BRENDA - Enzyme Database show
show all sequences of 2.1.3.1

The importance of methionine residues for the catalysis of the biotin enzyme, transcarboxylase. Analysis by site-directed mutagenesis

Shenoy, B.C.; Xie, Y.; Park, V.L.; Kumar, G.K.; Beegen, H.; Wood, H.G.; Samols, D.; J. Biol. Chem. 267, 18407-18412 (1992)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
1.3S subunit cloned and expressed in Escherichia coli
Propionibacterium freudenreichii subsp. shermanii
Engineering
Amino acid exchange
Commentary
Organism
A87G
Km not significantly changed, significantly reduced kcat
Propionibacterium freudenreichii subsp. shermanii
M88A
Km not significantly changed, significantly reduced kcat
Propionibacterium freudenreichii subsp. shermanii
M88C
Km not significantly changed, significantly reduced kcat
Propionibacterium freudenreichii subsp. shermanii
M88L
Km not significantly changed, significantly reduced kcat
Propionibacterium freudenreichii subsp. shermanii
M88T
Km not significantly changed, significantly reduced kcat
Propionibacterium freudenreichii subsp. shermanii
M90L
Km and kcat not significantly changed
Propionibacterium freudenreichii subsp. shermanii
additional information
double mutant A87M and M88A
Propionibacterium freudenreichii subsp. shermanii
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
kinetic parameters of wild-type and mutant enzyme
Propionibacterium freudenreichii subsp. shermanii
0.0044
-
pyruvate
5S-subunit
Propionibacterium freudenreichii subsp. shermanii
0.0077
-
(2S)-methylmalonyl-coenzyme A
-
Propionibacterium freudenreichii subsp. shermanii
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Co2+
requirement
Propionibacterium freudenreichii subsp. shermanii
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
120000
-
the 26S holoenzyme consists of a hexameric central 12S subunit, 360000 Da and six peripheral dimeric 5S subunits, 6 * 120000 Da each of which is linked to the central subunit by 2 biotinyl 1.3S subunits, 12 * MW 12000
Propionibacterium freudenreichii subsp. shermanii
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Propionibacterium freudenreichii subsp. shermanii
-
-
-
Purification (Commentary)
Commentary
Organism
recombinant enzyme and mutant 1.3S subunit; separation of transcarboxylase complexes from uncombined 12S, 5S and 1.3S subunits by gel filtration
Propionibacterium freudenreichii subsp. shermanii
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
comparison of wild-type and mutant enzymes
Propionibacterium freudenreichii subsp. shermanii
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
propionyl-CoA + oxaloacetate
-
485822
Propionibacterium freudenreichii subsp. shermanii
(S)-methylmalonyl-CoA + pyruvate
-
485822
Propionibacterium freudenreichii subsp. shermanii
r
Subunits
Subunits
Commentary
Organism
More
amino acid sequence of biotinyl subunit; the 26S holoenzyme consists of a hexameric central 12S subunit, 360000 Da and six peripheral dimeric 5S subunits, 6 * 120000 Da each of which is linked to the central subunit by 2 biotinyl 1.3S subunits, 12 * MW 12000
Propionibacterium freudenreichii subsp. shermanii
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
assay at
Propionibacterium freudenreichii subsp. shermanii
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
2530 nmol oxaloacetate per nmol biotin per min
Propionibacterium freudenreichii subsp. shermanii
Cofactor
Cofactor
Commentary
Organism
Structure
biotin
covalently linked to the 1.3 subunit to the epsilon-amino group of Lys-89, which lies in the conserved sequence Ala-Met-Lys-Met
Propionibacterium freudenreichii subsp. shermanii
Cloned(Commentary) (protein specific)
Commentary
Organism
1.3S subunit cloned and expressed in Escherichia coli
Propionibacterium freudenreichii subsp. shermanii
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
biotin
covalently linked to the 1.3 subunit to the epsilon-amino group of Lys-89, which lies in the conserved sequence Ala-Met-Lys-Met
Propionibacterium freudenreichii subsp. shermanii
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
A87G
Km not significantly changed, significantly reduced kcat
Propionibacterium freudenreichii subsp. shermanii
M88A
Km not significantly changed, significantly reduced kcat
Propionibacterium freudenreichii subsp. shermanii
M88C
Km not significantly changed, significantly reduced kcat
Propionibacterium freudenreichii subsp. shermanii
M88L
Km not significantly changed, significantly reduced kcat
Propionibacterium freudenreichii subsp. shermanii
M88T
Km not significantly changed, significantly reduced kcat
Propionibacterium freudenreichii subsp. shermanii
M90L
Km and kcat not significantly changed
Propionibacterium freudenreichii subsp. shermanii
additional information
double mutant A87M and M88A
Propionibacterium freudenreichii subsp. shermanii
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
kinetic parameters of wild-type and mutant enzyme
Propionibacterium freudenreichii subsp. shermanii
0.0044
-
pyruvate
5S-subunit
Propionibacterium freudenreichii subsp. shermanii
0.0077
-
(2S)-methylmalonyl-coenzyme A
-
Propionibacterium freudenreichii subsp. shermanii
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Co2+
requirement
Propionibacterium freudenreichii subsp. shermanii
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
120000
-
the 26S holoenzyme consists of a hexameric central 12S subunit, 360000 Da and six peripheral dimeric 5S subunits, 6 * 120000 Da each of which is linked to the central subunit by 2 biotinyl 1.3S subunits, 12 * MW 12000
Propionibacterium freudenreichii subsp. shermanii
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant enzyme and mutant 1.3S subunit; separation of transcarboxylase complexes from uncombined 12S, 5S and 1.3S subunits by gel filtration
Propionibacterium freudenreichii subsp. shermanii
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
comparison of wild-type and mutant enzymes
Propionibacterium freudenreichii subsp. shermanii
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
propionyl-CoA + oxaloacetate
-
485822
Propionibacterium freudenreichii subsp. shermanii
(S)-methylmalonyl-CoA + pyruvate
-
485822
Propionibacterium freudenreichii subsp. shermanii
r
Subunits (protein specific)
Subunits
Commentary
Organism
More
amino acid sequence of biotinyl subunit; the 26S holoenzyme consists of a hexameric central 12S subunit, 360000 Da and six peripheral dimeric 5S subunits, 6 * 120000 Da each of which is linked to the central subunit by 2 biotinyl 1.3S subunits, 12 * MW 12000
Propionibacterium freudenreichii subsp. shermanii
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
assay at
Propionibacterium freudenreichii subsp. shermanii
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
2530 nmol oxaloacetate per nmol biotin per min
Propionibacterium freudenreichii subsp. shermanii
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
-
-
1
-
1
-
-
-
-
-
-
2
-
3
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
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-
1
-
-
1
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-
-
-
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-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
719105
Jia
Enhanced production of ansamit ...
