BRENDA - Enzyme Database show
show all sequences of 2.1.3.1

Transcarboxylase

Wood, H.G.; The Enzymes, 3rd Ed. (Boyer, P. D. , ed. ) 6, 83-115 (1972)
No PubMed abstract available

Data extracted from this reference:

General Stability
General Stability
Organism
alkaline pH, low ionic strength, monovalent ions, low protein concentration and elevated temperatures favor dissociation to inactive 5S, 6S and 1.3S subunits
Propionibacterium sp.
glycerol, 20% retards dissociation of 12S and 6S-biotinyl subunit
Propionibacterium sp.
polyvalent anions stabilize
Propionibacterium sp.
Inhibitors
Inhibitors
Commentary
Organism
Structure
(S)-methylmalonyl-CoA
-
Propionibacterium sp.
2-oxobutyrate
-
Propionibacterium sp.
3-methyloxaloacetate
strong
Propionibacterium sp.
Avidin
strong
Propionibacterium sp.
coenzyme A
-
Propionibacterium sp.
additional information
no inhibition by metal chelating agents, such as EDTA
Propionibacterium sp.
oxalate
-
Propionibacterium sp.
oxaloacetate
-
Propionibacterium sp.
propionyl pantetheine
-
Propionibacterium sp.
propionyl-CoA
-
Propionibacterium sp.
pyruvate
-
Propionibacterium sp.
SH-reagents
weak
Propionibacterium sp.
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
kinetics and mechanism
Propionibacterium sp.
0.0077
-
(2S)-methylmalonyl-coenzyme A
-
Propionibacterium sp.
0.034
-
propionyl-CoA
-
Propionibacterium sp.
0.035
-
malonyl-CoA
-
Propionibacterium sp.
0.063
-
oxaloacetate
-
Propionibacterium sp.
0.25
-
butyryl-CoA
-
Propionibacterium sp.
0.5
-
acetyl-CoA
-
Propionibacterium sp.
0.77
-
pyruvate
-
Propionibacterium sp.
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytoplasm
-
Propionibacterium sp.
5737
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Co2+
requirement
Propionibacterium sp.
additional information
no additional metal requirement
Propionibacterium sp.
Zn2+
requirement, can replace Co2+
Propionibacterium sp.
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
additional information
-
two active forms of enzyme: 18S and 16S, the 16S species arises from 18S species by loss of a 6S biotin, Co, Zn subunit
Propionibacterium sp.
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
propionyl-CoA + oxaloacetate
Propionibacterium sp.
-
(S)-methylmalonyl-CoA + pyruvate
-
Propionibacterium sp.
r
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Propionibacterium sp.
-
-
-
Purification (Commentary)
Commentary
Organism
-
Propionibacterium sp.
Reaction
Reaction
Commentary
Organism
(S)-methylmalonyl-CoA + pyruvate = propanoyl-CoA + oxaloacetate
mechanism
Propionibacterium sp.
Specific Activity [micromol/min/mg]
Specific Activity Minimum [Ámol/min/mg]
Specific Activity Maximum [Ámol/min/mg]
Commentary
Organism
40
-
-
Propionibacterium sp.
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
acetoacetyl-CoA + oxaloacetate
carboxylation at about 2.5% the rate of propionyl-CoA
485816
Propionibacterium sp.
3-oxoglutaryl-CoA + pyruvate
-
485816
Propionibacterium sp.
-
acetyl-CoA + oxaloacetate
carboxylation at about 50% the rate of propionyl-CoA
485816
Propionibacterium sp.
malonyl-CoA + pyruvate
-
485816
Propionibacterium sp.
r
butyryl-CoA + oxaloacetate
carboxylation at about 10% the rate of propionyl-CoA
485816
Propionibacterium sp.
ethylmalonyl-CoA + pyruvate
-
485816
Propionibacterium sp.
-
additional information
2-oxobutyrate, 2-oxovalerate, 2-oxoglutarate, 3-oxoglutarate cannot replace pyruvate and is no C1-donor
485816
Propionibacterium sp.
?
-
-
-
-
propionyl-CoA + oxaloacetate
-
485816
Propionibacterium sp.
(S)-methylmalonyl-CoA + pyruvate
-
485816
Propionibacterium sp.
r
propionyl-CoA + oxaloacetate
-
485816
Propionibacterium sp.
