Escherichia coli
P0A9V8
strain K12 BW25113
-
Escherichia coli K12 BW25113
P0A9V8
strain K12 BW25113
-
Purification (Commentary)
Commentary
Organism
purified using cobalt-based immobilized TALON metal affinity chromatography resins with a gravity-flow column
Escherichia coli
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.062
-
substrate: gamma-hydroxybutyrate
Escherichia coli
0.067
-
substrate: methylglyoxal
Escherichia coli
0.2
-
substrate: succinic semialdehyde
Escherichia coli
9
-
substrate: 3-hydroxypropane sulfonate
Escherichia coli
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3-hydroxypropane sulfonate + NAD+
-
698903
Escherichia coli
? + NADH
-
-
-
?
3-hydroxypropane sulfonate + NAD+
-
698903
Escherichia coli K12 BW25113
? + NADH
-
-
-
?
3-hydroxypropane sulfonate + NAD+
-
698903
Escherichia coli
? + NADH + H+
-
-
-
r
gamma-hydroxybutyrate + NAD+
-
698903
Escherichia coli
succinic semialdehyde + NADH + H+
-
-
-
r
methylglyoxal + NAD+
-
698903
Escherichia coli
? + NADH
-
-
-
?
methylglyoxal + NAD+
-
698903
Escherichia coli K12 BW25113
? + NADH
-
-
-
?
methylglyoxal + NAD+
-
698903
Escherichia coli
? + NADH + H+
-
-
-
r
additional information
no activity with D-glycerate and 3-hydroxypropanoate
698903
Escherichia coli
?
-
-
-
-
succinic semialdehyde + NADH + H+
-
698903
Escherichia coli
4-hydroxybutyrate + NAD+
-
-
-
r
succinic semialdehyde + NADH + H+
-
698903
Escherichia coli K12 BW25113
4-hydroxybutyrate + NAD+
-
-
-
r
succinic semialdehyde + NADH + H+
succinic semialdehyde is the preferred substrate
698903
Escherichia coli
gamma-hydroxybutyrate + NAD+
-
-
-
r
Subunits
Subunits
Commentary
Organism
homotetramer
4 * 31154, calculated from amino acid sequence
Escherichia coli
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
-
Escherichia coli
NADH
; the NADH-dependent succinic semialdehyde reductase activity is 4fold higher than that with NADPH
Escherichia coli
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed as a histidine-tagged recombinant protein in Escherichia coli
Escherichia coli
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
-
Escherichia coli
NADH
the NADH-dependent succinic semialdehyde reductase activity is 4fold higher than that with NADPH
Escherichia coli
NADH
-
Escherichia coli
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1
-
3-hydroxypropane sulfonate
in 100 mM Tris-HCl buffer (pH 8.8), at 37°C
Escherichia coli
1
-
3-hydroxypropane sulfonate
-
Escherichia coli
4.3
-
Succinic semialdehyde
in 100 mM MOPS-KOH buffer (pH 7.2), at 37°C
Escherichia coli
4.3
-
Succinic semialdehyde
-
Escherichia coli
9
-
methylglyoxal
in 100 mM Tris-HCl buffer (pH 8.8), at 37°C
Escherichia coli
9
-
methylglyoxal
-
Escherichia coli
102
-
4-hydroxybutyrate
-
Escherichia coli
102
-
gamma-hydroxybutyrate
in 100 mM Tris-HCl buffer (pH 8.8), at 37°C
Escherichia coli
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
additional information
no significant differences in the activity are observed when using different divalent metals (Mg2+, Mn2+, Ca2+, Co2+, and Zn2+)
Escherichia coli
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
31154
-
4 * 31154, calculated from amino acid sequence
Escherichia coli
143000
-
gel filtration
Escherichia coli
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
gamma-hydroxybutyrate + NAD+
Escherichia coli
-
succinic semialdehyde + NADH + H+
-
-
r
succinic semialdehyde + NADH + H+
Escherichia coli
succinic semialdehyde is the preferred substrate
gamma-hydroxybutyrate + NAD+
-
-
r
Purification (Commentary) (protein specific)
Commentary
Organism
purified using cobalt-based immobilized TALON metal affinity chromatography resins with a gravity-flow column
Escherichia coli
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.062
-
substrate: gamma-hydroxybutyrate
Escherichia coli
0.067
-
substrate: methylglyoxal
Escherichia coli
0.2
-
substrate: succinic semialdehyde
Escherichia coli
9
-
substrate: 3-hydroxypropane sulfonate
Escherichia coli
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3-hydroxypropane sulfonate + NAD+
-
698903
Escherichia coli
? + NADH
-
-
-
?
3-hydroxypropane sulfonate + NAD+
-
698903
Escherichia coli K12 BW25113
? + NADH
-
-
-
?
