1.14.14.154: sterol 14alpha-demethylase
This is an abbreviated version!
For detailed information about sterol 14alpha-demethylase, go to the full flat file.
Word Map on EC 1.14.14.154
-
1.14.14.154
-
azole
-
candida
-
fluconazole
-
aspergillus
-
fumigatus
-
albicans
-
ergosterol
-
voriconazole
-
itraconazole
-
azole-resistant
-
fungicide
-
triazole
-
posaconazole
-
cholesterol
-
aspergillosis
-
ketoconazole
-
microdilution
-
candidiasis
-
fluconazole-resistant
-
amphotericin
-
glabrata
-
cross-resistance
-
tebuconazole
-
echinocandins
-
eucast
-
parapsilosis
-
tropicalis
-
isavuconazole
-
agriculture
-
araf
-
vulvovaginal
-
clotrimazole
-
drug development
-
stricto
-
mycology
-
digitatum
-
etest
-
propiconazole
-
prochloraz
-
graminicola
-
micafungin
-
non-albicans
-
krusei
-
cholesterogenic
-
caspofungin
-
benznidazole
-
pharmacology
-
anidulafungin
-
mycosphaerella
-
terbinafine
-
auris
-
candidemia
-
tubingensis
-
medicine
- 1.14.14.154
- azole
- candida
- fluconazole
- aspergillus
- fumigatus
- albicans
- ergosterol
- voriconazole
- itraconazole
-
azole-resistant
-
fungicide
- triazole
- posaconazole
- cholesterol
- aspergillosis
- ketoconazole
-
microdilution
- candidiasis
-
fluconazole-resistant
- amphotericin
- glabrata
-
cross-resistance
- tebuconazole
-
echinocandins
-
eucast
- parapsilosis
- tropicalis
-
isavuconazole
- agriculture
-
araf
-
vulvovaginal
- clotrimazole
- drug development
-
stricto
-
mycology
- digitatum
-
etest
- propiconazole
- prochloraz
- graminicola
- micafungin
-
non-albicans
- krusei
-
cholesterogenic
- caspofungin
- benznidazole
- pharmacology
- anidulafungin
-
mycosphaerella
- terbinafine
- auris
- candidemia
- tubingensis
- medicine
Reaction
Synonyms
14-alpha sterol demethylase, 14-demethylase, 14alpha-demethylase, 14alpha-lanosterol demethylase, 14alpha-methylsterol 14alpha-demethylase, 14alpha-sterol demethylase, 14DM, AF_14DM, C- I4 demethylase, CACYP51, CA_14DM, CYP51, Cyp51A, CYP51A1, CYP51Ap, CYP51B, CYP51b1, CYP51Bp, CYP51F1, CYP51G1, CYPL1, cytochrome CYP51, cytochrome P 450 CYP51, cytochrome P-450 lanosterol 14alpha-demethylase, cytochrome P-450-dependent 14alpha-sterol demethylase, cytochrome P-450-dependent obtusifoliol 14alpha-demethylase, cytochrome P-450/14DM, cytochrome P-45014DM, cytochrome P450 14alpha-demethylase, cytochrome P450 14DM, cytochrome P450 51, cytochrome P450 CYP51, cytochrome P450 lanosterol 14alpha-demethylase, cytochrome P450 sterol 14alpha-demethylase, cytochrome-P450 14alpha-demethylase, demethylase, methylsterol 14alpha-, eburicol 14 alpha-demethylase, eburicol 14alpha-demethylase, EC 1.14.13.70, ERG11, Erg11p, lanosterol 14 alpha-demethylase, lanosterol 14-alpha demethylase, lanosterol 14-demethylase, lanosterol 14alpha-demethylase, lanosterol 14alpha-methyldemethylase, lanosterol C-14 demethylase, lanosterol demethylase, lanosterol-14alpha-demethylase, LDM, methylsterol 14alpha-demethylase (P 450 CYP51), More, Obtusifoliol 14-alpha demethylase, obtusifoliol 14-demethylase, obtusifoliol 14alpha-demethylase, obtusifoliol-metabolizing 14alpha-demethylase, obtusufoliol 14-demethylase, P 450 lanosterol C-14 demethylase, P-450 lanosterol demethylase, P-45014DM, P-45014DM-containing monooxygenase system, P-450OBT 14DM, P450 14alpha-lanosterol demethylases A, P450 14alpha-lanosterol demethylases B, P450(14DM), P450-14DM, P450-L1A1, P45014DM, PCERG11, rLDM, sterol 14-alpha demethylase, sterol 14-demethylase, sterol 14-demethylase P450, sterol 14alpha-demethylase, sterol 14alpha-demethylase (CYP51), sterol 14alpha-demethylase cytochrome P 450, sterol 14alpha-demethylase P450, sterol C14 demethylase, sterol C14-demethylase, sterol demethylase P450, sterol-14alpha-demethylase, TC14DM
