BRENDA - Enzyme Database
show all sequences of 4.2.1.112

Purification and characterization of acetylene hydratase of Pelobacter acetylenicus, a tungsten iron-sulfur protein

Rosner, B.M.; Schink, B.; J. Bacteriol. 177, 5767-5772 (1995)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
Dithionite
a strong reductant is required for activity
Pelobacter acetylenicus
additional information
no activation by tungstate at 5 mM
Pelobacter acetylenicus
Ti(III)citrate
a strong reductant is required for activity
Pelobacter acetylenicus
Inhibitors
Inhibitors
Commentary
Organism
Structure
CO
90% inhibition at 0.8 mM
Pelobacter acetylenicus
HgCl2
reduces enzyme activity by 40% at 0.01 mM, 80% at 0.1 mM, and 98% at 0.2 mM
Pelobacter acetylenicus
KCN
20% inhibition at 1 mM, 40% inhibition at 5-10 mM
Pelobacter acetylenicus
molybdate
-
Pelobacter acetylenicus
additional information
no inhibition by citrate, ascorbate, tiron, ferrocene, and EDTA, no inhibition by ethylene at 8 mM
Pelobacter acetylenicus
nitric oxide
complete inhibition at 3 mM
Pelobacter acetylenicus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
the enzyme activity depends on the redox status, overview
Pelobacter acetylenicus
0.014
-
Acetylene
pH 7.0, 30°C
Pelobacter acetylenicus
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Iron-sulfur cluster
dependent on, the enzyme is a tungsten/iron-sulfur protein, 4.8 mol of iron per mol of enzyme and 3.9 mol od acid-labile sulfur per mol of enzyme
Pelobacter acetylenicus
additional information
no molybdenum detectable
Pelobacter acetylenicus
Tungsten
dependent on, the enzyme is a tungsten/iron-sulfur protein, 0.4 mol of tungsten per mol of enzyme
Pelobacter acetylenicus
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
60000
-
gel filtration
Pelobacter acetylenicus
73000
-
1 * 73000, SDS-PAGE
Pelobacter acetylenicus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
acetylene + H2O
Pelobacter acetylenicus
-
acetaldehyde
-
-
?
acetylene + H2O
Pelobacter acetylenicus WoAcy1 / DSM 3246
-
acetaldehyde
-
-
?
Organism
Organism
UniProt
Commentary
Textmining
Pelobacter acetylenicus
-
-
-
Pelobacter acetylenicus WoAcy1 / DSM 3246
-
-
-
Purification (Commentary)
Purification (Commentary)
Organism
under air at room temperature, native enzyme 240-fold by ammonium sulfate fractionation, anion exchange chromatography, gel filtration, and a second anion exchange chromatography step to homogeneity
Pelobacter acetylenicus
Source Tissue
Source Tissue
Commentary
Organism
Textmining
culture condition:acetylene-grown cell
-
Pelobacter acetylenicus
-
culture condition:molybdate-grown cell
-
Pelobacter acetylenicus
-
culture condition:tungstate-grown cell
-
Pelobacter acetylenicus
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
69.2
-
purified enzyme
Pelobacter acetylenicus
Storage Stability
Storage Stability
Organism
enzyme activity is stable even after prolonged storage of the cell extract or of the purified protein under air
Pelobacter acetylenicus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
acetylene + H2O
-
669072
Pelobacter acetylenicus
acetaldehyde
-
-
-
?
acetylene + H2O
-
669072
Pelobacter acetylenicus WoAcy1 / DSM 3246
acetaldehyde
-
-
-
?
additional information
no activity with ethylene, methylene blue, or anthraquinone disulfonate, the purified enzyme has no coenzyme A-acetylating aldehyde dehydrogenase activity
669072
Pelobacter acetylenicus
?
-
-
-
?
additional information
no activity with ethylene, methylene blue, or anthraquinone disulfonate, the purified enzyme has no coenzyme A-acetylating aldehyde dehydrogenase activity
669072
Pelobacter acetylenicus WoAcy1 / DSM 3246
?
-
-
-
?