3-hydroxypropane sulfonate + NAD+
-
698903
Escherichia coli
? + NADH + H+
-
-
-
r
gamma-hydroxybutyrate + NAD+
-
698903
Escherichia coli
succinic semialdehyde + NADH + H+
-
-
-
r
methylglyoxal + NAD+
-
698903
Escherichia coli
? + NADH
-
-
-
?
methylglyoxal + NAD+
-
698903
Escherichia coli K12 BW25113
? + NADH
-
-
-
?
methylglyoxal + NAD+
-
698903
Escherichia coli
? + NADH + H+
-
-
-
r
additional information
no activity with D-glycerate and 3-hydroxypropanoate
698903
Escherichia coli
?
-
-
-
-
succinic semialdehyde + NADH + H+
-
698903
Escherichia coli
4-hydroxybutyrate + NAD+
-
-
-
r
succinic semialdehyde + NADH + H+
-
698903
Escherichia coli K12 BW25113
4-hydroxybutyrate + NAD+
-
-
-
r
succinic semialdehyde + NADH + H+
succinic semialdehyde is the preferred substrate
698903
Escherichia coli
gamma-hydroxybutyrate + NAD+
-
-
-
r
Subunits (protein specific)
Subunits
Commentary
Organism
homotetramer
4 * 31154, calculated from amino acid sequence
Escherichia coli
General Information
General Information
Commentary
Organism
malfunction
a yihU deletion mutant displays reduced tolerance to the cytotoxic effects of exogenous addition of succinic semialdehyde
Escherichia coli
metabolism
the enzyme is involved in the metabolism of succinic semialdehyde, and other potentially toxic intermediates that may accumulate under stress conditions in Escherichia coli
Escherichia coli
General Information (protein specific)
General Information
Commentary
Organism
malfunction
a yihU deletion mutant displays reduced tolerance to the cytotoxic effects of exogenous addition of succinic semialdehyde
Escherichia coli
metabolism
the enzyme is involved in the metabolism of succinic semialdehyde, and other potentially toxic intermediates that may accumulate under stress conditions in Escherichia coli
Escherichia coli
Other publictions for EC 1.1.1.61
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)
737764
Yoshida
Production of 4-hydroxybutyrat ...
Porphyromonas gingivalis, Porphyromonas gingivalis ATCC 33277
Biochim. Biophys. Acta
1850
2582-2591
2015
-
-
1
-
-
-
-
2
-
1
1
4
-
10
-
-
1
-
-
-
-
-
4
1
-
-
-
1
1
1
-
2
-
-
-
-
-
1
2
-
-
-
-
-
-
2
-
1
1
4
-
-
-
1
-
-
-
-
4
1
-
-
-
1
1
1
-
-
-
-
-
-
-
-
698903
Saito
Metabolite profiling reveals Y ...
Escherichia coli, Escherichia coli K12 BW25113
J. Biol. Chem.
284
16442-16451
2009
-
-
1
-
-
-
-
5
-
1
2
2
-
4
-
-
1
-
-
-
4
-
11
1
-
-
-
-
-
-
-
2
-
-
-
-
-
1
3
-
-
-
-
-
-
8
-
1
3
2
-
-
-
1
-
-
4
-
11
1
-
-
-
-
-
-
-
-
-
2
2
-
-
-
656423
Bravo
Reliable, sensitive, rapid and ...
Cupriavidus necator
J. Forensic Sci.
49
379-387
2004
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1
1
-
-
1
-
2
-
-
2
1
-
2
-
-
1
-
-
-
-
-
2
-
-
-
2
-
-
-
-
-
-
-
-
-
1
1
-
-
-
1
-
-
-
2
-
-
2
1
-
-
-
1
-
-
-
-
2
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
656170
Breitkreuz
A novel gamma-hydroxybutyrate ...
Arabidopsis thaliana
J. Biol. Chem.
278
41552-41556
2003
-
-
1
-
-
-
-
-
-
-
1
1
-
4
-
-
-
-
-
4
-
-
2
-
-
-
-
-
-
-
-
1
-
1
-
-
-
1
1
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
4
-
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
287171
Wolff
Purification and characterizat ...
Clostridium kluyveri
Protein Expr. Purif.
6
206-212
1995
-
-
-
-
-
-
1
4
-
2
2
-
-
2
-
-
1
-
-
-
-
-
-
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
4
-
2
2
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
287170
Nirenberg
Enzymatic utilization of gamma ...
Pseudomonas sp.
J. Biol. Chem.
235
954-960
1960
-
-
-
-
-
-
1
-
-
-
-
1
-
1
-
-
1
-
-
-
-
-
1
-
-
-
-
-
2
-
-
2
-
-
-
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-
-
2
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-
-
1
-
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-
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-
1
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1
-
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-
1
-
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-
2
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