ECTree
1.14.14.154 sterol 14alpha-demethylaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 1.14.14.154 - sterol 14alpha-demethylase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
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
(3b,4a,5a)-4,14-dimethylcholest-8-en-3-ol + [reduced NADPH-hemoprotein reductase] + O2
? + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
good substrate, 67% of activity compared to obtusifoliol
-
-
?
(3beta,4alpha,5alpha)-4,14-dimethylcholest-8-en-3-ol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
r
14alpha-methyl-24,28-dihydrofecosterol + [reduced NADPH-hemoprotein reductase] + O2
? + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
50% of activity compared to obtusifoliol
-
-
?
2-phenylimidazole + [reduced NADPH-hemoprotein reductase] + O2
?
-
2-phenylimidazole binding causes thermally induced alterations in CYP51 active site structure and/or binding modes for the small ligand
-
-
?
24(28)-methylene-24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
(3beta,5alpha)-4,4-dimethylcholesta-8,14-dien-3-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
24,25-dihydro-4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
24,28-dihydroobtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
24-methylene-24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
14alpha-demethyl-24-methylene-4alpha-methyl-5alpha-ergosta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
24-methylene-24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
24-methylenedihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
preferred substrate
-
-
?
7-lanosten-3beta-ol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethylcholesta-7,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
very low activity
-
-
?
7-lanostene-3beta,32-diol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethylcholesta-7,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
very low activity
-
-
?
8-lanostene-3beta,32-diol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethylcholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
eburicol + O2 + [reduced NADPH-hemoprotein reductase] + O2
2-(3-hydroxy-4,4,10,13-tetramethyl-2,3,4,5,6,7,10,11,12,13,16,17-dodecahydro-1H-cyclopenta[a]phenanthren-17-yl)-6-methyl-5-methylene-heptanoic acid + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
eburicol + [reduced NADPH-hemoprotein reductase] + O2
? + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
estriol + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
lanosterol + NADPH + O2
4,4-dimethylcholesta-8,14,24-trien-3-ol + NADP+ + H2O
artificial fused enzymes have comparable activity to the reconstituted system. Reduction of CYP51 both in the fused enzyme and the reconstituted system is biphasic and consisted of an initial fast phase followed by a slow phase
-
-
?