(S)-methylmalonyl-CoA + pyruvate
enzyme specific for the S isomer
485816
Propionibacterium sp.
r
Subunits
Subunits
Commentary
Organism
More
structure
Propionibacterium sp.
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
5.5
7.8
broad
Propionibacterium sp.
Cofactor
Cofactor
Commentary
Organism
Structure
biotin
biotinyl-enzyme, 6 mol per 18S and 4 mol per 16S enzyme species; requirement
Propionibacterium sp.
additional information
no ATP requirement
Propionibacterium sp.
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.000018
-
oxalate
-
Propionibacterium sp.
0.00004
-
(S)-methylmalonyl-CoA
-
Propionibacterium sp.
0.00049
-
propionyl-CoA
-
Propionibacterium sp.
0.0007
-
oxaloacetate
-
Propionibacterium sp.
0.003
0.007
propionyl pantetheine
-
Propionibacterium sp.
0.003
-
3-methyloxaloacetate
-
Propionibacterium sp.
0.0063
-
coenzyme A
-
Propionibacterium sp.
0.0089
-
pyruvate
-
Propionibacterium sp.
0.025
-
2-oxobutyrate
-
Propionibacterium sp.
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
biotin
biotinyl-enzyme, 6 mol per 18S and 4 mol per 16S enzyme species; requirement
Propionibacterium sp.
additional information
no ATP requirement
Propionibacterium sp.
General Stability (protein specific)
General Stability
Organism
alkaline pH, low ionic strength, monovalent ions, low protein concentration and elevated temperatures favor dissociation to inactive 5S, 6S and 1.3S subunits
Propionibacterium sp.
glycerol, 20% retards dissociation of 12S and 6S-biotinyl subunit
Propionibacterium sp.
polyvalent anions stabilize
Propionibacterium sp.
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
(S)-methylmalonyl-CoA
-
Propionibacterium sp.
2-oxobutyrate
-
Propionibacterium sp.
3-methyloxaloacetate
strong
Propionibacterium sp.
Avidin
strong
Propionibacterium sp.
coenzyme A
-
Propionibacterium sp.
additional information
no inhibition by metal chelating agents, such as EDTA
Propionibacterium sp.
oxalate
-
Propionibacterium sp.
oxaloacetate
-
Propionibacterium sp.
propionyl pantetheine
-
Propionibacterium sp.
propionyl-CoA
-
Propionibacterium sp.
pyruvate
-
Propionibacterium sp.
SH-reagents
weak
Propionibacterium sp.
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.000018
-
oxalate
-
Propionibacterium sp.
0.00004
-
(S)-methylmalonyl-CoA
-
Propionibacterium sp.
0.00049
-
propionyl-CoA
-
Propionibacterium sp.
0.0007
-
oxaloacetate
-
Propionibacterium sp.
0.003
0.007
propionyl pantetheine
-
Propionibacterium sp.
0.003
-
3-methyloxaloacetate
-
Propionibacterium sp.
0.0063
-
coenzyme A
-
Propionibacterium sp.
0.0089
-
pyruvate
-
Propionibacterium sp.
0.025
-
2-oxobutyrate
-
Propionibacterium sp.
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
kinetics and mechanism
Propionibacterium sp.
0.0077
-
(2S)-methylmalonyl-coenzyme A
-
Propionibacterium sp.
0.034
-
propionyl-CoA
-
Propionibacterium sp.
0.035
-
malonyl-CoA
-
Propionibacterium sp.
0.063
-
oxaloacetate
-
Propionibacterium sp.
0.25
-
butyryl-CoA
-
Propionibacterium sp.
0.5
-
acetyl-CoA
-
Propionibacterium sp.
0.77
-
pyruvate
-
Propionibacterium sp.
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytoplasm
-
Propionibacterium sp.
5737
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Co2+
requirement
Propionibacterium sp.
additional information
no additional metal requirement
Propionibacterium sp.
Zn2+
requirement, can replace Co2+
Propionibacterium sp.
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
additional information
-
two active forms of enzyme: 18S and 16S, the 16S species arises from 18S species by loss of a 6S biotin, Co, Zn subunit
Propionibacterium sp.
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
propionyl-CoA + oxaloacetate
Propionibacterium sp.
-
(S)-methylmalonyl-CoA + pyruvate
-
Propionibacterium sp.
r
Purification (Commentary) (protein specific)
Commentary
Organism
-
Propionibacterium sp.
