BRENDA - Enzyme Database show
show all sequences of 1.14.14.57

Characterisation of taurochenodeoxycholic acid 6alpha-hydroxylase from pig liver microsomes

Araya, Z.; Hellman, U.; Hansson, R.; Eur. J. Biochem. 231, 855-861 (1995)

Data extracted from this reference:

KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0629
-
taurochenodeoxycholate
-
Sus scrofa
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
microsome
-
Sus scrofa
-
-
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
53000
-
x * 53000, SDS-PAGE
Sus scrofa
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Sus scrofa
-
-
-
Purification (Commentary)
Commentary
Organism
-
Sus scrofa
Source Tissue
Source Tissue
Commentary
Organism
Textmining
liver
-
Sus scrofa
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
lithocholate + [reduced NADPH-hemoprotein reductase] + O2
activity is low compared to activity with taurochenodeoxycholate
658588
Sus scrofa
hyocholate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
taurochenodeoxycholate + [reduced NADPH-hemoprotein reductase] + O2
-
658588
Sus scrofa
taurohyocholate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
Subunits
Subunits
Commentary
Organism
?
x * 53000, SDS-PAGE
Sus scrofa
Cofactor
Cofactor
Commentary
Organism
Structure
cytochrome P450
-
Sus scrofa
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
cytochrome P450
-
Sus scrofa
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0629
-
taurochenodeoxycholate
-
Sus scrofa
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
microsome
-
Sus scrofa
-
-
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
53000
-
x * 53000, SDS-PAGE
Sus scrofa
Purification (Commentary) (protein specific)
Commentary
Organism
-
Sus scrofa
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
liver
-
Sus scrofa
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
lithocholate + [reduced NADPH-hemoprotein reductase] + O2
activity is low compared to activity with taurochenodeoxycholate
658588
Sus scrofa
hyocholate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
taurochenodeoxycholate + [reduced NADPH-hemoprotein reductase] + O2
-
658588
Sus scrofa
taurohyocholate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 53000, SDS-PAGE
Sus scrofa
Other publictions for EC 1.14.14.57
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)
745513
Cheng
Intestinal CYP3A4 protects ag ...
Mus musculus
J. Lipid Res.
55
455-465
2014
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1
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657837
Lundell
The porcine taurochenodeoxycho ...
Sus scrofa
Biochem. J.
378
1053-1058
2004
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1
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2
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1
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657550
Russell
The enzymes, regulation, and g ...
Homo sapiens
Annu. Rev. Biochem.
72
137-174
2003
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744381
Lundell
Gene structure of pig sterol ...
Sus scrofa
Biochim. Biophys. Acta
1634
86-96
2003
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6
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4
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1
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4
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1
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659165
Kramer
Identification of the bile aci ...
Oryctolagus cuniculus
J. Biol. Chem.
276
7291-7301
2001
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659166
Lundell
Cloning and expression of a pi ...
Sus scrofa
J. Biol. Chem.
276
9606-9612
2001
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744378
Araya
6alpha-hydroxylation of tauro ...
Homo sapiens
Biochim. Biophys. Acta
1438
47-54
1999
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1
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1
1
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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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1
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3
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1
1
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658588
Araya
Characterisation of taurocheno ...
Sus scrofa
Eur. J. Biochem.
231
855-861
1995
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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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2
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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