lanosterol + O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14,24-triene-3beta-ol + formate + NADP+ + H2O
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethylcholesta-8,14,24-trien-3-ol + [oxidized NADPH-hemoprotein reductase] + H2O
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethylcholesta-8,14,24-trienol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethylzymosterol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
14alpha-methylzymosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
14alpha-methylzymosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
(3beta,5alpha)-4,4-dimethylcholesta-8,14-dien-3-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
(3beta,5alpha)-4,4-dimethylcholesta-8,14-dien-3-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
(3beta,5alpha)-4,4-dimethylcholesta-8,14-dien-3-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
8-lanosta-3beta-ol
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
DHL
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
8-lanosten-3beta-ol
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
4,4,14alpha-trimethyl-5alpha-cholesta-8-en-3beta-ol
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
8-lanosta-3beta-ol
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
DHL
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
8-lanosten-3beta-ol
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
4,4,14alpha-trimethyl-5alpha-cholesta-8-en-3beta-ol
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
8-lanosta-3beta-ol
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
DHL
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
8-lanosten-3beta-ol
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
4,4,14alpha-trimethyl-5alpha-cholesta-8-en-3beta-ol
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
8-lanosta-3beta-ol
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
DHL
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
8-lanosten-3beta-ol
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
4,4,14alpha-trimethyl-5alpha-cholesta-8-en-3beta-ol
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
8-lanosta-3beta-ol
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
DHL
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
8-lanosten-3beta-ol
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
4,4,14alpha-trimethyl-5alpha-cholesta-8-en-3beta-ol
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
not the natural substrate
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
8-lanosta-3beta-ol
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
DHL
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
8-lanosten-3beta-ol
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
4,4,14alpha-trimethyl-5alpha-cholesta-8-en-3beta-ol
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
the enzyme is involved in ergosterol and cholesterol biosynthesis
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
the enzyme is involved in ergosterol and cholesterol biosynthesis
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
i.e. anosta-8-en-3ebta-ol
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
the enzyme is involved in ergosterol and cholesterol biosynthesis
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
the enzyme is involved in ergosterol and cholesterol biosynthesis
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
the enzyme is involved in ergosterol and cholesterol biosynthesis
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
24,28-dihydroobtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
good substrate, 75% of activity to obtusifoliol
-
-
?
24,28-dihydroobtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
DHO
-
-
?
24,28-dihydroobtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
4alpha,14alpha-dimethyl-5alpha-ergosta-8-en-3beta-ol
-
-
?
24,28-dihydroobtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
very poor substrate, about 10% of obtusifoliol demethylation, activity disappears in the presence of same concentration of lanosterol, 24-methylene-24,25-dihydrolanosterol, obtusifoliol or 24,25-dihydrolanosterol
-
-
?
24,28-dihydroobtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
DHO
-
-
?
24,28-dihydroobtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
4alpha,14alpha-dimethyl-5alpha-ergosta-8-en-3beta-ol
-
-
?
24,28-dihydroobtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
good substrate, 75% of activity to obtusifoliol
-
-
?
24,28-dihydroobtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
DHO
-
-
?
24,28-dihydroobtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
4alpha,14alpha-dimethyl-5alpha-ergosta-8-en-3beta-ol
-
-
?
24-methylene-24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
poorest substrate, catalyzes 14alpha-demethylation of 24-methylene-DHL, but activity is considerably lower than that for lanosterol and for 24,25-dihydrolanosterol, DHL
-
-
?
24-methylene-24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
4,4,14alpha-trimethylergosta-8,24(28)-dien-3beta-ol
-
-
?
24-methylene-24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
24-methylenelanost-8-en-3beta-ol, 24-methylene-DHL
-
-
?
24-methylene-24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
good substrate
-
-
?
24-methylene-24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
4,4,14alpha-trimethylergosta-8,24(28)-dien-3beta-ol
-
-
?
24-methylene-24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
activity for 24-methylene-DHL is considerably higher, 4fold, than that for 24,25-dihydrolanosterol, DHL
-
-
?
24-methylene-24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
24-methylenelanost-8-en-3beta-ol, 24-methylene-DHL
-
-
?
24-methylene-24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
about 60% activity to that of lanosterol
-
-
?
24-methylenedihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
24-methylenedihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
24-methylenedihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
24-methylenedihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis
-
-
?
24-methylenedihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
24-methylenedihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
24-methylenedihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
24-methylenedihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis
-
-
?
24-methylenedihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
24-methylenedihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis
-
-
?
eburicol + [reduced NADPH-hemoprotein reductase] + O2
?
-
isozymes CYP51A and CYP51B
-
-
?
eburicol + [reduced NADPH-hemoprotein reductase] + O2
?
