Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.3.1.21 - 7-dehydrocholesterol reductase and Organism(s) Rattus norvegicus and UniProt Accession Q9Z2Z8

for references in articles please use BRENDA:EC1.3.1.21
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
The enzyme is part of the cholesterol biosynthesis pathway.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Rattus norvegicus
UNIPROT: Q9Z2Z8
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Rattus norvegicus
The enzyme appears in selected viruses and cellular organisms
Synonyms
dhcr7, 7-dehydrocholesterol reductase, neverland, daf-36, sterol delta7-reductase, 7-dhc reductase, 3beta-hydroxysterol delta7-reductase, 7-dehydrocholesterol delta7-reductase, 7-dhcr, 3beta-hydroxysterol-delta7-reductase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3-hydroxysterol DELTA7-reductase
-
-
3beta-hydroxysterol DELTA7-reductase
-
-
7-DHC reductase
-
-
-
-
Dhcr7
Dwarf5 protein
-
-
-
-
reductase, 7-dehydrocholesterol
-
-
-
-
Sterol delta-7-reductase
-
-
-
-
sterol DELTA7-reductase
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
cholesterol + NADP+ = cholesta-5,7-dien-3beta-ol + NADPH + H+
show the reaction diagram
mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
cholesterol:NADP+ DELTA7-oxidoreductase
The enzyme is part of the cholesterol biosynthesis pathway.
CAS REGISTRY NUMBER
COMMENTARY hide
9080-21-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
20,22-hydroxylumisterol-3 + NADPH + H+
? + NADP+
show the reaction diagram
-
-
-
?
20S-hydroxy-7-dehydrocholesterol + NADPH + H+
20S-hdroxycholesterol + NADP+
show the reaction diagram
-
-
-
?
22-hydroxylumisterol-3 + NADPH + H+
? + NADP+
show the reaction diagram
-
-
-
?
27-hydroxydehydrocholesterol + NADPH + H+
27-hydroxycholesterol + NADP+
show the reaction diagram
-
-
-
?
7-dehydrodesmosterol + NADPH + H+
desmosterol + NADP+
show the reaction diagram
-
-
-
?
7-hydroxycholesterol + NADPH + H+
cholesterol + NADP+
show the reaction diagram
-
-
-
?
cholesta-5,7-dien-3beta-ol + NADPH
cholesterol + NADP+
show the reaction diagram
enzyme catalyzes the terminal step in cholesterol biosynthesis by reducing 7-dehydrocholesterol
-
-
?
ergosterol + NADPH + H+
brassicasterol + NADP+
show the reaction diagram
-
-
-
?
lumisterol-3 + NADPH + H+
? + NADP+
show the reaction diagram
-
-
-
?
7-dehydrodesmosterol + NADPH
desmosterol + NADP+
show the reaction diagram
-
-
-
-
?
7-dehydrositosterol + NADPH
sitosterol + NADP+
show the reaction diagram
-
25% of that with 7-dehydrocholesterol
-
?
cholesta-5,7-dien-3-beta-ol + NADPH
cholesterol + NADP+
show the reaction diagram
cholesta-5,7-dien-3alpha-ol + NADPH
epicholesterol + NADP+
show the reaction diagram
-
i.e. 7-dehydroepicholesterol, 25% activity of that with 7-dehydrocholesterol
-
-
?
cholesta-5,7-dien-3beta-ol + NADPH
cholesterol + NADP+
show the reaction diagram
cholesta-7-en-3beta-ol + NADPH
?
show the reaction diagram
ergosta-5,7,22-trien-3beta-ol + NADPH
ergosta-5,22-diene-3beta-ol + NADP+
show the reaction diagram
ergosterol + NADP+
?
show the reaction diagram
-
-
-
-
r
additional information
?
-
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
cholesta-5,7-dien-3beta-ol + NADPH
cholesterol + NADP+
show the reaction diagram
enzyme catalyzes the terminal step in cholesterol biosynthesis by reducing 7-dehydrocholesterol
-
-
?
