BRENDA - Enzyme Database
show all sequences of 2.8.3.16

Differential substrate specificity and kinetic behavior of Escherichia coli YfdW and Oxalobacter formigenes formyl coenzyme A transferase

Toyota, C.G.; Berthold, C.L.; Gruez, A.; Jonsson, S.; Lindqvist, Y.; Cambillau, C.; Richards, N.G.; J. Bacteriol. 190, 2556-2564 (2008)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
expression Escherichia coli BL21-DE3
Oxalobacter formigenes
expression in Escherichia coli K12
Escherichia coli
Crystallization (Commentary)
Crystallization (Commentary)
Organism
FRC variants W48F and W48Q, hanging drop vapour diffusion method
Oxalobacter formigenes
Engineering
Protein Variants
Commentary
Organism
W48F
FRC variant
Oxalobacter formigenes
W48Q
FRC variant
Oxalobacter formigenes
Inhibitors
Inhibitors
Commentary
Organism
Structure
acetyl-CoA
-
Escherichia coli
coenzyme A
free CoA
Escherichia coli
oxalate
substrate inhibition
Escherichia coli
oxalate
-
Oxalobacter formigenes
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.002
-
formyl-CoA
wild-type FRC
Oxalobacter formigenes
0.0047
-
formyl-CoA
His-FRC
Oxalobacter formigenes
0.0058
-
formyl-CoA
W48Q FRC
Oxalobacter formigenes
0.0171
-
formyl-CoA
W48F FRC
Oxalobacter formigenes
0.35
-
formyl-CoA
His-YfdW
Escherichia coli
0.43
-
oxalate
W48Q FRC
Oxalobacter formigenes
0.51
-
oxalate
His-YfdW
Escherichia coli
1.2
-
oxalate
His-FRC
Oxalobacter formigenes
1.5
-
oxalate
W48F FRC
Oxalobacter formigenes
3.9
-
oxalate
wild-type FRC
Oxalobacter formigenes
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
formyl-CoA + oxalate
Oxalobacter formigenes
FRC and oxalyl-CoA decarboxylase are essential for the survival of Oxalobacter in that they mediate the conversion of oxalate into formate and CO2 in a coupled catalytic cycle
formate + oxalyl-CoA
-
-
?
formyl-CoA + oxalate
Escherichia coli
YfdW catalyzes the conversion of oxalate into oxalyl-CoA by using formyl-CoA as a donor, YfdW is a formyl-CoA transferase and YfdW appears to be more stringent than the corresponding enzyme (FRC) in Oxalobacter in employing formyl-CoA and oxalate as substrates
formate + oxalyl-CoA
-
-
?
formyl-CoA + oxalate
Escherichia coli MG1655
YfdW catalyzes the conversion of oxalate into oxalyl-CoA by using formyl-CoA as a donor, YfdW is a formyl-CoA transferase and YfdW appears to be more stringent than the corresponding enzyme (FRC) in Oxalobacter in employing formyl-CoA and oxalate as substrates
formate + oxalyl-CoA
-
-
?
Organism
Organism
UniProt
Commentary
Textmining
Escherichia coli
-
MG1655
-
Escherichia coli MG1655
-
MG1655
-
Oxalobacter formigenes
O06644
-
-
Purification (Commentary)
Purification (Commentary)
Organism
His-tagged FRC protein is purified by Ni-nitrilotriacetic acid column and subsequent gel filtration
Oxalobacter formigenes
His-tagged YfdW protein is purified by metal affinity chromatography and subsequent gel filtration on a Superdex 200 column, eluting with 5 mM HEPES buffer containing 150 mM NaCl, pH 7.5.
Escherichia coli
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
formyl-CoA + oxalate
-
692851
Escherichia coli
formate + oxalyl-CoA
-
-
-
?
formyl-CoA + oxalate
-
692851
Oxalobacter formigenes
formate + oxalyl-CoA
-
-
-
?
formyl-CoA + oxalate
FRC and oxalyl-CoA decarboxylase are essential for the survival of Oxalobacter in that they mediate the conversion of oxalate into formate and CO2 in a coupled catalytic cycle
692851
Oxalobacter formigenes
formate + oxalyl-CoA
-
-
-
?
formyl-CoA + oxalate
YfdW catalyzes the conversion of oxalate into oxalyl-CoA by using formyl-CoA as a donor, YfdW is a formyl-CoA transferase and YfdW appears to be more stringent than the corresponding enzyme (FRC) in Oxalobacter in employing formyl-CoA and oxalate as substrates
692851
Escherichia coli
formate + oxalyl-CoA
-
-
-
?
formyl-CoA + oxalate
-
692851
Escherichia coli MG1655
formate + oxalyl-CoA
-
-
-
?
formyl-CoA + oxalate
YfdW catalyzes the conversion of oxalate into oxalyl-CoA by using formyl-CoA as a donor, YfdW is a formyl-CoA transferase and YfdW appears to be more stringent than the corresponding enzyme (FRC) in Oxalobacter in employing formyl-CoA and oxalate as substrates
692851
Escherichia coli MG1655
formate + oxalyl-CoA
-
-
-
?
