BRENDA - Enzyme Database show
show all sequences of 4.1.3.22

Isolation and function of the subunits of citramalate lyase and formation of hybrids with the subunits of citrate lyase

Dimroth, P.; Buckel, W.; Loyal, R.; Eggerer, H.; Eur. J. Biochem. 80, 469-477 (1977)

Data extracted from this reference:

Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Clostridium tetanomorphum
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
citramalate
the alpha-subunit catalyzes the formation of acetyl-CoA and citramalate. The beta-subunit catalyzes the cleavage of (3S)-citramalyl-thio-acyl carrier protein lyase
33256
Clostridium tetanomorphum
acetate + pyruvate
-
33256
Clostridium tetanomorphum
-
Subunits
Subunits
Commentary
Organism
oligomer
the alpha-subunit represents an acetyl-thio-acyl carrier protein:citramalate acyl carrier protein transferase and the beta-subunit a (3S)-citramalyl-thio-acyl carrier protein lyase
Clostridium tetanomorphum
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
citramalate
the alpha-subunit catalyzes the formation of acetyl-CoA and citramalate. The beta-subunit catalyzes the cleavage of (3S)-citramalyl-thio-acyl carrier protein lyase
33256
Clostridium tetanomorphum
acetate + pyruvate
-
33256
Clostridium tetanomorphum
-
Subunits (protein specific)
Subunits
Commentary
Organism
oligomer
the alpha-subunit represents an acetyl-thio-acyl carrier protein:citramalate acyl carrier protein transferase and the beta-subunit a (3S)-citramalyl-thio-acyl carrier protein lyase
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
-
1
1
-
-
-
-
-
-
-
-
-
-
5
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
748589
Parimi
Eliminating acetate formation ...
Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661
Microb. Cell Fact.
16
114
2017
-
1
1
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
692849
Risso
Elucidation of an alternate is ...
Geobacter sulfurreducens, Geobacter sulfurreducens ATCC 51573 / DSM 12127
J. Bacteriol.
190
2266-2274
2008
-
-
-
-
3
-
-
-
-
-
-
3
-
4
-
-
-
-
-
-
3
-
6
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
3
-
6
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
679907
Zou
A comprehensive survey on isol ...
Leptospira biflexa, Leptospira interrogans, Leptospira meyeri
FEMS Microbiol. Lett.
269
90-96
2007
-
-
-
-
-
-
-
-
-
-
-
-
-
15
-
-
-
-
-
-
10
-
10
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
10
-
10
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
680494
Drevland
Enzymology and evolution of th ...
Methanocaldococcus jannaschii
J. Bacteriol.
189
4391-4400
2007
-
-
-
-
-
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
666279
Filatova
-
A study of the mechanism of ac ...
Rhodobacter sphaeroides
Microbiology
74
270-278
2005
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
33256
Dimroth
Isolation and function of the ...
Clostridium tetanomorphum
Eur. J. Biochem.
80
469-477
1977
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
33257
Dimroth
Structure of the prosthetic gr ...
Clostridium tetanomorphum
FEBS Lett.
76
280-283
1977
1
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
33255
Buckel
The enzyme complex citramalate ...
Clostridium tetanomorphum
Eur. J. Biochem.
64
255-262
1976
1
-
-
-
-
-
1
-
-
-
1
-
-
4
-
-
1
-
-
-
1
1
2
1
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
1
-
-
1
1
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
33258
Buckel
-
Substrate stereochemistry of t ...
Clostridium tetanomorphum
Biochem. Soc. Trans.
3
924-926
1975
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
33254
Barker
-
Citramalate pyruvate lyase ...
Clostridium tetanomorphum
Methods Enzymol.
13
344-346
1969
-
-
-
-
-
-
4
1
-
3
-
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
4
-
1
-
3
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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
-
-
-
-
-
-
4
1
-
1
-
-
-
17
-
-
-
-
-
-
-
-
4
-
-
-
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
4
-
1
-
1
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
2
1
-
-
-
-
-
-
-
-