-
isozymes CYP51A and CYP51B
-
-
?
eburicol + [reduced NADPH-hemoprotein reductase] + O2
?
i.e. 24-methylenelanosta-8-en-3beta-ol
-
-
?
eburicol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
eburicol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
eburicol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
eburicol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
estriol + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
estriol + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
lanosterol + O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14,24-triene-3beta-ol + formate + NADP+ + H2O
-
-
-
-
?
lanosterol + O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14,24-triene-3beta-ol + formate + NADP+ + H2O
-
-
-
?
lanosterol + O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14,24-triene-3beta-ol + formate + NADP+ + H2O
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
lanosta-8,24-dien-3beta-ol
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
4,4,14alpha-trimethyl-5alpha-cholesta-8,24-dien-3beta-ol
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
lanosta-8,24-dien-3beta-ol
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
4,4,14alpha-trimethyl-5alpha-cholesta-8,24-dien-3beta-ol
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
lanosta-8,24-dien-3beta-ol
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
4,4,14alpha-trimethyl-5alpha-cholesta-8,24-dien-3beta-ol
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
best substrate
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
natural substrate
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
lanosta-8,24-dien-3beta-ol
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
lanosta-8,24-dien-3beta-ol
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
4,4,14alpha-trimethyl-5alpha-cholesta-8,24-dien-3beta-ol
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
4,4,14alpha-trimethyl-5alpha-cholesta-8,24-dien-3beta-ol
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
best substrate
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
natural substrate
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
lanosta-8,24-dien-3beta-ol
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
4,4,14alpha-trimethyl-5alpha-cholesta-8,24-dien-3beta-ol
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
P-45014DM catalyzes all three oxygenation steps from lanosterol to dimethylcholestratrienol
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
ergosterol synthesis in yeast involves oxidative removal of the 14alpha-methyl group, C-32, of lanosterol
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
lanosta-8,24-dien-3beta-ol
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
4,4,14alpha-trimethyl-5alpha-cholesta-8,24-dien-3beta-ol
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethylcholesta-8,14,24-trien-3-ol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethylcholesta-8,14,24-trien-3-ol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethylcholesta-8,14,24-trien-3-ol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethylcholesta-8,14,24-trien-3-ol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethylcholesta-8,14,24-trien-3-ol + [oxidized NADPH-hemoprotein reductase] + H2O
i.e. lanosta-8,24-dien-3beta-ol
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethylcholesta-8,14,24-trien-3-ol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethylcholesta-8,14,24-trien-3-ol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethylcholesta-8,14,24-trien-3-ol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethylcholesta-8,14,24-trien-3-ol + [oxidized NADPH-hemoprotein reductase] + H2O
Pyricularia oryzae Guy11
-
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethylcholesta-8,14,24-trienol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethylcholesta-8,14,24-trienol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
deletion of the enzyme is lethal
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethylcholesta-8,14,24-trienol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethylcholesta-8,14,24-trienol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
deletion of the enzyme is lethal
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethylcholesta-8,14,24-trienol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethylcholesta-8,14,24-trienol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
isozymes CYP51A and CYP51B
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
isozymes CYP51A and CYP51B
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
production of follicular fluid-meiosis activating steroid by lanosterol demethylation
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
the enzyme is involved in ergosterol and cholesterol biosynthesis
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
production of follicular fluid-meiosis activating steroid by lanosterol demethylation
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
CYP51 responds to cholesterol feedback regulation, being upregulated in sterol limiting conditions and downregulated in cholesterol rich conditions, regulation involves the sterol regulatory elements SRE in the promoter of the gene which bind sterol regulatory element binding protein, SREBP, the CYP51 promoter also contains a cAMP regulatory element, CRE, binding cAMP regulatory proteins CREB/CREM, overview
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
the enzyme is involved in ergosterol and cholesterol biosynthesis
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
the enzyme is regulated by cholesterol feedback regulation through sterol regulatory element binding proteins, i.e. SREBPs, regulation mechanisms of enzyme expression, overview
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
the enzyme is involved in ergosterol and cholesterol biosynthesis
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
the enzyme is involved in ergosterol and cholesterol biosynthesis
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
the enzyme is involved in ergosterol and cholesterol biosynthesis
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
the enzyme is involved in ergosterol and cholesterol biosynthesis
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
active site contains an isoleucine, lanosterol is the preferred substrate
-
-
?
norlanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
norlanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
i.e. 4alpha,14alpha-dimethylcholesta-8,24-dien-3beta-ol
-
-
?
norlanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
-
?
norlanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis
-
-
?
norlanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis
-
-
?
norlanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
low activity
-
-
?
norlanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
i.e. 4alpha,4alpha-dimethylcholesta-8,24-dien-3beta-ol
-
-
?
norlanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
low activity
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
low activity
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
preferred substrate
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
low activity
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
low activity
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
low activity
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
preferred substrate
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
preferred substrate
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
the enzyme is involved in biosynthesis of sitosterol and brassinosteroids, pathways overview
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
low activity
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
low activity
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
preferred substrate
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
4alpha,14alpha-dimethyl-24-methylene-5alpha-cholesta-8-en-3beta-ol
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
catalyzes 14alpha-demethylation of obtusifoliol
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
4alpha,14alpha-dimethyl-5alpha-ergosta-8,24(28)-dien-3beta-ol
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
i.e. 4alpha,14alpha-dimethyl-5'-ergosta-8,24(24')-dien-3beta-ol
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
4alpha,14alpha-dimethyl-24-methylene-5alpha-cholesta-8-en-3beta-ol
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
catalyzes 14alpha-demethylation of obtusifoliol
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
4alpha,14alpha-dimethyl-5alpha-ergosta-8,24(28)-dien-3beta-ol
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
4alpha,14alpha-dimethyl-24-methylene-5alpha-cholesta-8-en-3beta-ol
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
catalyzes 14alpha-demethylation of obtusifoliol
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
4alpha,14alpha-dimethyl-5alpha-ergosta-8,24(28)-dien-3beta-ol
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
presence of the large phenylalanine side chain in the active site seems to lead to preferred processing of obtusifoliol
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
best substrate
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
4alpha,14alpha-dimethyl-24-methylene-5alpha-cholesta-8-en-3beta-ol
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
catalyzes 14alpha-demethylation of obtusifoliol
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
4alpha,14alpha-dimethyl-5alpha-ergosta-8,24(28)-dien-3beta-ol
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
additional information
?
-
-
azole binding properties of purified CYP51A and CYP51B, overview
-
-
?
additional information
?
-
-
azole binding properties of purified CYP51A and CYP51B, overview
-
-
?
additional information
?
-
-
enzyme of sterol biosynthesis, sterol 14-demethylation occurs in all organism exhibiting de novo sterol biosynthesis
-
-
?
additional information
?
-
-
the regio- and stereospecific 14alpha-demethylation CYP51 reaction proceeds in three steps, each requiring one molecule of oxygen and two NADPH-derived reducing equivalents, via 14alpha-carboxyalcohol and 14alpha-carboxyaldehyde intermediates, cleavage of the the C-C bond by radical or Bayer-Villiger mechanism, DELTA14,15 double bond introduction into the sterol core
-
-
?
additional information
?
-
-
enzyme of sterol biosynthesis, sterol 14-demethylation occurs in all organism exhibiting de novo sterol biosynthesis
-
-
?
additional information
?
-
-
can not catalyze demethylation of sterols having 4beta-methyl group, favorably interacts with sterols having saturated side chain
-
-
?
additional information
?
-
-
yeast enzyme poorly metabolizes sterols having saturated side chain, plant enzyme shows considerable activity for such sterols
-
-
?
additional information
?
-
-
substrate for 14alpha-demethylation reaction in plants is different from that in animals and fungi
-
-
?
additional information
?
-
-
14alpha-demethylation is a key step of sterol biosynthesis in eukaryotes
-
-
?
additional information
?