Synonyms
Synonyms
Commentary
Organism
formyl coenzyme A transferase
-
Escherichia coli
formyl-CoA-transferase
-
Oxalobacter formigenes
FRC
-
Oxalobacter formigenes
YfdW
-
Escherichia coli
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
23
-
oxalate
-
Escherichia coli
74
-
oxalate
W48Q FRC, the W48F FRC is not inhibited by oxalate at concentrations of up to 154 mM
Oxalobacter formigenes
Cloned(Commentary) (protein specific)
Commentary
Organism
expression Escherichia coli BL21-DE3
Oxalobacter formigenes
expression in Escherichia coli K12
Escherichia coli
Crystallization (Commentary) (protein specific)
Crystallization
Organism
FRC variants W48F and W48Q, hanging drop vapour diffusion method
Oxalobacter formigenes
Engineering (protein specific)
Protein Variants
Commentary
Organism
W48F
FRC variant
Oxalobacter formigenes
W48Q
FRC variant
Oxalobacter formigenes
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
acetyl-CoA
-
Escherichia coli
coenzyme A
free CoA
Escherichia coli
oxalate
substrate inhibition
Escherichia coli
oxalate
-
Oxalobacter formigenes
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
23
-
oxalate
-
Escherichia coli
74
-
oxalate
W48Q FRC, the W48F FRC is not inhibited by oxalate at concentrations of up to 154 mM
Oxalobacter formigenes
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.002
-
formyl-CoA
wild-type FRC
Oxalobacter formigenes
0.0047
-
formyl-CoA
His-FRC
Oxalobacter formigenes
0.0058
-
formyl-CoA
W48Q FRC
Oxalobacter formigenes
0.0171
-
formyl-CoA
W48F FRC
Oxalobacter formigenes
0.35
-
formyl-CoA
His-YfdW
Escherichia coli
0.43
-
oxalate
W48Q FRC
Oxalobacter formigenes
0.51
-
oxalate
His-YfdW
Escherichia coli
1.2
-
oxalate
His-FRC
Oxalobacter formigenes
1.5
-
oxalate
W48F FRC
Oxalobacter formigenes
3.9
-
oxalate
wild-type FRC
Oxalobacter formigenes
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
formyl-CoA + oxalate
Oxalobacter formigenes
FRC and oxalyl-CoA decarboxylase are essential for the survival of Oxalobacter in that they mediate the conversion of oxalate into formate and CO2 in a coupled catalytic cycle
formate + oxalyl-CoA
-
-
?
formyl-CoA + oxalate
Escherichia coli
YfdW catalyzes the conversion of oxalate into oxalyl-CoA by using formyl-CoA as a donor, YfdW is a formyl-CoA transferase and YfdW appears to be more stringent than the corresponding enzyme (FRC) in Oxalobacter in employing formyl-CoA and oxalate as substrates
formate + oxalyl-CoA
-
-
?
formyl-CoA + oxalate
Escherichia coli MG1655
YfdW catalyzes the conversion of oxalate into oxalyl-CoA by using formyl-CoA as a donor, YfdW is a formyl-CoA transferase and YfdW appears to be more stringent than the corresponding enzyme (FRC) in Oxalobacter in employing formyl-CoA and oxalate as substrates
formate + oxalyl-CoA
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
His-tagged FRC protein is purified by Ni-nitrilotriacetic acid column and subsequent gel filtration
Oxalobacter formigenes
His-tagged YfdW protein is purified by metal affinity chromatography and subsequent gel filtration on a Superdex 200 column, eluting with 5 mM HEPES buffer containing 150 mM NaCl, pH 7.5.
Escherichia coli
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
formyl-CoA + oxalate
-
692851
Escherichia coli
formate + oxalyl-CoA
-
-
-
?
formyl-CoA + oxalate
-
692851
Oxalobacter formigenes
formate + oxalyl-CoA
-
-
-
?
formyl-CoA + oxalate
FRC and oxalyl-CoA decarboxylase are essential for the survival of Oxalobacter in that they mediate the conversion of oxalate into formate and CO2 in a coupled catalytic cycle
692851
Oxalobacter formigenes
formate + oxalyl-CoA
-
-
-
?
formyl-CoA + oxalate
YfdW catalyzes the conversion of oxalate into oxalyl-CoA by using formyl-CoA as a donor, YfdW is a formyl-CoA transferase and YfdW appears to be more stringent than the corresponding enzyme (FRC) in Oxalobacter in employing formyl-CoA and oxalate as substrates
692851
Escherichia coli
formate + oxalyl-CoA
-
-
-
?
formyl-CoA + oxalate
-
692851
Escherichia coli MG1655
formate + oxalyl-CoA
-
-
-
?
formyl-CoA + oxalate
YfdW catalyzes the conversion of oxalate into oxalyl-CoA by using formyl-CoA as a donor, YfdW is a formyl-CoA transferase and YfdW appears to be more stringent than the corresponding enzyme (FRC) in Oxalobacter in employing formyl-CoA and oxalate as substrates
692851
Escherichia coli MG1655
formate + oxalyl-CoA
-
-
-
?
