BRENDA - Enzyme Database
show all sequences of 4.1.3.22

Eliminating acetate formation improves citramalate production by metabolically engineered Escherichia coli

Parimi, N.S.; Durie, I.A.; Wu, X.; Niyas, A.M.M.; Eiteman, M.A.; Microb. Cell Fact. 16, 114 (2017)

Data extracted from this reference:

Application
Application
Commentary
Organism
synthesis
synthesis of citramalate at high yield by Escherichia coli overexpressing citramalate synthase. Citramalate is a chemical precursor to the industrially important methacrylic acid. Acetate is an undesirable by-product potentially formed from pyruvate and acetyl-CoA, the precursors of citramalate during aerobic growth of Escherichia coli. Gene deletions critical to reducing acetate accumulation during aerobic growth and citramalate production are ifdentified in metabolically engineered Escherichia coli strains. The key knockouts critical to minimizing acetate formation are identified as pta, ackA and poxB
Methanocaldococcus jannaschii
Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli
Methanocaldococcus jannaschii
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Methanocaldococcus jannaschii
Q58787
-
-
Methanocaldococcus jannaschii DSM 2661
Q58787
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
acetate + pyruvate
-
748589
Methanocaldococcus jannaschii
citramalate
-
-
-
?
acetate + pyruvate
-
748589
Methanocaldococcus jannaschii DSM 2661
citramalate
-
-
-
?
Application (protein specific)
Application
Commentary
Organism
synthesis
synthesis of citramalate at high yield by Escherichia coli overexpressing citramalate synthase. Citramalate is a chemical precursor to the industrially important methacrylic acid. Acetate is an undesirable by-product potentially formed from pyruvate and acetyl-CoA, the precursors of citramalate during aerobic growth of Escherichia coli. Gene deletions critical to reducing acetate accumulation during aerobic growth and citramalate production are ifdentified in metabolically engineered Escherichia coli strains. The key knockouts critical to minimizing acetate formation are identified as pta, ackA and poxB
Methanocaldococcus jannaschii
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Methanocaldococcus jannaschii
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
acetate + pyruvate
-
748589
Methanocaldococcus jannaschii
citramalate
-
-
-
?
acetate + pyruvate
-
748589
Methanocaldococcus jannaschii DSM 2661
citramalate
-
-
-
?
General Information
General Information
Commentary
Organism
metabolism
key enzyme in metabolic pathways for citramalate synthesis
Methanocaldococcus jannaschii
General Information (protein specific)
General Information
Commentary
Organism
metabolism
key enzyme in metabolic pathways for citramalate synthesis
Methanocaldococcus jannaschii
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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748589
Parimi
Eliminating acetate formation ...
Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661
Microb. Cell Fact.
16
114
2017
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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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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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680494
Drevland
Enzymology and evolution of th ...
Methanocaldococcus jannaschii
J. Bacteriol.
189
4391-4400
2007
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666279
Filatova
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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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33257
Dimroth
Structure of the prosthetic gr ...
Clostridium tetanomorphum
FEBS Lett.
76
280-283
1977
1
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33255
Buckel
The enzyme complex citramalate ...
Clostridium tetanomorphum
Eur. J. Biochem.
64
255-262
1976
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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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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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