Actinosynnema pretiosum, Actinosynnema pretiosum ATCC 31565
Biores. Technol.
102
10147-10150
2011
-
-
-
-
-
-
2
-
-
4
-
-
-
3
-
-
-
-
-
-
-
-
-
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2
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4
-
-
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-
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
689897
Bhat
The 5S subunit of transcarboxy ...
Propionibacterium freudenreichii subsp. shermanii
Protein Pept. Lett.
15
624-629
2008
-
-
1
-
-
-
-
-
-
-
5
1
-
1
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
1
-
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-
-
1
1
-
-
-
-
-
-
-
-
-
5
1
-
-
-
1
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
674054
Herve
Transcarboxylase mRNA: a marke ...
Propionibacterium freudenreichii
Int. J. Food Microbiol.
113
303-314
2007
-
3
-
-
-
-
-
-
-
-
6
1
-
3
-
-
1
-
-
2
-
-
1
1
-
-
-
-
-
-
-
-
-
6
-
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3
-
-
-
-
-
-
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-
-
-
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6
1
-
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1
-
2
-
-
1
1
-
-
-
-
-
-
-
6
-
-
-
-
-
-
676760
Kumar Bhat
New and easy strategy for clon ...
Propionibacterium freudenreichii subsp. shermanii
Prep. Biochem. Biotechnol.
37
13-26
2007
-
-
1
-
-
-
-
-
-
-
4
1
-
2
-
-
1
-
-
-
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1
1
2
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1
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1
1
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4
1
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1
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1
1
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
684167
Yamada
Crystallization and preliminar ...
Corynebacterium glutamicum
Acta Crystallogr. Sect. F
63
120-122
2007
-
-
1
1
-
-
-
-
-
-
1
-
-
3
-
-
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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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
672701
Suwannakham
Enhanced propionic acid fermen ...
Acidipropionibacterium acidipropionici
Biotechnol. Bioeng.
91
325-337
2005
-
-
-
-
1
-
-
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2
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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
-
-
-
1
-
-
-
-
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-
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2
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1
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658551
Hall
Transcarboxylase 5S structures ...
Propionibacterium freudenreichii subsp. shermanii
EMBO J.
23
3621-3631
2004
-
-
-
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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658542
Hall
Transcarboxylase 12S crystal s ...
Propionibacterium freudenreichii subsp. shermanii
EMBO J.
22
2334-2347
2003
-
-
-
1
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-
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3
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1
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1
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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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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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485826
Zheng
Substrate binding induces a co ...
Propionibacterium freudenreichii subsp. shermanii
Biochemistry
41
10741-10746
2002
-
-
-
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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2
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
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1
1
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1
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-
-
-
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485833
Choi
Effects of rapeseed oil on act ...
Streptomyces fradiae, Streptomyces fradiae T1558
Biosci. Biotechnol. Biochem.
62
902-906
1998
-
1
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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
1
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1
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1
1
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1
1
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1
1
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485828
Shenoy
The nonbiotinylated form of th ...
Propionibacterium freudenreichii subsp. shermanii
Protein Expr. Purif.
4
85-94
1993
-
-
1
-
-
-
-
-
-
-
1
-
-
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
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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
-
-
1
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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
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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
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1
1
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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
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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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4
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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
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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
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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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1
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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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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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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
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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
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3
12
8
1
3
1
1
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1
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1
1
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1
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6
1
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1
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2
9
-
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2
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3
-
12
9
8
1
3
1
1
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1
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1
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6
1
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1
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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
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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
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1
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