-
-
enzyme of plant sterol, phytosterol, biosynthesis
-
-
?
additional information
?
-
-
housekeeping enzyme essential for viability of mammals, essential step in cholesterol biosynthesis
-
-
?
additional information
?
-
-
enzyme of sterol biosynthesis, sterol 14-demethylation occurs in all organism exhibiting de novo sterol biosynthesis
-
-
?
additional information
?
-
-
there is a possibility that P45014DM participates not only in sterol biogenesis but also in production of biosignal substance regulating meiosis of mammalian oocytes
-
-
?
additional information
?
-
-
analysis of active site by stectroscopic titration, resonance Raman spectroscopy and EPR
-
-
?
additional information
?
-
-
CYP51 plays a key role in fertilization by producing intermediates that could serve as ligands for nuclear receptors
-
-
?
additional information
?
-
-
enzyme inhibition may result in endocrine disruption since follicular fluid-meiosis activating steroid, the direct product of lanosterol demethylation, is involved in the control of meiosis
-
-
?
additional information
?
-
-
the regio- and stereospecific 14alpha-demethylation CYP51 reaction proceeds in three steps, each requiring one molecule of oxygen and two NADPH-derived reducing equivalents, via 14alpha-carboxyalcohol and 14alpha-carboxyaldehyde intermediates, cleavage of the the C-C bond by radical or Bayer-Villiger mechanism, DELTA14,15 double bond introduction into the sterol core
-
-
?
additional information
?
-
-
the enzyme catalyzes a step in the cholesterol biosynthesis via the mevalonate pathway, overview
-
-
?
additional information
?
-
-
structure-activity relationship study of enzyme-ligand binding, pyridine binds within the heme binding pocket in an analogy with azoles, overview
-
-
?
additional information
?
-
-
CYP51 participates in biosynthesis of cholesterol
-
-
?
additional information
?
-
-
the regio- and stereospecific 14alpha-demethylation CYP51 reaction proceeds in three steps, each requiring one molecule of oxygen and two NADPH-derived reducing equivalents, via 14alpha-carboxyalcohol and 14alpha-carboxyaldehyde intermediates, cleavage of the the C-C bond by radical or Bayer-Villiger mechanism, DELTA14,15 double bond introduction into the sterol core
-
-
?
additional information
?
-
the enzyme is a demethylation inhibitor fungicide resistance determinant in Monilinia fructicola field isolates
-
-
?
additional information
?
-
-
the enzyme is a demethylation inhibitor fungicide resistance determinant in Monilinia fructicola field isolates
-
-
?
additional information
?
-
-
the enzyme is involved in follicle-stimulating hormone-induced mouse oocyte maturation and follicle-stimulating hormone-induced oocyte meiotic resumption, regulation, overview. The enzyme is involved in CREB phosphorylation
-
-
?
additional information
?
-
analysis of active site by spectroscopic titration, resonance Raman spectroscopy and EPR
-
-
?
additional information
?
-
-
analysis of active site by spectroscopic titration, resonance Raman spectroscopy and EPR
-
-
?
additional information
?
-
-
P420 formation process with protonation of Cys394 and structure by binding of CO to P450, overview
-
-
?
additional information
?
-
-
the regio- and stereospecific 14alpha-demethylation CYP51 reaction proceeds in three steps, each requiring one molecule of oxygen and two NADPH-derived reducing equivalents, via 14alpha-carboxyalcohol and 14alpha-carboxyaldehyde intermediates, cleavage of the the C-C bond by radical or Bayer-Villiger mechanism, DELTA14,15 double bond introduction into the sterol core
-
-
?
additional information
?
-
CYP51 is a major checkpoint in membrane sterol biosynthesis, is a key target for fungal antibiotic therapy
-
-
?
additional information
?
-
-
CYP51 is a major checkpoint in membrane sterol biosynthesis, is a key target for fungal antibiotic therapy
-
-
?
additional information
?
