BRENDA - Enzyme Database
show all sequences of 2.8.3.16

Kinetic and mechanistic characterization of the formyl-CoA transferase from Oxalobacter formigenes

Jonsson, S.; Ricagno, S.; Lindqvist, Y.; Richards, N.G.; J. Biol. Chem. 279, 36003-36012 (2004)

Data extracted from this reference:

Crystallization (Commentary)
Crystallization (Commentary)
Organism
crystallization and structure determination of the enzyme/oxalyl-CoA complex, hanging drop technique. Crystallization and structure determination of the D169A, D169E, and D169S mutants
Oxalobacter formigenes
Engineering
Protein Variants
Commentary
Organism
D169A
mutant enzyme is correctly folded and forms interlocked dimers, 1300fold decrease in activity
Oxalobacter formigenes
D169E
mutant enzyme is correctly folded and forms interlocked dimers, inactive mutant enzyme
Oxalobacter formigenes
D169S
mutant enzyme is correctly folded and forms interlocked dimers, inactive mutant enzyme
Oxalobacter formigenes
Inhibitors
Inhibitors
Commentary
Organism
Structure
formate
-
Oxalobacter formigenes
oxalyl-CoA
-
Oxalobacter formigenes
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
81000
-
gel filtration
Oxalobacter formigenes
Organism
Organism
UniProt
Commentary
Textmining
Oxalobacter formigenes
-
-
-
Purification (Commentary)
Purification (Commentary)
Organism
enzyme recombinantly expressed in Escherichia coli
Oxalobacter formigenes
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
formyl-CoA + oxalate
involvement of the Asp169 side chain in mediating enzyme-catalyzed CoA transfer via a series of anhydride intermediates
662253
Oxalobacter formigenes
formate + oxalyl-CoA
-
-
-
?
Subunits
Subunits
Commentary
Organism
dimer
-
Oxalobacter formigenes
Synonyms
Synonyms
Commentary
Organism
FRC
-
Oxalobacter formigenes
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
4.3
-
formyl-CoA
-
Oxalobacter formigenes
4.3
-
oxalate
-
Oxalobacter formigenes
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
additional information
-
additional information
Kis for formate is 17 mM, Kii for formate is 380 mM, Kis for oxalyl-CoA is 0.15 mM, Kii for oxalyl-CoA is 0.28 mM
Oxalobacter formigenes
Crystallization (Commentary) (protein specific)
Crystallization
Organism
crystallization and structure determination of the enzyme/oxalyl-CoA complex, hanging drop technique. Crystallization and structure determination of the D169A, D169E, and D169S mutants
Oxalobacter formigenes
Engineering (protein specific)
Protein Variants
Commentary
Organism
D169A
mutant enzyme is correctly folded and forms interlocked dimers, 1300fold decrease in activity
Oxalobacter formigenes
D169E
mutant enzyme is correctly folded and forms interlocked dimers, inactive mutant enzyme
Oxalobacter formigenes
D169S
mutant enzyme is correctly folded and forms interlocked dimers, inactive mutant enzyme
Oxalobacter formigenes
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
formate
-
Oxalobacter formigenes
oxalyl-CoA
-
Oxalobacter formigenes
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
additional information
-
additional information
Kis for formate is 17 mM, Kii for formate is 380 mM, Kis for oxalyl-CoA is 0.15 mM, Kii for oxalyl-CoA is 0.28 mM
Oxalobacter formigenes
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
81000
-
gel filtration
Oxalobacter formigenes
Purification (Commentary) (protein specific)
Commentary
Organism
enzyme recombinantly expressed in Escherichia coli
Oxalobacter formigenes
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
formyl-CoA + oxalate
involvement of the Asp169 side chain in mediating enzyme-catalyzed CoA transfer via a series of anhydride intermediates
662253
Oxalobacter formigenes
formate + oxalyl-CoA
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
-
Oxalobacter formigenes
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
4.3
-
formyl-CoA
-
Oxalobacter formigenes
4.3
-
oxalate
-
Oxalobacter formigenes
Other publictions for EC 2.8.3.16
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)
739759
Herve
Diversity and ecology of oxalo ...
Actinobacteria, Firmicutes, Proteobacteria
World J. Microbiol. Biotechnol.
32
28
2016
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3
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8
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3
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6
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3
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3
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-
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-
-
-
-
-
-
-
-
-
-
726452
Mullins
Formyl-coenzyme A (CoA):oxalat ...
Acetobacter aceti 1023, Acetobacter aceti
Protein Sci.
21
686-696
2012
-
-
1
1
-
-
-
2
1
-
4
2
-
4
-
-
1
-
-
-
-
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2
1
3
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2
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1
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1
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2
1
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4
2
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1
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2
1
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-
2
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-
1
-
-
1
2
2
692851
Toyota
Differential substrate specifi ...
Escherichia coli, Escherichia coli MG1655, Oxalobacter formigenes
J. Bacteriol.
190
2556-2564
2008
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-
2
1
2
-
4
10
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3
-
32
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2
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6
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4
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2
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2
-
1
2
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4
2
10
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3
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2
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6
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693216
Berthold
Reinvestigation of the catalyt ...
Oxalobacter formigenes
J. Biol. Chem.
283
6519-6529
2008
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-
1
1
3
-
2
8
-
-
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1
-
2
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-
1
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1
2
1
1
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2
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1
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1
3
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2
2
8
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1
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1
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1
2
1
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693608
Khammar
Use of the frc gene as a molec ...
Ancylobacter oerskovii, Ancylobacter polymorphus, Arquibacter sp., Azorhizobium sp., Azospirillum brasilense, Azospirillum lipoferum, Bradyrhizobium japonicum, Bradyrhizobium sp., Cupriavidus necator, Cupriavidus necator JMP 134-1, Cupriavidus oxalaticus, Escherichia coli, Herminiimonas arsenicoxydans, Herminiimonas saxobsidens, Janthinobacterium sp. Marseille, Methylobacterium organophilum, Methylorubrum extorquens, Methylorubrum thiocyanatum, Oxalicibacterium flavum, Oxalobacter formigenes, Pandoraea sp., Paraburkholderia xenovorans, Rhodopseudomonas palustris, Shigella flexneri, Starkeya novella, Streptomyces avermitilis, Streptomyces coelicolor, Streptomyces violaceoruber, Variovorax paradoxus, Xanthobacter autotrophicus, Xanthobacter flavus, Xanthomonas sp.
