BRENDA - Enzyme Database show
show all sequences of 1.1.1.52

Reversible enzymatic oxidation of bile acids

Hayaishi, O.; Saito, Y.; Jakoby, W.B.; Stohlman, E.F.; Arch. Biochem. Biophys. 56, 554-555 (1955)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
additional information
SH-groups are required for activity
Escherichia sp.
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytoplasm
-
Escherichia sp.
5737
-
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
3alpha-hydroxy-5beta-cholanate + NAD+
Escherichia sp.
-
3-oxo-5beta-cholanate + NADH
-
-
r
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia sp.
-
tentative identification: E. freundii
-
Purification (Commentary)
Commentary
Organism
partial
Escherichia sp.
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3alpha-hydroxy-5beta-cholanate + NAD+
-
287082
Escherichia sp.
3-oxo-5beta-cholanate + NADH
-
-
-
r
3alpha-hydroxy-5beta-cholanate + NAD+
i.e. lithocholic acid
287082
Escherichia sp.
3-oxo-5beta-cholanate + NADH
-
287082
Escherichia sp.
r
3alpha-hydroxy-bis-norcholanic acid + NAD+
oxidation at the same rate as hydroxycholanic acid
287082
Escherichia sp.
3-oxo-bis-norcholanic acid + NADH
-
-
-
r
3alpha-hydroxy-norcholanic acid + NAD+
oxidation at the same rate as hydroxycholanic acid
287082
Escherichia sp.
3-oxo-norcholanic acid + NADH
-
-
-
r
cholic acid + NAD+
oxidation at the same rate as hydroxycholanic acid
287082
Escherichia sp.
7alpha,12alpha-dihydroxy-3-oxo-5beta-cholan-24-oic acid + NADH
-
-
-
r
dehydrocholic acid + NADH
i.e. 3,7,12-trioxocholan-24-oic acid
287082
Escherichia sp.
3-hydroxy-7,12-dihydroxy-5beta-cholan-24-oic acid + NAD+
-
-
-
r
deoxycholic acid + NAD+
oxidation at the same rate as hydroxycholanic acid
287082
Escherichia sp.
12alpha-hydroxy-3-oxo-5beta-cholan-24-oic acid + NADH + H+
-
-
-
r
additional information
no substrates: androsterone and tetrahydrocortisone, methylation of carboxyl group or reduction to alcohol inactivates
287082
Escherichia sp.
?
-
-
-
-
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
26
-
assay at
Escherichia sp.
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
10.4
-
oxidation, assay at
Escherichia sp.
pH Range
pH Minimum
pH Maximum
Commentary
Organism
additional information
-
oxidation proceeds at alkaline and reduction favorably at neutral pH-values
Escherichia sp.
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
NADP+ cannot replace NAD+
Escherichia sp.
NADH
-
Escherichia sp.
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
additional information
SH-groups are required for activity
Escherichia sp.
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
NADP+ cannot replace NAD+
Escherichia sp.
NADH
-
Escherichia sp.
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytoplasm
-
Escherichia sp.
5737
-
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
3alpha-hydroxy-5beta-cholanate + NAD+
Escherichia sp.
-
3-oxo-5beta-cholanate + NADH
-
-
r
Purification (Commentary) (protein specific)
Commentary
Organism
partial
Escherichia sp.
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3alpha-hydroxy-5beta-cholanate + NAD+
-
287082
Escherichia sp.
3-oxo-5beta-cholanate + NADH
-
-
-
r
3alpha-hydroxy-5beta-cholanate + NAD+
i.e. lithocholic acid
287082
Escherichia sp.
3-oxo-5beta-cholanate + NADH
-
287082
Escherichia sp.
r
3alpha-hydroxy-bis-norcholanic acid + NAD+
oxidation at the same rate as hydroxycholanic acid
287082
Escherichia sp.
3-oxo-bis-norcholanic acid + NADH
-
-
-
r
3alpha-hydroxy-norcholanic acid + NAD+
oxidation at the same rate as hydroxycholanic acid
287082
Escherichia sp.
3-oxo-norcholanic acid + NADH
-
-
-
r
cholic acid + NAD+
oxidation at the same rate as hydroxycholanic acid
287082
Escherichia sp.
7alpha,12alpha-dihydroxy-3-oxo-5beta-cholan-24-oic acid + NADH
-
-
-
r
dehydrocholic acid + NADH
i.e. 3,7,12-trioxocholan-24-oic acid
287082
Escherichia sp.
3-hydroxy-7,12-dihydroxy-5beta-cholan-24-oic acid + NAD+
-
-
-
r
deoxycholic acid + NAD+
oxidation at the same rate as hydroxycholanic acid
287082
Escherichia sp.
12alpha-hydroxy-3-oxo-5beta-cholan-24-oic acid + NADH + H+
-
-
-
r
additional information
no substrates: androsterone and tetrahydrocortisone, methylation of carboxyl group or reduction to alcohol inactivates
287082
Escherichia sp.
?
-
-
-
-
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
26
-
assay at
Escherichia sp.
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
10.4
-
oxidation, assay at
Escherichia sp.
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
additional information
-
oxidation proceeds at alkaline and reduction favorably at neutral pH-values
Escherichia sp.
Other publictions for EC 1.1.1.52
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)
287082
Hayaishi
Reversible enzymatic oxidation ...
Escherichia sp.
Arch. Biochem. Biophys.
56
554-555
1955
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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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8
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1
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