BRENDA - Enzyme Database
show all sequences of 4.1.3.25

Structure of the prosthetic groups of citrate lyase and citramalate lyase

Dimroth, P.; Loyal, R.; FEBS Lett. 76, 280-283 (1977)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
dehospho-CoA
EC 4.1.3.22 and EC 4.1.3.25 have a common prosthetic group, which is covalently-bound dephospho-CoA. The linkage between dephospho-CoAs and the protein occurs through ribose-5-phosphate. This is bound in phosphodiester linkage to Ser and glycosidically to the 2'- or 3'-hydroxyl group of ribose of dephospho-CoA
Clostridium tetanomorphum
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Clostridium tetanomorphum
-
-
-
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
dehospho-CoA
EC 4.1.3.22 and EC 4.1.3.25 have a common prosthetic group, which is covalently-bound dephospho-CoA. The linkage between dephospho-CoAs and the protein occurs through ribose-5-phosphate. This is bound in phosphodiester linkage to Ser and glycosidically to the 2'- or 3'-hydroxyl group of ribose of dephospho-CoA
Clostridium tetanomorphum
Other publictions for EC 4.1.3.25
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)
746855
Chen
Identification of an itaconic ...
Aspergillus terreus, Aspergillus terreus LYT10
Appl. Microbiol. Biotechnol.
100
7541-7548
2016
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1
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1
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746828
Kronen
Mesaconase activity of class ...
Paraburkholderia xenovorans, Paraburkholderia xenovorans DSMZ 17367 / LB400
Appl. Environ. Microbiol.
81
5632-5638
2015
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728354
Sasikaran
Bacterial itaconate degradatio ...
Pseudomonas aeruginosa, Yersinia pestis
Nat. Chem. Biol.
10
371-377
2014
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6
6
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727258
Zarzycki
The crystal structures of the ...
Chloroflexus aurantiacus, Chloroflexus aurantiacus OK-70-fl / DSM 636
BMC Struct. Biol.
13
28
2013
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1
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2493
Jain
-
The molecular cloning of genes ...
Pseudomonas putida, Pseudomonas putida NCIB9869
Appl. Microbiol. Biotechnol.
45
502-508
1996
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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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33269
Sasaki
Enzymatic cleavage of (+)citra ...
Bacillus sp. (in: Bacteria)
J. Biochem.
73
599-608
1973
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33270
Sai
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Enzymatic formation of (-)-cit ...
Saccharomyces pastorianus
Agric. Biol. Chem.
32
1398-1400
1968
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5793
Cooper
The utilization of itaconate b ...
Pseudomonas sp., Pseudomonas sp. B2aba
Biochem. J.
91
82-91
1964
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