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Enzyme Nomenclature
Information on EC 1.1.1.170 - 3beta-hydroxysteroid-4alpha-carboxylate 3-dehydrogenase (decarboxylating)
for references in articles please use BRENDA:EC1.1.1.170
Word Map on EC 1.1.1.170
- 1.1.1.170
- cholesterol
- child
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x-linked
-
dehydrogenase-like
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hemidysplasia
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ichthyosiform
- nevus
- ergosterol
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acronym
- erg27p
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male-lethal
- erythroderma
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x-inactivation
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verruciform
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.1.1.170
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RECOMMENDED NAME
GeneOntology No.
3beta-hydroxysteroid-4alpha-carboxylate 3-dehydrogenase (decarboxylating)
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a 3beta-hydroxysteroid-4alpha-carboxylate + NAD(P)+ = a 3-oxosteroid + CO2 + NAD(P)H
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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.
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CAS REGISTRY NUMBER
COMMENTARY
71822-23-6
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
I/LnJ and KK/HlJ inbred strains and cross breeds between KK/HlJ and I/LnJ
UniProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
additional information
malfunction
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mutations in NSDHL gene are associated with human CHILD syndrome, congenital hemidysplasia with ichthyosiform nevus and limb defects
malfunction
a I/LnJ-specific nonsynonymous polymorphism in X-linked Nsdhl, which codes for sterol-4-alpha-carboxylate 3-dehydrogenase in the cholesterol synthesis pathway, causes reduced HDL cholesterol levels in plasma
metabolism
the enzyme sterol-4-alpha-carboxylate 3-dehydrogenase is important in the cholesterol synthesis pathway
metabolism
Q5A1B0;
the sterol-4-alpha-carboxylate-3-dehydrogenase is an essential enzyme in the ergosterol/cholesterol biosynthesis pathway
metabolism
the sterol-4-alpha-carboxylate-3-dehydrogenase is an essential enzyme in the ergosterol/cholesterol biosynthesis pathway
metabolism
the sterol-4-alpha-carboxylate-3-dehydrogenase is an essential enzyme in the ergosterol/cholesterol biosynthesis pathway
metabolism
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the sterol-4-alpha-carboxylate-3-dehydrogenase is an essential enzyme in the ergosterol/cholesterol biosynthesis pathway
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physiological function
Q5A1B0;
the sterol-4-alpha-carboxylate-3-dehydrogenase is an essential enzyme in the ergosterol/cholesterol biosynthesis pathway
physiological function
the sterol-4-alpha-carboxylate-3-dehydrogenase is an essential enzyme in the ergosterol/cholesterol biosynthesis pathway
physiological function
the sterol-4-alpha-carboxylate-3-dehydrogenase is an essential enzyme in the ergosterol/cholesterol biosynthesis pathway
physiological function
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the sterol-4-alpha-carboxylate-3-dehydrogenase is an essential enzyme in the ergosterol/cholesterol biosynthesis pathway
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additional information
HDL and non-HDL lipid contents in different mouse genotypes and correlation to gene Nsdhl, overview
additional information
ERG26p structure homology modeling based on the crystal structure of Pseudomonas aeruginosa UDP-N-acetylglucosamine 4-epimerase complexed with UDP-N-acetylgalactosamine, PDB ID 1SB8
additional information
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ERG26p structure homology modeling based on the crystal structure of Pseudomonas aeruginosa UDP-N-acetylglucosamine 4-epimerase complexed with UDP-N-acetylgalactosamine, PDB ID 1SB8
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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
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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
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no epimerization of 4beta-isomer into 4alpha-isomer
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ir
3beta-hydroxy-cholest-8,24-dien-4alpha-carboxylate + NAD+
4alpha-methyl-cholest-8,24-dien-3-one + CO2 + NADH
4alpha-carboxy-4beta-methyl-5alpha-cholesta-8,24-dien-3beta-ol + NADP+
3-dehydro-4-methylzymosterol + NADPH + CO2
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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
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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
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-
-
-
?
4alpha-carboxy-5alpha-cholesta-8-en-3beta-ol + NADP+
5alpha-cholesta-8-en-3-one + CO2 + NADPH
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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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3beta-hydroxy-cholest-8,24-dien-4alpha-carboxylate + NAD+
4alpha-methyl-cholest-8,24-dien-3-one + CO2 + NADH
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-
?
3beta-hydroxy-cholest-8,24-dien-4alpha-carboxylate + NAD+
4alpha-methyl-cholest-8,24-dien-3-one + CO2 + NADH
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-
-
?
