BRENDA - Enzyme Database show
show all sequences of 1.1.1.170

Investigation of the component reactions of oxidative sterol demethylation. Partial purification of a microsomal sterol 4alpha-carboxylic acid decarboxylase

Rahimtula, A.D.; Gaylor, J.L.; J. Biol. Chem. 247, 9-15 (1972)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
5alpha-cholest-7-en-3-one
2-9.3% inhibition between 16 and 130 nmol
Rattus sp.
5alpha-Cholest-7-en-3beta-ol
15.5-65% inhibition between 30 and 260 nmol
Rattus sp.
Fe2+
less than 25% inhibition at 1 mM
Rattus sp.
Zn2+
marked inhibition between 0.1 and 1 mM
Rattus sp.
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.007
-
3beta-hydroxy-4beta-methyl-5alpha-cholest-7-en-4alpha-oic acid
-
Rattus sp.
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
3beta-hydroxy-4alpha-methyl-5alpha-cholest-7-ene-4beta-carboxylate + NAD+
Rattus sp.
-
4alpha-methyl-5alpha-cholest-7-en-3-one + CO2 + NADH
-
Rattus sp.
?
3beta-hydroxy-4beta-methyl-5alpha-cholest-7-en-4alpha-oic acid + NAD+
Rattus sp.
no epimerization of 4beta-isomer into 4alpha-isomer
4alpha-methyl-5alpha-cholest-7-en-3-one + CO2 + NADH
-
Rattus sp.
ir
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Rattus sp.
-
-
-
Posttranslational Modification
Posttranslational Modification
Commentary
Organism
phospholipoprotein
presence of phosphatidylcholine and phosphatidylethanolamine, no loss of activity after removal of phospholipids
Rattus sp.
Purification (Commentary)
Commentary
Organism
near homogeneity, chromatography techniques, sodium deoxycholate solubilization
Rattus sp.
Source Tissue
Source Tissue
Commentary
Organism
Textmining
liver
-
Rattus sp.
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [Ámol/min/mg]
Specific Activity Maximum [Ámol/min/mg]
Commentary
Organism
0.11
-
-
Rattus sp.
Storage Stability
Storage Stability
Organism
4░C, 10 mM phosphate buffer, pH 7.4, no loss of activity within 2 weeks
Rattus sp.
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3beta-hydroxy-4alpha-methyl-5alpha-cholest-7-ene-4beta-carboxylate + NAD+
-
286111
Rattus sp.
4alpha-methyl-5alpha-cholest-7-en-3-one + CO2 + NADH
-
286111
Rattus sp.
?
3beta-hydroxy-4beta-methyl-5alpha-cholest-7-en-4alpha-oic acid + NAD+
no epimerization of 4beta-isomer into 4alpha-isomer
286111
Rattus sp.
4alpha-methyl-5alpha-cholest-7-en-3-one + CO2 + NADH
-
286111
Rattus sp.
ir
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
9
-
Rattus sp.
pH Range
pH Minimum
pH Maximum
Commentary
Organism
additional information
-
acidic pH results in a very low decarboxylation rate
Rattus sp.
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
can not be replaced by NADP+
Rattus sp.
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
can not be replaced by NADP+
Rattus sp.
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
5alpha-cholest-7-en-3-one
2-9.3% inhibition between 16 and 130 nmol
Rattus sp.
5alpha-Cholest-7-en-3beta-ol
15.5-65% inhibition between 30 and 260 nmol
Rattus sp.
Fe2+
less than 25% inhibition at 1 mM
Rattus sp.
Zn2+
marked inhibition between 0.1 and 1 mM
Rattus sp.
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.007
-
3beta-hydroxy-4beta-methyl-5alpha-cholest-7-en-4alpha-oic acid
-
Rattus sp.
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
3beta-hydroxy-4alpha-methyl-5alpha-cholest-7-ene-4beta-carboxylate + NAD+
Rattus sp.
-
4alpha-methyl-5alpha-cholest-7-en-3-one + CO2 + NADH
-
Rattus sp.
?
3beta-hydroxy-4beta-methyl-5alpha-cholest-7-en-4alpha-oic acid + NAD+
Rattus sp.
no epimerization of 4beta-isomer into 4alpha-isomer
4alpha-methyl-5alpha-cholest-7-en-3-one + CO2 + NADH
-
Rattus sp.
ir
Posttranslational Modification (protein specific)
Posttranslational Modification
Commentary
Organism
phospholipoprotein
presence of phosphatidylcholine and phosphatidylethanolamine, no loss of activity after removal of phospholipids
Rattus sp.
Purification (Commentary) (protein specific)
Commentary
Organism
near homogeneity, chromatography techniques, sodium deoxycholate solubilization
Rattus sp.
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
liver
-
Rattus sp.
-
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [Ámol/min/mg]
Specific Activity Maximum [Ámol/min/mg]
Commentary
Organism
0.11
-
-
Rattus sp.
Storage Stability (protein specific)
Storage Stability
Organism
4░C, 10 mM phosphate buffer, pH 7.4, no loss of activity within 2 weeks
Rattus sp.
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3beta-hydroxy-4alpha-methyl-5alpha-cholest-7-ene-4beta-carboxylate + NAD+
-
286111
Rattus sp.
4alpha-methyl-5alpha-cholest-7-en-3-one + CO2 + NADH
-
286111
Rattus sp.
?
3beta-hydroxy-4beta-methyl-5alpha-cholest-7-en-4alpha-oic acid + NAD+
no epimerization of 4beta-isomer into 4alpha-isomer
286111
Rattus sp.
4alpha-methyl-5alpha-cholest-7-en-3-one + CO2 + NADH
-
286111
Rattus sp.
ir
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
9
-
Rattus sp.
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
additional information
-
acidic pH results in a very low decarboxylation rate
Rattus sp.
Other publictions for EC 1.1.1.170
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)
656813
Lucas
Identification of two novel mu ...
Mus musculus
Mol. Genet. Metab.
80
227-233
2003
-
-
1
-
3
-
-
-
-
-
-
1
-
5
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
3
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
722377
Caldas
NSDHL, an enzyme involved in c ...
Homo sapiens
Hum. Mol. Genet.
12
2981-91
2003
-
-
-
-
-
-
-
-
2
-
-
-
-
3
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
723668
Gachotte
Characterization of the Saccha ...
Saccharomyces cerevisiae
Proc. Natl. Acad. Sci. USA
95
13794-9
1998
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
286111
Rahimtula
Investigation of the component ...
Rattus sp.
J. Biol. Chem.
247
9-15
1972
-
-
-
-
-
-
4
1
-
-
-
2
-
1
-
1
1
-
-
1
1
1
2
-
-
-
-
-
1
1
-
1
-
-
-
-
-
-
1
-
-
-
-
4
-
1
-
-
-
2
-
-
1
1
-
1
1
1
2
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-