7-dehydrodesmosterol + NADPH
desmosterol + NADP+
show the reaction diagram
-
-
-
-
?
cholesta-5,7-dien-3-beta-ol + NADPH
cholesterol + NADP+
show the reaction diagram
cholesta-5,7-dien-3beta-ol + NADPH
cholesterol + NADP+
show the reaction diagram
-
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
20S-hydroxy-7-dehydrocholesterol
inhibits the conversion of ergosterol to brassicasterol similarly to 7-dehydrocholesterol
-
20S-hydroxylumisterol
-
-
22-hydroxy-lumisterol
-
-
27-hydroxydehydrocholesterol
inhibits the conversion of ergosterol by 25%
-
7-dehydrocholesterol
0.03 mM, inhibits the conversion of ergosterol to brassicasterol by 93%
8-dehydrocholesterol
-
1-[p-(beta-Diethylaminoethoxy) phenyl]1-(p-tolyl)-2-(p-chlorophenyl)ethanol
-
i.e. MER-29 or triparanol
20,25-Diazacholesterol
-
-
3beta-[2-(diethylamino)ethoxy]androst-5-en-17-one
-
i.e. U18666A
4-(2-[1-(n-chlorocinnamyl) piperazin-4-yl] ethyl) benzoic acid
7-dehydrocholesterol
-
depending on age of rats
AY9944
-
noncompetitive, specific inhibitor
BM15.766
-
noncompetitive, specific inhibitor
brassicasterol
-
higher concentration, competitive
epicholesterol
-
higher concentration, competitive
ergosterol
-
non-competetively, concentration 0.025 mM
sitosterol
-
higher concentration, competitive
trans-1,4-Bis-(2-chlorobenzylaminomethyl)cyclohexane dihydrochloride
Triparanol
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Lipid transfer protein
-
cytosolic, activity enhancement which is inhibited by addition of Tween 80, probably identical with sterol carrier protein
-
Sterol carrier protein
-
from cytosol, required for activity, probably identical with lipid transfer protein
Tween 80
-
can substitute carrier protein
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.28
NADPH
substrate ergosterol, pH 7.5, 37°C
1.14
7-dehydrocholesterol
-
-
0.21
ergosterol
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0014
20,25-Diazacholesterol
-
-
0.000109 - 0.00024
trans-1,4-Bis-(2-chlorobenzylaminomethyl)cyclohexane dihydrochloride
0.047 - 0.083
Triparanol
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00011
-
testis enzyme, extract
0.000756
-
-
0.00108
-
solubilized by 1.5% 3-[3-(cholamidopropyl)-dimethylammonio]-1-propanesulfonate, i.e. CHAPS, from microsomes
0.0023
-
liver enzyme, extract
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8
-
assay at
7.3
-
assay at, phosphate buffer 0.1 M
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
progenitor cells, immature cells, and adult cells, differentially expressed transcripts and enzyme expression levels during development and differentiation, overview
Manually annotated by BRENDA team
-
15-20% of total activiy in brain, lipid exchange between microsomes and myelin
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
105000 x g fraction supernatant
Manually annotated by BRENDA team
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DHCR7_RAT
471
6
54155
Swiss-Prot
Mitochondrion (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
54200
-
? * 54200, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
? * 54200, SDS-PAGE
additional information
-
protein structure
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
analysis of differentially expressed transcripts of gene dhcr7 in progenitor Leydig cells and in immature Leydig cells, increased expression of the enzyme during differentiation process
-
DNA and amino acid sequence determination, gene structure and organization, gene dhcr7 maps to chromosome 8q2.1
-
expression in Saccharomyces cerevisiae with c-myc epitope
-
gene Dhcr7, chromosome mapping to 8q2.1, DNA and amino acid sequence determination and analysis of the full-length gene and the splicing variants Dhcr7-AS-1-5, gene structure, physical map, 5 alternative splicing variants
gene Dhcr7, DNA and amino acid sequence determination and analysis, 1723 nucleotides, about 636 base pairs, gene structure, physical map, transcript half-life, alternative splicing variant 4
gene Dhcr7, DNA and amino acid sequence determination and analysis, gene structure, 1474 nucleotides, about 387 base pairs, physical map, transcript half-life, alternative splicing variant 1
gene Dhcr7, DNA and amino acid sequence determination and analysis, gene structure, 1595 nucleotides, about 508 base pairs, physical map, transcript half-life, alternative splicing variant 2
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
-
enzyme is a key marker of early Leydig cell steroidogenesis, using the technique of differential display RT-PCR
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Srikantaiah, M.V.; Assef, S.; Morin, R.J.
Effects of Tween 80 on liver microsomal 7-dehydrocholesterol reductase
Biochem. Biophys. Res. Commun.
81
1087-1090
1978
Rattus norvegicus
Manually annotated by BRENDA team
Bjrkhem, I.; Holmberg, I.
Mechanism of enzymatic reduction of steroid double bonds
Eur. J. Biochem.
33
364-367
1973
Rattus norvegicus
Manually annotated by BRENDA team
Banik, N.L.; Davison, A.N.
Exchange of sterols between myelin and other membranes of developing rat brain
Biochem. J.
