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show all sequences of 1.3.8.13

The fixA and fixB genes are necessary for anaerobic carnitine reduction in Escherichia coli

Walt, A.; Kahn, M.; J. Bacteriol. 184, 4044-4047 (2002)

Data extracted from this reference:

Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
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General Information
General Information
Commentary
Organism
physiological function
mutants lacking fixA and fixB proteins are unable to use carnitine anaerobically as the sole terminal electron acceptor and that these mutants are unable to metabolize carnitine to gamma-butyrobetaine. FixA and FixB proteins may be involved in bringing reductant to crotonobetainyl-CoA reductase CaiA
Escherichia coli
General Information (protein specific)
General Information
Commentary
Organism
physiological function
mutants lacking fixA and fixB proteins are unable to use carnitine anaerobically as the sole terminal electron acceptor and that these mutants are unable to metabolize carnitine to gamma-butyrobetaine. FixA and FixB proteins may be involved in bringing reductant to crotonobetainyl-CoA reductase CaiA
Escherichia coli
Other publictions for EC 1.3.8.13
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)
724139
Engemann
Identification and functional ...
Proteus sp., Proteus sp. LE138
Arch. Microbiol.
183
176-189
2005
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740600
Walt
The fixA and fixB genes are ne ...
Escherichia coli
J. Bacteriol.
184
4044-4047
2002
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1
1
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740464
Engemann
Epigenetic regulation of carni ...
Proteus sp., Proteus sp. LE138
FEMS Microbiol. Lett.
196
1-6
2001
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2
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2
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740036
Elssner
Isolation, identification, and ...
Escherichia coli
Biochemistry
39
10761-10769
2000
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740094
Preusser
Crotonobetaine reductase from ...
Escherichia coli
Biochim. Biophys. Acta
1431
166-178
1999
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739868
Roth
Crotonobetaine reductase from ...
Escherichia coli
Antonie van Leeuwenhoek
65
63-69
1994
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12
1
1
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