J. Microbiol. Methods
76
120-127
2008
-
93
31
-
-
-
-
-
-
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36
-
39
-
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-
62
-
-
72
-
35
-
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-
105
35
-
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-
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36
-
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70
-
-
72
-
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-
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-
-
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-
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-
674225
Turroni
Oxalate consumption by lactoba ...
Lactobacillus acidophilus
J. Appl. Microbiol.
103
1600-1609
2007
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-
1
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-
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-
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1
1
-
5
-
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2
1
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1
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1
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1
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1
1
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-
2
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
692373
Lewanika
Lactobacillus gasseri Gasser A ...
Lactobacillus gasseri, Lactobacillus gasseri Gasser AM63T
FEMS Microbiol. Ecol.
61
110-120
2007
-
1
-
-
-
-
-
-
-
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-
2
-
6
-
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4
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2
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1
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4
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692677
Ye
Stable expression of the oxc a ...
Oxalobacter formigenes
Int. J. Mol. Med.
20
521-526
2007
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1
1
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1
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1
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4
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2
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2
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1
1
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1
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1
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-
2
-
-
-
-
-
-
-
-
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-
-
-
-
-
671452
Azcarate-Peril
Transcriptional and functional ...
Bifidobacterium animalis subsp. lactis, Lactobacillus acidophilus, Lactobacillus acidophilus NCFM, Lactobacillus gasseri
Appl. Environ. Microbiol.
72
1891-1899
2006
1
-
3
-
1
-
-
-
-
-
-
2
-
14
-
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4
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1
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3
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1
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4
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-
662253
Jonsson
Kinetic and mechanistic charac ...
Oxalobacter formigenes
J. Biol. Chem.
279
36003-36012
2004
-
-
-
1
3
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2
-
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-
1
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3
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1
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1
1
1
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2
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1
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1
3
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2
1
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1
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1
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1
1
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2
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645962
Ricagno
Crystallization and preliminar ...
Oxalobacter formigenes
Acta Crystallogr. Sect. D
59
1276-1277
2003
-
-
-
1
-
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-
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1
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3
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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
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1
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645963
Ricagno
Formyl-CoA transferase enclose ...
Oxalobacter formigenes
EMBO J.
22
3210-3219
2003
-
-
1
1
-
-
-
-
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-
1
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4
-
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1
1
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3
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4
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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3
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4
1
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645961
Sidhu
DNA sequencing and expression ...
Oxalobacter formigenes
J. Bacteriol.
179
3378-3381
1997
-
-
1
-
-
-
-
-
-
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1
1
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4
-
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1
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3
1
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1
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1
1
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1
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3
1
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645960
Baetz
-
Localization of oxalyl-coenzym ...
Oxalobacter formigenes, Oxalobacter formigenes OxB / ATCC 35274
Syst. Appl. Microbiol.
15
167-171
1992
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-
-
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1
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2
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2
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1
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1
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1
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645959
Baetz
Purification and characterizat ...
Oxalobacter formigenes
J. Bacteriol.
172
3537-3540
1990
-
-
-
-
-
-
2
3
-
-
2
1
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2
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1
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1
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3
1
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1
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1
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1
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2
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1
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1
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1
1
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1
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