-
-
CYP51b1 shows activity with coumarin derivatives as substrates, e.g. with 7-ethoxycoumarin, 4-methyl-7-hydroxycoumarin, 4-methyl-7-aminocoumarin, and 7-aminocoumarin-4-acetic acid, that are competitive to lanosterol. In the model system for assay of CYP51b1 activity, a flavin domain of the cytochrome P450BM-3, BMR, from Bacillus megaterium may serve as the electron donor, overview
-
-
?
additional information
?
-
analysis of active site by spectroscopic titration, resonance Raman spectroscopy and EPR
-
-
?
additional information
?
-
CYP51 is a major checkpoint in membrane sterol biosynthesis, is a key target for fungal antibiotic therapy
-
-
?
additional information
?
-
-
the regio- and stereospecific 14alpha-demethylation CYP51 reaction proceeds in three steps, each requiring one molecule of oxygen and two NADPH-derived reducing equivalents, via 14alpha-carboxyalcohol and 14alpha-carboxyaldehyde intermediates, cleavage of the the C-C bond by radical or Bayer-Villiger mechanism, DELTA14,15 double bond introduction into the sterol core
-
-
?
additional information
?
-
CYP51 is one of the key enzymes of sterol biosynthesis in biological kingdoms and is a prime target of antifungal drugs
-
-
?
additional information
?
-
-
CYP51 is one of the key enzymes of sterol biosynthesis in biological kingdoms and is a prime target of antifungal drugs
-
-
?
additional information
?
-
-
enzyme of sterol biosynthesis, sterol 14-demethylation occurs in all organism exhibiting de novo sterol biosynthesis
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
sterol composition of different species isolated from human lung, two distinct sterol compositional phenotypes occur, one, the wild-type, is characterized by DELTA7 C28- and C24 24-alkylsterols with only low proportions of higher molecular mass components, the other type, a mutant with 14alpha-demethylase deficiency, is dominated by high C31 and C32 24-alkylsterols, especially pneumocysterol, NMR sterol analysis, overview
-
-
?
additional information
?
-
-
housekeeping enzyme essential for viability of mammals, essential step in cholesterol biosynthesis
-
-
?
additional information
?
-
-
enzyme of sterol biosynthesis, sterol 14-demethylation occurs in all organism exhibiting de novo sterol biosynthesis
-
-
?
additional information
?
-
-
brain microsomes, existence of sterol biosynthetic pathway in brain, cholesterol is synthesized de novo in brain
-
-
?
additional information
?
-
-
removal of 14alpha-methyl group, C32, from 14alpha-methylated precursor sterols is an essential step of sterol biosynthesis in eukaryotes
-
-
?
additional information
?
-
-
lanosterol 14-demethylation is situated at the root of sterol-biosynthetic branch of mevalonic acid pathway
-
-
?
additional information
?
-
enzyme for regulation of cholesterol biosynthesis
-
-
?
additional information
?
-
-
there is a possibility that P45014DM participates not only in sterol biogenesis but also in production of biosignal substance regulating meiosis of mammalian oocytes
-
-
?
additional information
?
-
-
the regio- and stereospecific 14alpha-demethylation CYP51 reaction proceeds in three steps, each requiring one molecule of oxygen and two NADPH-derived reducing equivalents, via 14alpha-carboxyalcohol and 14alpha-carboxyaldehyde intermediates, cleavage of the the C-C bond by radical or Bayer-Villiger mechanism, DELTA14,15 double bond introduction into the sterol core
-
-
?
additional information
?
-
-
4beta-methyl group, C31, does not affect the activity of yeast P-45014DM, although removal reduces affinity for enzyme in some extent
-
-
?
additional information
?
-
-
8-double bond of lanosterol plays an important critical role in enzyme-substrate interaction of cytochrome P-45014DM
-
-
?
additional information
?
-
-
no activity with 6-lanostene-3beta,32-diol and lanostane-3beta,32-diol
-
-
?
additional information
?
-
-
yeast enzyme poorly metabolizes sterols having saturated side chain, plant enzyme shows considerable activity for such sterols
-
-
?
additional information
?