Subunits
Subunits
Commentary
Organism
monomer
1 * 73000, SDS-PAGE
Pelobacter acetylenicus
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
50
-
-
Pelobacter acetylenicus
Temperature Range [°C]
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
22
80
-
Pelobacter acetylenicus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6
6.5
-
Pelobacter acetylenicus
pH Range
pH Minimum
pH Maximum
Commentary
Organism
4
9
-
Pelobacter acetylenicus
pI Value
Organism
Commentary
pI Value Maximum
pI Value
Pelobacter acetylenicus
chromatofocusing
-
4.3
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
Dithionite
a strong reductant is required for activity
Pelobacter acetylenicus
additional information
no activation by tungstate at 5 mM
Pelobacter acetylenicus
Ti(III)citrate
a strong reductant is required for activity
Pelobacter acetylenicus
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
CO
90% inhibition at 0.8 mM
Pelobacter acetylenicus
HgCl2
reduces enzyme activity by 40% at 0.01 mM, 80% at 0.1 mM, and 98% at 0.2 mM
Pelobacter acetylenicus
KCN
20% inhibition at 1 mM, 40% inhibition at 5-10 mM
Pelobacter acetylenicus
molybdate
-
Pelobacter acetylenicus
additional information
no inhibition by citrate, ascorbate, tiron, ferrocene, and EDTA, no inhibition by ethylene at 8 mM
Pelobacter acetylenicus
nitric oxide
complete inhibition at 3 mM
Pelobacter acetylenicus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
the enzyme activity depends on the redox status, overview
Pelobacter acetylenicus
0.014
-
Acetylene
pH 7.0, 30°C
Pelobacter acetylenicus
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Iron-sulfur cluster
dependent on, the enzyme is a tungsten/iron-sulfur protein, 4.8 mol of iron per mol of enzyme and 3.9 mol od acid-labile sulfur per mol of enzyme
Pelobacter acetylenicus
additional information
no molybdenum detectable
Pelobacter acetylenicus
Tungsten
dependent on, the enzyme is a tungsten/iron-sulfur protein, 0.4 mol of tungsten per mol of enzyme
Pelobacter acetylenicus
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
60000
-
gel filtration
Pelobacter acetylenicus
73000
-
1 * 73000, SDS-PAGE
Pelobacter acetylenicus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
acetylene + H2O
Pelobacter acetylenicus
-
acetaldehyde
-
-
?
acetylene + H2O
Pelobacter acetylenicus WoAcy1 / DSM 3246
-
acetaldehyde
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
under air at room temperature, native enzyme 240-fold by ammonium sulfate fractionation, anion exchange chromatography, gel filtration, and a second anion exchange chromatography step to homogeneity
Pelobacter acetylenicus
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
culture condition:acetylene-grown cell
-
Pelobacter acetylenicus
-
culture condition:molybdate-grown cell
-
Pelobacter acetylenicus
-
culture condition:tungstate-grown cell
-
Pelobacter acetylenicus
-
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
69.2
-
purified enzyme
Pelobacter acetylenicus
Storage Stability (protein specific)
Storage Stability
Organism
enzyme activity is stable even after prolonged storage of the cell extract or of the purified protein under air
Pelobacter acetylenicus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
acetylene + H2O
-
669072
Pelobacter acetylenicus
acetaldehyde
-
-
-
?
acetylene + H2O
-
669072
Pelobacter acetylenicus WoAcy1 / DSM 3246
acetaldehyde
-
-
-
?
additional information
no activity with ethylene, methylene blue, or anthraquinone disulfonate, the purified enzyme has no coenzyme A-acetylating aldehyde dehydrogenase activity
669072
Pelobacter acetylenicus
?
-
-
-
?
additional information
no activity with ethylene, methylene blue, or anthraquinone disulfonate, the purified enzyme has no coenzyme A-acetylating aldehyde dehydrogenase activity
669072
Pelobacter acetylenicus WoAcy1 / DSM 3246
?