122
751-758
1971
Rattus norvegicus
Manually annotated by BRENDA team
Dempsey, M.E.; Seaton, J.D.; Schroepfer, G.J.; Trockman, R.W.
The intermediary role of DELTA5,7-cholestadien-3beta-ol in cholesterol biosynthesis
J. Biol. Chem.
239
1381-1387
1964
Rattus norvegicus
Manually annotated by BRENDA team
Niemiro, R.; Fumagalli, R.
Studies on the inhibitory mechanism of some hypocholesterolemic agents on 7-dehydrocholesterol DELTA-7-bond reductase activity
Biochim. Biophys. Acta
98
624-631
1965
Rattus norvegicus
Manually annotated by BRENDA team
Dempsey, M.E.
Pathways of enzymic synthesis and conversion to cholesterol of DELTA-5,7,24-cholestatrien-3beta-ol and other naturally occurring sterols
J. Biol. Chem.
240
4176-4188
1965
Rattus norvegicus
Manually annotated by BRENDA team
Trzaskos, J.M.; Gaylor, J.L.
Cytosolic modulators of activities of microsomal enzymes of cholesterol biosynthesis. Purification and characterization of a non-specific lipid-transfer protein
Biochim. Biophys. Acta
751
52-65
1983
Rattus norvegicus
Manually annotated by BRENDA team
Wilton, D.C.; Munday, K.A.; Skinner, S.J.M.; Akhtar, M.
The biological conversion of 7-dehydrocholesterol into cholesterol and comments on the reduction of double bonds
Biochem. J.
106
803
1968
Rattus norvegicus
Manually annotated by BRENDA team
Lee, J.N.; Paik, Y.K.
Cholesterol biosynthesis from lanosterol: development of a novel assay method, characterization, and solubilization of rat hepatic microsomal sterol DELTA7-reductase
J. Biochem. Mol. Biol.
30
370-377
1997
Rattus norvegicus
-
Manually annotated by BRENDA team
Waterham, H.R.; Wanders, R.J.A.
Biochemical and genetic aspects of 7-dehydrocholesterol reductase and Smith-Lemli-Opitz syndrome
Biochim. Biophys. Acta
1529
340-356
2000
Arabidopsis thaliana, Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Shefer, S.; Salen, G.; Honda, A.; Batta, A.K.; Nguyen, L.B.; Tint, G.S.; Ioannou, Y.A.; Desnick, R.
Regulation of rat hepatic 3beta-hydroxysterol DELTA7-reductase: substrate specificity, competitive and non-competitive inhibition, and phosphorylation/dephosphorylation
J. Lipid Res.
39
2471-2476
1998
Rattus norvegicus
Manually annotated by BRENDA team
Honda, A.; Salen, G.; Shefer, S.; Batta, A.K.; Honda, M.; Xu, G.; Tint, G.S.; Matsuzaki, Y.; Shoda, J.; Tanaka, N.
Bile acid synthesis in the Smith-Lemli-Opitz syndrome: effects of dehydrocholesterols on cholesterol 7.alpha-hydroxylase and 27-hydroxylase activities in rat liver
J. Lipid Res.
40
1520-1528
1999
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Lee, J.N.; Bae, S.H.; Paik, Y.K.
Structure and alternative splicing of the rat 7-dehydrocholesterol reductase gene
Biochim. Biophys. Acta
1576
148-156
2002
Mus musculus (O88455), Mus musculus, Rattus norvegicus (Q9E2H5), Rattus norvegicus (Q9Z2Z8), Homo sapiens (Q9UBM7), Homo sapiens
Manually annotated by BRENDA team
Anbalagan, M.; Yashwanth, R.; Jagannadha Rao, A.
DD-RT-PCR identifies 7-dehydrocholesterol reductase as a key marker of early Leydig cell steroidogenesis
Mol. Cell. Endocrinol.
219
37-45
2004
Rattus norvegicus
Manually annotated by BRENDA team
Correa-Cerro, L.S.; Porter, F.D.
3beta-hydroxysterol DELTA7-reductase and the Smith-Lemli-Opitz syndrome
Mol. Genet. Metab.
84
112-126
2005
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Tuckey, R.; Tang, E.; Chen, Y.; Slominski, A.
Selective ability of rat 7-dehydrocholesterol reductase (DHCR7) to act on some 7-dehydrocholesterol metabolites but not on lumisterol metabolites
J. Steroid Biochem. Mol. Biol.
212
105929
2021
Rattus norvegicus (Q9Z2Z8)
Manually annotated by BRENDA team