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

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.1.1.170
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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
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of antibiotics
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cholesterol biosynthesis I
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cholesterol biosynthesis II (via 24,25-dihydrolanosterol)
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cholesterol biosynthesis III (via desmosterol)
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Metabolic pathways
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Steroid biosynthesis
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zymosterol biosynthesis
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cholesterol biosynthesis
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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
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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mutations in NSDHL gene are associated with human CHILD syndrome, congenital hemidysplasia with ichthyosiform nevus and limb defects
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
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-
-
?
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
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no epimerization of 4beta-isomer into 4alpha-isomer
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ir
4alpha-carboxy-4beta-methyl-5alpha-cholesta-8,24-dien-3beta-ol + NADP+
3-dehydro-4-methylzymosterol + NADPH + CO2
show the reaction diagram
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-
-
-
?
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
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enzyme is involved in the sequential removal of two C-4 methyl groups in post-squalene cholesterol biosynthesis
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?
4alpha-carboxy-5alpha-cholesta-8,24-dien-3beta-ol + NADP+
5alpha-cholesta-8,24-dien-3-one + NADPH + CO2
show the reaction diagram
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-
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?
4alpha-carboxy-5alpha-cholesta-8-en-3beta-ol + NADP+
5alpha-cholesta-8-en-3-one + CO2 + NADPH
show the reaction diagram
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enzyme is involved in the sequential removal of two C-4 methyl groups in post-squalene cholesterol biosynthesis
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?
additional information
?
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involved in the removal of C-4 methyl groups in postsqualene cholesterol synthesis
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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
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no epimerization of 4beta-isomer into 4alpha-isomer
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ir
additional information
?
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involved in the removal of C-4 methyl groups in postsqualene cholesterol synthesis
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
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can not be replaced by NADP+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5alpha-cholest-7-en-3-one
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2-9.3% inhibition between 16 and 130 nmol
5alpha-Cholest-7-en-3beta-ol
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15.5-65% inhibition between 30 and 260 nmol
Fe2+
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less than 25% inhibition at 1 mM
Zn2+
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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
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.11
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8 - 9
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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acidic pH results in a very low decarboxylation rate
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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surface of
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Manually annotated by BRENDA team
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospholipoprotein
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presence of phosphatidylcholine and phosphatidylethanolamine, no loss of activity after removal of phospholipids
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 10 mM phosphate buffer, pH 7.4, no loss of activity within 2 weeks
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
near homogeneity, chromatography techniques, sodium deoxycholate solubilization
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
complementation of erg26 deficient Saccharomyces cerevisiae strain SDG200
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A94T
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naturally occurring missense mutant, mutant is not able to complement erg26 deficiency in Saccharomyces cerevisiae strain SDG200
G280A
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loss of a HhaI restriction site
V53D
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naturally occurring missense mutant, mutant is not able to complement erg26 deficiency in Saccharomyces cerevisiae strain SDG200