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
monomer
1 * 73000, SDS-PAGE
Pelobacter acetylenicus
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
50
-
-
Pelobacter acetylenicus
Temperature Range [°C] (protein specific)
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
22
80
-
Pelobacter acetylenicus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6
6.5
-
Pelobacter acetylenicus
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
4
9
-
Pelobacter acetylenicus
pI Value (protein specific)
Organism
Commentary
pI Value Maximum
pI Value
Pelobacter acetylenicus
chromatofocusing
-
4.3
Other publictions for EC 4.2.1.112
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
Synonyms
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)
748243
Kroneck
Acetylene hydratase a non-re ...
Rhodococcus opacus, Rhodococcus ruber, Rhodobacter capsulatus, Norcadia rhodochorous, Rhodococcus sp. A1, Gordona alkanivorans, Pelobacter acetylenicus
J. Biol. Inorg. Chem.
21
29-38
2016
-
-
-
1
5
-
2
-
1
19
-
7
-
7
-
-
-
7
-
2
-
-
14
1
-
-
-
-
-
-
-
-
14
-
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-
-
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-
14
1
5
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2
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1
19
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7
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2
-
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14
1
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-
-
-
-
-
-
-
-
9
9
-
-
-
748431
Boll
Structure and function of the ...
Pelobacter acetylenicus
J. Mol. Microbiol. Biotechnol.
26
119-137
2016
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1
5
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2
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1
4
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1
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2
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1
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2
2
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3
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3
1
5
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2
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1
4
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1
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2
2
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2
2
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730116
Liao
Convergence in the QM-only and ...
Escherichia coli
J. Comput. Chem.
34
2389-2397
2013
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1
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4
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1
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1
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1
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3
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1
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2
-
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-
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-
1
1
-
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-
713603
Liao
-
Theoretical study of the chemo ...
Pelobacter acetylenicus
ACS Catal.
1
937-944
2011
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1
-
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1
-
1
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1
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2
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2
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1
1
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715374
Tenbrink
Exploring the active site of t ...
Pelobacter acetylenicus, Pelobacter acetylenicus WoAcy1 / DSM 3246
J. Bacteriol.
193
1229-1236
2011
-
-
1
1
4
-
-
1
1
2
-
2
-
7
-
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1
-
-
2
-
4
1
-
1
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1
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1
-
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1
1
1
4
-
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1
1
2
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2
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2
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4
1
1
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1
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703363
Vincent
A DFT study of the possible ro ...
Pelobacter acetylenicus
Dalton Trans.
39
3816-3822
2010
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1
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1
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716769
Liao
Mechanism of tungsten-dependen ...
Pelobacter acetylenicus
Proc. Natl. Acad. Sci. USA
107
22523-22527
2010
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706054
Antony
-
Theoretical studies of models ...
Pelobacter acetylenicus
Organometallics
28
4938-4944
2009
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1
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670710
Seiffert
Structure of the non-redox-act ...
Pelobacter acetylenicus
Proc. Natl. Acad. Sci. USA
104
3073-3077
2007
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667090
Einsle
Crystallization and preliminar ...
Pelobacter acetylenicus, Pelobacter acetylenicus WoAcy1 / DSM 3246
Acta Crystallogr. Sect. F
F61
299-301
2005
2
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7
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668453
Meckenstock
Acetylene hydratase of Pelobac ...
Pelobacter acetylenicus
Eur. J. Biochem.
264
176-182
1999
1
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3
2
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1
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1
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668651
Rosner
Acetylene degradation by new i ...
Rhodococcus opacus, Rhodococcus ruber, Gordonia sp., Rhodococcus ruber aerobic, Gordonia sp. aerobic
FEMS Microbiol. Lett.
148
175-180
1997
2
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6
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14
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3
3
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669039
Yadav
-
A functional mimic of the new ...
Pelobacter acetylenicus
J. Am. Chem. Soc.
119
4315-4316
1997
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669072
Rosner
Purification and characterizat ...
Pelobacter acetylenicus, Pelobacter acetylenicus WoAcy1 / DSM 3246
J. Bacteriol.
177
5767-5772
1995
3
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6
2
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2
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10
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6
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