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
-
-
-
-
-
-
-
-
-
-
-
3
-
8
-
-
-
-
-
-
-
-
3
-
6
-
-
-
-
-
-
-
-
-
-
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-
-
-
-
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-
-
-
-
-
-
-
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3
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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
-
-
-
-
-
2
1
3
-
-
-
2
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
2
1
-
4
2
-
-
-
1
-
-
-
-
2
1
-
-
-
2
-
-
-
-
1
-
-
1
2
2
692851
Toyota
Differential substrate specifi ...
Escherichia coli, Escherichia coli MG1655, Oxalobacter formigenes
J. Bacteriol.
190
2556-2564
2008
-
-
2
1
2
-
4
10
-
-
-
3
-
32
-
-
2
-
-
-
-
-
6
-
4
-
-
-
-
-
-
-
-
2
-
-
-
-
2
-
1
2
-
-
4
2
10
-
-
-
3
-
-
-
2
-
-
-
-
6
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
693216
Berthold
Reinvestigation of the catalyt ...
Oxalobacter formigenes
J. Biol. Chem.
283
6519-6529
2008
-
-
1
1
3
-
2
8
-
-
-
1
-
2
-
-
1
-
-
-
-
1
2
1
1
-
-
-
-
-
-
-
-
2
-
-
-
-
1
-
1
3
-
-
2
2
8
-
-
-
1
-
-
-
1
-
-
-
1
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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
-
-
-
-
-
-
-
-
36
-
39
-
-
-
-
-
62
-
-
72
-
35
-
-
-
-
-
-
-
-
-
-
-
-
105
35
-
-
-
-
-
-
-
-
-
-
-
36
-
-
-
-
-
70
-
-
72
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
674225
Turroni
Oxalate consumption by lactoba ...
Lactobacillus acidophilus
J. Appl. Microbiol.
103
1600-1609
2007
-
-
1
-
-
-
-
-
-
-
1
1
-
5
-
-
-
-
-
-
-
-
2
1
-
1
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
2
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
692373
Lewanika
Lactobacillus gasseri Gasser A ...
Lactobacillus gasseri, Lactobacillus gasseri Gasser AM63T
FEMS Microbiol. Ecol.
61
110-120
2007
-
1
-
-
-
-
-
-
-
-
-
2
-
6
-
-
-
-
-
-
-
-
4
-
2
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
692677
Ye
Stable expression of the oxc a ...
Oxalobacter formigenes
Int. J. Mol. Med.
20
521-526
2007
-
1
1
-
-
-
-
-
1
-
-
1
-
4
-
-
-
-
-
-
-
-
2
-
2
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
3
-
-
1
-
-
-
-
-
-
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-
2
-
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-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
662253
Jonsson
Kinetic and mechanistic charac ...
Oxalobacter formigenes
J. Biol. Chem.
279
36003-36012
2004
-
-
-
1
3
-
2
-
-
-
1
-
-
3
-
-
1
-
-
-
-
-
1
1
1
-
-
-
2
-
-
-
-
1
-
-
-
-
-
-
1
3
-
-
2
1
-
-
-
1
-
-
-
-
1
-
-
-
-
1
1
-
-
-
2
-
-
-
-
-
-
-
-
-
-
645962
Ricagno
Crystallization and preliminar ...
Oxalobacter formigenes
Acta Crystallogr. Sect. D
59
1276-1277
2003
-
-
-
1
-
-
-
-
-
-
-
1
-
3
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
645963
Ricagno
Formyl-CoA transferase enclose ...
Oxalobacter formigenes
EMBO J.
22
3210-3219
2003
-
-
1
1
-
-
-
-
-
-
-
1
-
4
-
-
1
1
-
3
-
-
4
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
1
-
-
-
1
-
3
-
-
4
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
645961
Sidhu
DNA sequencing and expression ...
Oxalobacter formigenes
J. Bacteriol.
179
3378-3381
1997
-
-
1
-
-
-
-
-
-
-
1
1
-
4
-
-
1
-
-
-
-
-
3
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
1
-
-
-
-
3
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
645960
Baetz
-
Localization of oxalyl-coenzym ...
Oxalobacter formigenes, Oxalobacter formigenes OxB / ATCC 35274
Syst. Appl. Microbiol.
15
167-171
1992
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645959
Baetz
Purification and characterizat ...
Oxalobacter formigenes
J. Bacteriol.
172
3537-3540
1990
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