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [Ámol/min/mg]
Specific Activity Maximum [Ámol/min/mg]
Commentary
Organism
40
-
-
Propionibacterium sp.
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
acetoacetyl-CoA + oxaloacetate
carboxylation at about 2.5% the rate of propionyl-CoA
485816
Propionibacterium sp.
3-oxoglutaryl-CoA + pyruvate
-
485816
Propionibacterium sp.
-
acetyl-CoA + oxaloacetate
carboxylation at about 50% the rate of propionyl-CoA
485816
Propionibacterium sp.
malonyl-CoA + pyruvate
-
485816
Propionibacterium sp.
r
butyryl-CoA + oxaloacetate
carboxylation at about 10% the rate of propionyl-CoA
485816
Propionibacterium sp.
ethylmalonyl-CoA + pyruvate
-
485816
Propionibacterium sp.
-
additional information
2-oxobutyrate, 2-oxovalerate, 2-oxoglutarate, 3-oxoglutarate cannot replace pyruvate and is no C1-donor
485816
Propionibacterium sp.
?
-
-
-
-
propionyl-CoA + oxaloacetate
-
485816
Propionibacterium sp.
(S)-methylmalonyl-CoA + pyruvate
-
485816
Propionibacterium sp.
r
propionyl-CoA + oxaloacetate
-
485816
Propionibacterium sp.
(S)-methylmalonyl-CoA + pyruvate
enzyme specific for the S isomer
485816
Propionibacterium sp.
r
Subunits (protein specific)
Subunits
Commentary
Organism
More
structure
Propionibacterium sp.
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
5.5
7.8
broad
Propionibacterium sp.
Other publictions for EC 2.1.3.1
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)
737181
Wang
-
Metabolic engineering of Propi ...
Propionibacterium freudenreichii, Propionibacterium freudenreichii DSM 4902
Process Biochem.
50
194-204
2015
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1
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1
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2
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1
1
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719105
Jia
Enhanced production of ansamit ...
Actinosynnema pretiosum, Actinosynnema pretiosum ATCC 31565
Biores. Technol.
102
10147-10150
2011
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2
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4
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1
1
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689897
Bhat
The 5S subunit of transcarboxy ...
Propionibacterium freudenreichii subsp. shermanii
Protein Pept. Lett.
15
624-629
2008
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1
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5
1
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1
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1
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1
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674054
Herve
Transcarboxylase mRNA: a marke ...
Propionibacterium freudenreichii
Int. J. Food Microbiol.
113
303-314
2007
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3
-
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6
1
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3
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1
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2
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1
1
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6
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3
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6
1
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1
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2
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1
1
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6
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676760
Kumar Bhat
New and easy strategy for clon ...
Propionibacterium freudenreichii subsp. shermanii
Prep. Biochem. Biotechnol.
37
13-26
2007
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1
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4
1
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2
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2
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684167
Yamada
Crystallization and preliminar ...
Corynebacterium glutamicum
Acta Crystallogr. Sect. F
63
120-122
2007
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1
1
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1
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3
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672701
Suwannakham
Enhanced propionic acid fermen ...
Acidipropionibacterium acidipropionici
Biotechnol. Bioeng.
91
325-337
2005
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1
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657477
Hall
Expression and crystallization ...
Propionibacterium freudenreichii subsp. shermanii
Acta Crystallogr. Sect. D
D60
521-523
2004
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1
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658551
Hall
Transcarboxylase 5S structures ...
Propionibacterium freudenreichii subsp. shermanii
EMBO J.
23
3621-3631
2004
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1
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3
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658542
Hall
Transcarboxylase 12S crystal s ...
Propionibacterium freudenreichii subsp. shermanii
EMBO J.
22
2334-2347
2003
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1
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485825
Rivera-Hainaj
Characterization of the carbox ...
Propionibacterium freudenreichii subsp. shermanii
Biochemistry
41
2191-2197
2002
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1
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485826
Zheng
Substrate binding induces a co ...
Propionibacterium freudenreichii subsp. shermanii
Biochemistry
41
10741-10746
2002
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1
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1
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485834
Jank
Expression and biotinylation o ...
Propionibacterium freudenreichii subsp. shermanii
Protein Expr. Purif.
