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Information on EC 1.1.1.170 - 3beta-hydroxysteroid-4alpha-carboxylate 3-dehydrogenase (decarboxylating) and Organism(s) Mus musculus and UniProt Accession Q9R1J0

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EC Tree
IUBMB Comments
The enzyme participates in the biosynthesis of several important sterols such as ergosterol and cholesterol. It is part of a three enzyme system that removes methyl groups from the C-4 position of steroid molecules. The first enzyme, EC 1.14.18.9, 4alpha-methylsterol monooxygenase, catalyses three successive oxidations of the methyl group, resulting in a carboxyl group; the second enzyme, EC 1.1.1.170, catalyses an oxidative decarboxylation that results in a reduction of the 3beta-hydroxy group at the C-3 carbon to an oxo group; and the last enzyme, EC 1.1.1.270, 3beta-hydroxysteroid 3-dehydrogenase, reduces the 3-oxo group back to a 3beta-hydroxyl. If a second methyl group remains at the C-4 position, this enzyme also catalyses its epimerization from 4beta to 4alpha orientation, so it could serve as a substrate for a second round of demethylation. cf. EC 1.1.1.418, plant 3beta-hydroxysteroid-4alpha-carboxylate 3-dehydrogenase (decarboxylating).
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Mus musculus
UNIPROT: Q9R1J0
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The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
nsdhl, erg26, erg26p, sterol-4-alpha-carboxylate 3-dehydrogenase, sterol-4-alpha-carboxylate-3-dehydrogenase, sterol-4alpha-carboxylate 3-dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
sterol-4-alpha-carboxylate 3-dehydrogenase
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3beta-hydroxy-4alpha-methylcholestenecarboxylate 3-dehydrogenase (decarboxylating)
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3beta-hydroxy-4beta-methylcholestenoate dehydrogenase
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sterol 4alpha-carboxylic decarboxylase
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sterol-4alpha-carboxylate 3-dehydrogenase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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oxidation
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reduction
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PATHWAY SOURCE
PATHWAYS
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-, -, -, -
SYSTEMATIC NAME
IUBMB Comments
3beta-hydroxysteroid-4alpha-carboxylate:NAD(P)+ 3-oxidoreductase (decarboxylating)
The enzyme participates in the biosynthesis of several important sterols such as ergosterol and cholesterol. It is part of a three enzyme system that removes methyl groups from the C-4 position of steroid molecules. The first enzyme, EC 1.14.18.9, 4alpha-methylsterol monooxygenase, catalyses three successive oxidations of the methyl group, resulting in a carboxyl group; the second enzyme, EC 1.1.1.170, catalyses an oxidative decarboxylation that results in a reduction of the 3beta-hydroxy group at the C-3 carbon to an oxo group; and the last enzyme, EC 1.1.1.270, 3beta-hydroxysteroid 3-dehydrogenase, reduces the 3-oxo group back to a 3beta-hydroxyl. If a second methyl group remains at the C-4 position, this enzyme also catalyses its epimerization from 4beta to 4alpha orientation, so it could serve as a substrate for a second round of demethylation. cf. EC 1.1.1.418, plant 3beta-hydroxysteroid-4alpha-carboxylate 3-dehydrogenase (decarboxylating).
CAS REGISTRY NUMBER
COMMENTARY hide
71822-23-6
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
a 3beta-hydroxysteroid-4alpha-carboxylate + NAD(P)+
a 3-oxosteroid + CO2 + NAD(P)H
show the reaction diagram
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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 SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
a 3beta-hydroxysteroid-4alpha-carboxylate + NAD(P)+
a 3-oxosteroid + CO2 + NAD(P)H
show the reaction diagram
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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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-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
I/LnJ and KK/HlJ inbred strains and cross breeds between KK/HlJ and I/LnJ
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
additional information
HDL and non-HDL lipid contents in different mouse genotypes and correlation to gene Nsdhl, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
NSDHL_MOUSE
362
1
40686
Swiss-Prot
other Location (Reliability: 1)
PROTEIN VARIANTS
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
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
complementation of erg26 deficient Saccharomyces cerevisiae strain SDG200
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lucas, M.E.; Ma, Q.; Cunningham, D.; Peters, J.; Cattanach, B.; Bard, M.; Elmore, B.K.; Herman, G.E.
Identification of two novel mutations in the murine Nsdhl sterol dehydrogenase gene and development of a functional complementation assay in yeast
Mol. Genet. Metab.
80
227-233
2003
Mus musculus
Manually annotated by BRENDA team
Bautz, D.J.; Broman, K.W.; Threadgill, D.W.
Identification of a novel polymorphism in X-linked sterol-4-alpha-carboxylate 3-dehydrogenase (Nsdhl) associated with reduced high-density lipoprotein cholesterol levels in I/LnJ mice
G3 (Bethesda)
3
1819-1825
2013
Mus musculus (Q9R1J0)
Manually annotated by BRENDA team