show 
The enzyme complex citramalate lyase from Clostridium tetanomorphum
Buckel, W.; Bobi, A.; Eur. J. Biochem. 64, 255-262 (1976)
Data extracted from this reference:
Activating Compound
Activating Compound
Commentary
Organism
Structure
additional information
the enzyme contains acetyl thioester residues which play the central role in the catalytic mechanism
Clostridium tetanomorphum
Inhibitors
Inhibitors
Commentary
Organism
Structure
iodoacetate
-
Clostridium tetanomorphum
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
520000
580000
gel filtration, sucrose density gradient centrifugation
Clostridium tetanomorphum
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Clostridium tetanomorphum
-
-
-
Purification (Commentary)
Commentary
Organism
-
Clostridium tetanomorphum
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
-
Clostridium tetanomorphum
Storage Stability
Storage Stability
Organism
-20°C, enzyme concentration 10 mg/ml, 0.1 M phoshate, pH 7.4, 1.0 mM MgCl2, stable for at least 6 months
Clostridium tetanomorphum
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
acetate + pyruvate
-
33255
Clostridium tetanomorphum
(+)-citramalate
-
33255
Clostridium tetanomorphum
-
citramalate
(+)-citramalate
33255
Clostridium tetanomorphum
acetate + pyruvate
-
33255
Clostridium tetanomorphum
-
Subunits
Subunits
Commentary
Organism
oligomer
6 * 53000-56000, alpha, + 6 * 33000-36000, beta, + 6 * 10000-12000, gamma, SDS-PAGE
Clostridium tetanomorphum
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
additional information
the enzyme contains acetyl thioester residues which play the central role in the catalytic mechanism
Clostridium tetanomorphum
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
iodoacetate
-
Clostridium tetanomorphum
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
520000
580000
gel filtration, sucrose density gradient centrifugation
Clostridium tetanomorphum
Purification (Commentary) (protein specific)
Commentary
Organism
-
Clostridium tetanomorphum
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
-
Clostridium tetanomorphum
Storage Stability (protein specific)
Storage Stability
Organism
-20°C, enzyme concentration 10 mg/ml, 0.1 M phoshate, pH 7.4, 1.0 mM MgCl2, stable for at least 6 months
Clostridium tetanomorphum
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
acetate + pyruvate
-
33255
Clostridium tetanomorphum
(+)-citramalate
-
33255
Clostridium tetanomorphum
-
citramalate
(+)-citramalate
33255
Clostridium tetanomorphum
acetate + pyruvate
-
33255
Clostridium tetanomorphum
-
Subunits (protein specific)
Subunits
Commentary
Organism
oligomer
6 * 53000-56000, alpha, + 6 * 33000-36000, beta, + 6 * 10000-12000, gamma, SDS-PAGE
Clostridium tetanomorphum
Other publictions for EC 4.1.3.22
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)
748351
Wu
Synthesis of citramalic acid ...
Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661
J. Ind. Microbiol. Biotechnol.
44
1483-1490
2017
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1
1
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2
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748589
Parimi
Eliminating acetate formation ...
Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661
Microb. Cell Fact.
16
114
2017
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1
1
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4
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2
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1
1
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692849
Risso
Elucidation of an alternate is ...
Geobacter sulfurreducens, Geobacter sulfurreducens ATCC 51573 / DSM 12127
J. Bacteriol.
190
2266-2274
2008
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3
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3
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6
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3
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3
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3
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6
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679907
Zou
A comprehensive survey on isol ...
Leptospira biflexa, Leptospira interrogans, Leptospira meyeri
FEMS Microbiol. Lett.
269
90-96
2007
-
-
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15
-
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10
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10
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10
-
10
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680494
Drevland
Enzymology and evolution of th ...
Methanocaldococcus jannaschii
J. Bacteriol.
189
4391-4400
2007
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6
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1
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1
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666279
Filatova
-
A study of the mechanism of ac ...
Rhodobacter sphaeroides
Microbiology
74
270-278
2005
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33256
Dimroth
Isolation and function of the ...
Clostridium tetanomorphum
Eur. J. Biochem.
80
469-477
1977
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1
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1
1
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1
1
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33257
Dimroth
Structure of the prosthetic gr ...
Clostridium tetanomorphum
FEBS Lett.
76
280-283
1977
1
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1
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1
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33255
Buckel
The enzyme complex citramalate ...
Clostridium tetanomorphum
Eur. J. Biochem.
64
255-262
1976
1
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1
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1
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4
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1
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1
1
2
1
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1
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1
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1
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1
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1
1
2
1
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-
33258
Buckel
-
Substrate stereochemistry of t ...
Clostridium tetanomorphum
Biochem. Soc. Trans.
3
924-926
1975
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33254
Barker
-
Citramalate pyruvate lyase ...
Clostridium tetanomorphum
Methods Enzymol.
13
344-346
1969
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4
1
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3
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1
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2
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4
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1
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3
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2
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33253
Barker
Citramalate lyase of Clostridi ...
Clostridium tetanomorphum, Clostridium tetanomorphum H1 / ATCC 15920, no activity in Clostridium kluyveri, no activity in Escherichia coli, no activity in Pseudomonas sp., no activity in Saccharomyces cerevisiae
Arch. Mikrobiol.
59
4-12
1967
-
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4
1
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1
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17
-
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4
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2
1
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4
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1
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1
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4
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2
1
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