Information on EC 1.1.1.170 - 3beta-hydroxysteroid-4alpha-carboxylate 3-dehydrogenase (decarboxylating)

Word Map on EC 1.1.1.170
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.1.1.170
-
RECOMMENDED NAME
GeneOntology No.
3beta-hydroxysteroid-4alpha-carboxylate 3-dehydrogenase (decarboxylating)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a 3beta-hydroxysteroid-4alpha-carboxylate + NAD(P)+ = a 3-oxosteroid + CO2 + NAD(P)H
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
cholesterol biosynthesis
-
-
Steroid biosynthesis
-
-
Metabolic pathways
-
-
Biosynthesis of antibiotics
-
-
zymosterol biosynthesis
-
-
cholesterol biosynthesis III (via desmosterol)
-
-
cholesterol biosynthesis II (via 24,25-dihydrolanosterol)
-
-
cholesterol biosynthesis I
-
-
SYSTEMATIC NAME
IUBMB Comments
3beta-hydroxysteroid-4alpha-carboxylate:NAD(P)+ 3-oxidoreductase (decarboxylating)
The enzyme catalyses the decarboxylation of the C-4 carbon and the dehydrogenation of a 3beta hydroxyl at the C-3 carbon of 3beta-hydroxysteroid-4alpha-carboxylates. It is involved in zymosterol and cholesterol biosynthesis.
CAS REGISTRY NUMBER
COMMENTARY hide
71822-23-6
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3beta-hydroxy-4alpha-methyl-5alpha-cholest-7-ene-4beta-carboxylate + NAD+
4alpha-methyl-5alpha-cholest-7-en-3-one + CO2 + NADH
show the reaction diagram
-
-
-
?
3beta-hydroxy-4beta-methyl-5alpha-cholest-7-en-4alpha-oic acid + NAD+
4alpha-methyl-5alpha-cholest-7-en-3-one + CO2 + NADH
show the reaction diagram
-
no epimerization of 4beta-isomer into 4alpha-isomer
-
ir
3beta-hydroxy-cholest-8,24-dien-4alpha-carboxylate + NAD+
4alpha-methyl-cholest-8,24-dien-3-one + CO2 + NADH
show the reaction diagram
4alpha-carboxy-4beta-methyl-5alpha-cholesta-8,24-dien-3beta-ol + NADP+
3-dehydro-4-methylzymosterol + NADPH + CO2
show the reaction diagram
-
-
-
-
?
4alpha-carboxy-4beta-methyl-5alpha-cholesta-8-en-3beta-ol + NADP+
4alpha-methyl-5alpha-cholesta-8-en-3-one + NADPH + CO2
show the reaction diagram
-
enzyme is involved in the sequential removal of two C-4 methyl groups in post-squalene cholesterol biosynthesis
-
-
?
4alpha-carboxy-5alpha-cholesta-8,24-dien-3beta-ol + NADP+
5alpha-cholesta-8,24-dien-3-one + NADPH + CO2
show the reaction diagram
-
-
-
-
?
4alpha-carboxy-5alpha-cholesta-8-en-3beta-ol + NADP+
5alpha-cholesta-8-en-3-one + CO2 + NADPH
show the reaction diagram
-
enzyme is involved in the sequential removal of two C-4 methyl groups in post-squalene cholesterol biosynthesis
-
-
?
a 3beta-hydroxysteroid-4alpha-carboxylate + NAD(P)+
a 3-oxosteroid + CO2 + NAD(P)H
show the reaction diagram
additional information
?
-
-
involved in the removal of C-4 methyl groups in postsqualene cholesterol synthesis
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3beta-hydroxy-4alpha-methyl-5alpha-cholest-7-ene-4beta-carboxylate + NAD+
4alpha-methyl-5alpha-cholest-7-en-3-one + CO2 + NADH
show the reaction diagram
-
-
-
?
3beta-hydroxy-4beta-methyl-5alpha-cholest-7-en-4alpha-oic acid + NAD+
4alpha-methyl-5alpha-cholest-7-en-3-one + CO2 + NADH
show the reaction diagram
-
no epimerization of 4beta-isomer into 4alpha-isomer
-
ir
a 3beta-hydroxysteroid-4alpha-carboxylate + NAD(P)+
a 3-oxosteroid + CO2 + NAD(P)H
show the reaction diagram
additional information
?
-
-
involved in the removal of C-4 methyl groups in postsqualene cholesterol synthesis
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5alpha-cholest-7-en-3-one
-
2-9.3% inhibition between 16 and 130 nmol
5alpha-Cholest-7-en-3beta-ol
-
15.5-65% inhibition between 30 and 260 nmol
Fe2+
-
less than 25% inhibition at 1 mM
FR171456
-
Zn2+
-
marked inhibition between 0.1 and 1 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.007
3beta-hydroxy-4beta-methyl-5alpha-cholest-7-en-4alpha-oic acid
-
-
0.55
3beta-hydroxy-cholest-8,24-dien-4alpha-carboxylate
pH 7.5, 30C
-
additional information
additional information
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00135
FR171456
in vitro inhibition, pH 7.5, 30C
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0000063 - 0.08
FR171456
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.11
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8 - 9
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
acidic pH results in a very low decarboxylation rate
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
surface of
-
Manually annotated by BRENDA team
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospholipoprotein
-
presence of phosphatidylcholine and phosphatidylethanolamine, no loss of activity after removal of phospholipids
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, 10 mM phosphate buffer, pH 7.4, no loss of activity within 2 weeks
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
near homogeneity, chromatography techniques, sodium deoxycholate solubilization
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
complementation of erg26 deficient Saccharomyces cerevisiae strain SDG200
-
gene Nsdhl, located on the X-chromosome, genotyping in 233 mice from a F2 cross between KK/HlJ and I/LnJ
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A94T
-
naturally occurring missense mutant, mutant is not able to complement erg26 deficiency in Saccharomyces cerevisiae strain SDG200
G280A
-
loss of a HhaI restriction site
V53D
-
naturally occurring missense mutant, mutant is not able to complement erg26 deficiency in Saccharomyces cerevisiae strain SDG200
Gly90Ser
additional information