BRENDA - Enzyme Database show
show all sequences of 2.1.3.1

Stabilization of the quaternary structure of transcarboxylase by cobalt (II) ions

Harmon, F.R.; Goss, N.H.; Wood, H.G.; Biochemistry 21, 2847-2852 (1982)

Data extracted from this reference:

General Stability
General Stability
Organism
Co2+ protects
Propionibacterium freudenreichii subsp. shermanii
Inhibitors
Inhibitors
Commentary
Organism
Structure
Guanidinium chloride
Co2+ protects
Propionibacterium freudenreichii subsp. shermanii
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Co2+
3 types of Co2+: tightly i.e. catalytic, not so tightly, and weakly bound, above 2 mM, stabilizes quarternary structure, no exchange between catalytic and stabilizing Co2+; no formation of Co-thiol bonds; requirement
Propionibacterium freudenreichii subsp. shermanii
Zn2+
slightly stabilizing
Propionibacterium freudenreichii subsp. shermanii
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Propionibacterium freudenreichii subsp. shermanii
-
-
-
Oxidation Stability
Oxidation Stability
Organism
oxygen prevents reassembly of dissociated subunits
Propionibacterium freudenreichii subsp. shermanii
Reaction
Reaction
Commentary
Organism
(S)-methylmalonyl-CoA + pyruvate = propanoyl-CoA + oxaloacetate
mechanism
Propionibacterium freudenreichii subsp. shermanii
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
33.6
-
-
Propionibacterium freudenreichii subsp. shermanii
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
assay at
Propionibacterium freudenreichii subsp. shermanii
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
25
-
dissociation and rapid loss of activity in dilute solution in alkaline 50 mM buffer (t1/2: 12 min), Co2+ protects, Zn2+ protects slightly (t1/2: 22 min)
Propionibacterium freudenreichii subsp. shermanii
50
-
denaturation within 1 min, Co2+ protects, Zn2+ protects slightly
Propionibacterium freudenreichii subsp. shermanii
pH Stability
pH Stability
pH Stability Maximum
Commentary
Organism
5.5
-
26S-form stable
Propionibacterium freudenreichii subsp. shermanii
8
-
dilute solution, 50 mM buffer, 25°C: enzyme dissociates into subunits and rapidly loses activity, Co2+ protects, Zn2+ protects slightly
Propionibacterium freudenreichii subsp. shermanii
9
-
enzyme dissociates into 12SH, 5SE, 6SE and 6SH subunits, in the presence of Co2+: the 6SE subunits binds to 12SH subunit
Propionibacterium freudenreichii subsp. shermanii
Cofactor
Cofactor
Commentary
Organism
Structure
biotin
requirement
Propionibacterium freudenreichii subsp. shermanii
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
biotin
requirement
Propionibacterium freudenreichii subsp. shermanii
General Stability (protein specific)
General Stability
Organism
Co2+ protects
Propionibacterium freudenreichii subsp. shermanii
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
Guanidinium chloride
Co2+ protects
Propionibacterium freudenreichii subsp. shermanii
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Co2+
3 types of Co2+: tightly i.e. catalytic, not so tightly, and weakly bound, above 2 mM, stabilizes quarternary structure, no exchange between catalytic and stabilizing Co2+; no formation of Co-thiol bonds; requirement
Propionibacterium freudenreichii subsp. shermanii
Zn2+
slightly stabilizing
Propionibacterium freudenreichii subsp. shermanii
Oxidation Stability (protein specific)
Oxidation Stability
Organism
oxygen prevents reassembly of dissociated subunits
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
33.6
-
-
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
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
25
-
dissociation and rapid loss of activity in dilute solution in alkaline 50 mM buffer (t1/2: 12 min), Co2+ protects, Zn2+ protects slightly (t1/2: 22 min)
Propionibacterium freudenreichii subsp. shermanii
50
-
denaturation within 1 min, Co2+ protects, Zn2+ protects slightly
Propionibacterium freudenreichii subsp. shermanii
pH Stability (protein specific)
pH Stability
pH Stability Maximum
Commentary
Organism
5.5
-
26S-form stable
Propionibacterium freudenreichii subsp. shermanii
8
-
dilute solution, 50 mM buffer, 25°C: enzyme dissociates into subunits and rapidly loses activity, Co2+ protects, Zn2+ protects slightly
Propionibacterium freudenreichii subsp. shermanii
9
-
enzyme dissociates into 12SH, 5SE, 6SE and 6SH subunits, in the presence of Co2+: the 6SE subunits binds to 12SH subunit
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
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1
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1
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2
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3
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2
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1
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2
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-
2
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-
-
-
-
1
1
-
-
-
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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3
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4
-
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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
-
-
-
-
-
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
-
-
3
-
-
-
-
-
-
-
-
-
-
-
6
1
-
-
-
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
-
-
-
-
1
1
2
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
4
1
-
-
-
1
-
-
-
1
1
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
684167
Yamada
Crystallization and preliminar ...