3beta-hydroxy-cholest-8,24-dien-4alpha-carboxylate + NAD+
4alpha-methyl-cholest-8,24-dien-3-one + CO2 + NADH
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-
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?
a 3beta-hydroxysteroid-4alpha-carboxylate + NAD(P)+
a 3-oxosteroid + CO2 + NAD(P)H
Q5A1B0;
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?
a 3beta-hydroxysteroid-4alpha-carboxylate + NAD(P)+
a 3-oxosteroid + CO2 + NAD(P)H
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?
a 3beta-hydroxysteroid-4alpha-carboxylate + NAD(P)+
a 3-oxosteroid + CO2 + NAD(P)H
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-
-
?
a 3beta-hydroxysteroid-4alpha-carboxylate + NAD(P)+
a 3-oxosteroid + CO2 + NAD(P)H
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?
a 3beta-hydroxysteroid-4alpha-carboxylate + NAD(P)+
a 3-oxosteroid + CO2 + NAD(P)H
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-
-
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
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
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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
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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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a 3beta-hydroxysteroid-4alpha-carboxylate + NAD(P)+
a 3-oxosteroid + CO2 + NAD(P)H
Q5A1B0
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?
a 3beta-hydroxysteroid-4alpha-carboxylate + NAD(P)+
a 3-oxosteroid + CO2 + NAD(P)H
Q15738
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?
a 3beta-hydroxysteroid-4alpha-carboxylate + NAD(P)+
a 3-oxosteroid + CO2 + NAD(P)H
Q9R1J0
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?
a 3beta-hydroxysteroid-4alpha-carboxylate + NAD(P)+
a 3-oxosteroid + CO2 + NAD(P)H
P53199
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?
a 3beta-hydroxysteroid-4alpha-carboxylate + NAD(P)+
a 3-oxosteroid + CO2 + NAD(P)H
P53199
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?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FR171456
Q5A1B0;
a natural specific inhibitor of yeast Erg26p from Monodictys sp.. FR171456 is a natural product with cholesterol-lowering properties in animal models. FR171456 significantly alters the levels of cholesterol pathway intermediates in yeast cells. FR171456 causes significant growth inhibition of strain SC5314 at. Erg26p inhibition requires the 4alpha-carboxyl group of FR171456, substitution of the 4alpha-carboxylic group of FR171456 by a carbobenzylamido group (Compound-1) decreases inhibition
FR171456
a natural specific inhibitor of mammalian NSDHL from Monodictys sp.. FR171456 is a natural product with cholesterol-lowering properties in animal models. FR171456 significantly alters the levels of cholesterol pathway intermediates in human cells. R171456 inhibits an artificial Hepatitis C viral replicon, and has broad antifungal activity, suggesting potential additional utility as an anti-infective. In a screen to profile compound activity against 503 cancer cell lines only five cell lines are sensitive to FR171456 with IC50 values below 0.005 mM. Calcidiol, a cholesterol metabolite situated downstream of NSDHL, is decreased in a FR171456 dose-dependent manner, consistent with a reduction of cholesterol synthesis, and new derivatives of NSDHL substrates are deteremined in the cells that are no longer effective as substrates
FR171456
a natural specific inhibitor of yeast Erg26p from Monodictys sp.. Genomic profiling identifies Erg26p as the FR171456 target, the ERG26 heterozygous strain (erg26DELTA/ERG26) shows the most significant hypersensitivity to FR171456. FR171456 is a natural product with cholesterol-lowering properties in animal models. FR171456 significantly alters the levels of cholesterol pathway intermediates in yeast cells. FR171456 causes significant growth inhibition of strain BY4743 at concentrations up to 0.2 mM. Multiple mutations, e.g. Gly90Ser, in enzyme ERG26 confer resistance to FR171456 in growth and enzyme assays. FR171456 inhibits an artificial Hepatitis C viral replicon, and has broad antifungal activity, suggesting potential additional utility as an anti-infective. Erg26p inhibition requires the 4a-carboxyl group of FR171456, substitution of the 4alpha-carboxylic group of FR171456 by a carbobenzylamido group (Compound-1) decreases inhibition by 300fold. FR171456 docking into a homology model of Erg26p. Modelling FR171456 resistance mutations on Erg26p, overview
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.55
3beta-hydroxy-cholest-8,24-dien-4alpha-carboxylate
pH 7.5, 30°C
additional information
additional information
Michaelis-Menten kinetics
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additional information
additional information
Michaelis-Menten kinetics
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
ERG26p structure homology modeling based on the crystal structure of Pseudomonas aeruginosa UDP-N-acetylglucosamine 4-epimerase complexed with UDP-N-acetylgalactosamine, PDB ID 1SB8
additional information
-
ERG26p structure homology modeling based on the crystal structure of Pseudomonas aeruginosa UDP-N-acetylglucosamine 4-epimerase complexed with UDP-N-acetylgalactosamine, PDB ID 1SB8
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospholipoprotein
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presence of phosphatidylcholine and phosphatidylethanolamine, no loss of activity after removal of phospholipids
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene Nsdhl, located on the X-chromosome, genotyping in 233 mice from a F2 cross between KK/HlJ and I/LnJ
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A94T
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naturally occurring missense mutant, mutant is not able to complement erg26 deficiency in Saccharomyces cerevisiae strain SDG200
V53D
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naturally occurring missense mutant, mutant is not able to complement erg26 deficiency in Saccharomyces cerevisiae strain SDG200
Gly90Ser
additional information
Gly90Ser
naturally occuring mutation of ERG26 that confers resistance to inhibitor FR171456
Gly90Ser
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naturally occuring mutation of ERG26 that confers resistance to inhibitor FR171456
-
additional information
multiple mutations in ERG26 confer resistance to inhibitor FR171456 in growth and enzyme assays. Some of these ERG26 mutations likely alter Erg26 binding to FR171456, based on a structure model of Erg26
additional information
-
multiple mutations in ERG26 confer resistance to inhibitor FR171456 in growth and enzyme assays. Some of these ERG26 mutations likely alter Erg26 binding to FR171456, based on a structure model of Erg26
-
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