17
123-127
1999
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-
1
-
-
-
-
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3
-
1
1
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1
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1
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1
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485833
Choi
Effects of rapeseed oil on act ...
Streptomyces fradiae, Streptomyces fradiae T1558
Biosci. Biotechnol. Biochem.
62
902-906
1998
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1
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1
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2
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4
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2
4
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6
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1
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1
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2
4
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6
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1
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-
485827
Shenoy
Dissection of the biotinyl sub ...
Propionibacterium freudenreichii subsp. shermanii
J. Biol. Chem.
268
2232-2238
1993
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1
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1
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1
1
1
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1
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1
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1
1
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1
1
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-
-
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-
-
485828
Shenoy
The nonbiotinylated form of th ...
Propionibacterium freudenreichii subsp. shermanii
Protein Expr. Purif.
4
85-94
1993
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1
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1
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2
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1
1
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1
1
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1
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1
1
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1
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1
1
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485829
Shenoy
The conserved methionines of t ...
Propionibacterium freudenreichii subsp. shermanii
Arch. Biochem. Biophys.
304
359-366
1993
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1
-
2
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1
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3
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1
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1
1
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1
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1
1
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2
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1
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1
1
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485830
Woo
Effect of deletion from the ca ...
Propionibacterium freudenreichii subsp. shermanii
J. Biol. Chem.
268
16413-16419
1993
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1
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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
1
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1
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1
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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-
-
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485831
Xie
Purification and characterizat ...
Propionibacterium freudenreichii subsp. shermanii
Protein Expr. Purif.
4
456-464
1993
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-
1
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2
1
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3
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1
1
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5
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1
1
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1
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1
1
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2
1
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1
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5
-
1
1
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485832
Shenoy
Identification and characteriz ...
Propionibacterium freudenreichii subsp. shermanii
Biochemistry
32
10750-10756
1993
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-
1
1
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1
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1
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3
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4
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1
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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4
-
1
1
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1
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-
485822
Shenoy
The importance of methionine r ...
Propionibacterium freudenreichii subsp. shermanii
J. Biol. Chem.
267
18407-18412
1992
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1
-
7
-
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3
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1
1
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2
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1
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1
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1
1
1
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1
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1
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1
1
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7
-
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3
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1
1
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1
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1
-
1
1
1
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1
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-
4552
Hoffmann
The carboxyltransferase activi ...
Veillonella parvula
Eur. J. Biochem.
179
645-650
1989
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-
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1
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2
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485823
O'Keefe
Biotin-dependent carboxylation ...
Propionibacterium freudenreichii subsp. shermanii
Biochemistry
25
6077-6084
1986
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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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485820
Harmon
Stabilization of the quaternar ...
Propionibacterium freudenreichii subsp. shermanii
Biochemistry
21
2847-2852
1982
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1
1
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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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1
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2
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3
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
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2
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3
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485821
Stubbe
Are carboxylations involving b ...
Propionibacterium sp.
J. Biol. Chem.
255
236-242
1980
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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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1
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1
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1
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485819
Maloy
Amino acid sequence of the bio ...
Propionibacterium freudenreichii subsp. shermanii
J. Biol. Chem.
254
11615-11622
1979
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-
-
-
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1
2
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4
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1
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1
1
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2
1
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1
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1
2
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1
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1
1
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2
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485818
Berger
Purification of the subunits o ...
Propionibacterium freudenreichii subsp. shermanii
J. Biol. Chem.
250
927-933
1975
-
-
-
-
-
1
1
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1
1
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1
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1
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1
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2
1
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1
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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1
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1
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2
1
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1
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485816
Wood
-
Transcarboxylase ...
Propionibacterium sp.
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
6
83-115
1972
-
-
-
-
-
3
12
8
1
3
1
1
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1
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-
1
1
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1
-
6
1
-
-
-
-
1
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-
2
9
-
-
-
-
-
2
-
-
3
-
12
9
8
1
3
1
1
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-
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1
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1
-
6
1
-
-
-
-
1
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-
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485817
Swick
The role of transcarboxylase i ...
Canis lupus familiaris, Propionibacterium freudenreichii subsp. shermanii, Propionibacterium freudenreichii subsp. shermanii 52W
Proc. Natl. Acad. Sci. USA
46
28-41
1960
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1
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2
2
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3
-
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1
-
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2
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1
12
-
1
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2
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-
-
2
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1
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2
2
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1
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2
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1
12
-
1
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