Corynebacterium glutamicum
Acta Crystallogr. Sect. F
63
120-122
2007
-
-
1
1
-
-
-
-
-
-
1
-
-
3
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
672701
Suwannakham
Enhanced propionic acid fermen ...
Acidipropionibacterium acidipropionici
Biotechnol. Bioeng.
91
325-337
2005
-
-
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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-
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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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2
-
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1
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-
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
658551
Hall
Transcarboxylase 5S structures ...
Propionibacterium freudenreichii subsp. shermanii
EMBO J.
23
3621-3631
2004
-
-
-
1
-
-
-
-
-
-
-
-
-
3
-
-
-
1
-
-
-
-
-
1
-
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-
-
-
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-
-
-
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-
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-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
658542
Hall
Transcarboxylase 12S crystal s ...
Propionibacterium freudenreichii subsp. shermanii
EMBO J.
22
2334-2347
2003
-
-
-
1
-
-
-
-
-
-
-
-
-
3
-
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-
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-
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-
-
1
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1
-
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-
-
-
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-
-
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-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
485825
Rivera-Hainaj
Characterization of the carbox ...
Propionibacterium freudenreichii subsp. shermanii
Biochemistry
41
2191-2197
2002
-
-
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
1
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-
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1
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-
-
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
485826
Zheng
Substrate binding induces a co ...
Propionibacterium freudenreichii subsp. shermanii
Biochemistry
41
10741-10746
2002
-
-
-
1
-
-
-
-
-
-
-
-
-
1
-
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-
1
-
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-
-
2
1
-
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-
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-
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-
-
-
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-
-
1
-
-
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-
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-
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-
-
-
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
485834
Jank
Expression and biotinylation o ...
Propionibacterium freudenreichii subsp. shermanii
Protein Expr. Purif.
17
123-127
1999
-
-
1
-
-
-
-
-
-
-
-
-
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3
-
1
1
-
-
-
-
-
1
-
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1
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1
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
485833
Choi
Effects of rapeseed oil on act ...
Streptomyces fradiae, Streptomyces fradiae T1558
Biosci. Biotechnol. Biochem.
62
902-906
1998
-
1
-
-
-
-
-
-
1
-
-
2
-
4
-
-
-
-
-
2
4
-
6
-
-
-
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1
-
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1
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1
-
-
2
-
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-
-
-
2
4
-
6
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
485827
Shenoy
Dissection of the biotinyl sub ...
Propionibacterium freudenreichii subsp. shermanii
J. Biol. Chem.
268
2232-2238
1993
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
1
1
1
-
-
-
-
1
1
-
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1
-
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1
1
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1
1
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
485828
Shenoy
The nonbiotinylated form of th ...
Propionibacterium freudenreichii subsp. shermanii
Protein Expr. Purif.
4
85-94
1993
-
-
1
-
-
-
-
-
-
-
1
-
-
2
-
-
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
-
2
-
-
-
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1
-
-
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
-
-
-
-
-
-
-
-
-
-
-
-
-
-
485830
Woo
Effect of deletion from the ca ...
Propionibacterium freudenreichii subsp. shermanii
J. Biol. Chem.
268
16413-16419
1993
-
-
1
-
-
-
-
-
-
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1
-
-
3
-
1
-
1
-
-
1
-
1
1
-
-
-
-
-
-
-
1
-
-
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-
1
1
-
-
-
-
-
-
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1
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-
-
1
-
-
-
1
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
485831
Xie
Purification and characterizat ...
Propionibacterium freudenreichii subsp. shermanii
Protein Expr. Purif.
4
456-464
1993
-
-
1
-
-
-
-
-
-
2
1
-
-
3
-
-
1
1
-
-
5
-
1
1
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
2
1
-
-
-
-
1
-
-
5
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
485832
Shenoy
Identification and characteriz ...
Propionibacterium freudenreichii subsp. shermanii
Biochemistry
32
10750-10756
1993
-
-
1
1
-
-
1
-
-
-
1
-
-
3
-
-
-
-
-
-
4
-
1
1
-
-
1
-
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-
-
-
-
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-
-
-
1
-
1
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
4
-
1
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
485822
Shenoy
The importance of methionine r ...
Propionibacterium freudenreichii subsp. shermanii
J. Biol. Chem.
267
18407-18412
1992
-
-
1
-
7
-
-
3
-
1
1
-
-
2
-
-
1
-
-
-
1
-
1
1
1
-
-
1
-
-
-
1
-
-
-
-
-
1
1
-
7
-
-
-
-
3
-
1
1
-
-
-
-
1
-
-
1
-
1
1
1
-
-
1
-
-
-
-
-
-
-
-
-
-
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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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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-
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-
2
-
-
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-
-
-
-
-
-
-
-
-
-
-
-
485823
O'Keefe
Biotin-dependent carboxylation ...
Propionibacterium freudenreichii subsp. shermanii
Biochemistry
25
6077-6084
1986
-
-
-
-
-
-
-
1
-
1
-
-
-
1
-
-
-
1
-
-
1
-
1
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
1
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
485820
Harmon
Stabilization of the quaternar ...
Propionibacterium freudenreichii subsp. shermanii
Biochemistry
21
2847-2852
1982
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-
-
-
-
1
1
-
-
2
-
-
-
1
1
-
-
1
-
-
1
-
-
-
1
-
2
-
-
-
3
1
-
-
-
-
-
-
1
-
-
1
-
1
-
-
-
2
-
-
-
1
-
-
-
-
1
-
-
-
1
-
2
-
-
-
3
-
-
-
-
-
-
-
485821
Stubbe
Are carboxylations involving b ...
Propionibacterium sp.
J. Biol. Chem.
255
236-242
1980
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-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
-
1
-
-
-
-
1
-
1
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-
-
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-
-
1
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-
1
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-
1
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-
-
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-
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1
-
1
-
-
-
-
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-
-
-
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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
-
-
4
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
2
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
2
-
-
-
-
1
-
-
-
-
1
1
-
-
-
-
-
-
2
-
-
-
-
-
-
-
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
-
-
1
-
-
1
-
-
-
1
-
2
1
-
-
-
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-
-
1
1
-
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-
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-
-
1
-
-
1
-
1
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-
1
1
-
-
-
-
1
-
-
1
-
2
1
-
-
-
-
-
-
1
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-
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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
-
1
-
-
1
1
-
-
1
-
6
1
-
-
-
-
1
-
-
2
9
-
-
-
-
-
2
-
-
3
-
12
9
8
1
3
1
1
-
-
-
1
-
-
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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-
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1
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2
2
-
-
-
3
-
-
1
-
-
2
-
1
12
-
1
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-
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-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
1
-
-
2
2
-
-
-
-
-
1
-
2
-
1
12
-
1
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-
-
-
-
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-
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-