-
-
enzyme recognizes 8-lanostene structure and favourably interacts with 8-lanostene derivatives, can act also with substrates having 7-lanostene structure, utilizes them with lower efficiency than 8-lanostene derivatives
-
-
?
additional information
?
-
-
cycloartenol: not or very poor substrate
-
-
?
additional information
?
-
-
3-hydroxy group, the 8-lanostene conformation of sterol ring and the side-chain terminal, C25, C26, C27, are the essential structures of substrates for interacting with the yeast enzyme
-
-
?
additional information
?
-
-
reaction reqires molecular oxygen, does not occur anaerobically
-
-
?
additional information
?
-
-
enzyme of sterol biosynthesis, sterol 14-demethylation occurs in all organism exhibiting de novo sterol biosynthesis
-
-
?
additional information
?
-
-
removal of 14alpha-methyl group, C32, from 14alpha-methylated precursor sterols is an essential step of sterol biosynthesis in eukaryotes
-
-
?
additional information
?
-
-
enzyme of ergosterol biosynthesis
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
14alpha-demethylation is a key step of sterol biosynthesis in eukaryotes
-
-
?
additional information
?
-
-
the regio- and stereospecific 14alpha-demethylation CYP51 reaction proceeds in three steps, each requiring one molecule of oxygen and two NADPH-derived reducing equivalents, via 14alpha-carboxyalcohol and 14alpha-carboxyaldehyde intermediates, cleavage of the the C-C bond by radical or Bayer-Villiger mechanism, DELTA14,15 double bond introduction into the sterol core
-
-
?
additional information
?
-
-
enzyme of sterol biosynthesis, sterol 14-demethylation occurs in all organism exhibiting de novo sterol biosynthesis
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
?
additional information
?
-
-
biosynthetic enzyme with very narrow substrate specificity
-
-
?
additional information
?
-
-
biosynthetic enzyme with very narrow substrate specificity
-
-
?
additional information
?
-
-
no activity with lanosterol, campesterol, sitosterol, or stigmasterol
-
-
?
additional information
?
-
-
enzyme is a multifunctional cytochrome P450, which as the same active site catalyze demethylation in three consecutive NADPH- and O2-dependent hydroxylation reactions, resulting in the elimination of the methyl group as formic acid and the introduction of a double bond at the DELTA14 position
-
-
?
additional information
?
-
-
enzyme is a multifunctional cytochrome P450, which as the same active site catalyze demethylation in three consecutive NADPH- and O2-dependent hydroxylation reactions, resulting in the elimination of the methyl group as formic acid and the introduction of a double bond at the DELTA14 position
-
-
?
additional information
?
-
-
substrate for 14alpha-demethylation reaction in plants is different from that in animals and fungi
-
-
?
additional information
?
-
-
plant sterol 14alpha-demethylase have high substrate specificity
-
-
?
additional information
?
-
-
plant sterol 14alpha-demethylase have high substrate specificity
-
-
?
additional information
?
-
-
catalyzes an essential step in sterol biosynthesis as evidenced by the absence of a 14alpha-methyl group in all known functional sterols, removal of the 14alpha-methyl group is essential
-
-
?
additional information
?
-
-
key enzyme in plant sterol, phytosterol, biosynthesis
-
-
?
additional information
?
-
-
enzyme of plant sterol, phytosterol, biosynthesis
-
-
?
additional information
?
-
-
poor activity with lanosterol, 24,25-dihydrolanosterol, and 24-methylenedihydrolanosterol, the regio- and stereospecific 14alpha-demethylation CYP51 reaction proceeds in three steps, each requiring one molecule of oxygen and two NADPH-derived reducing equivalents, via 14alpha-carboxyalcohol and 14alpha-carboxyaldehyde intermediates, cleavage of the the C-C bond by radical or Bayer-Villiger mechanism, DELTA14,15 double bond introduction into the sterol core
-
-
?
additional information
?
-
-
poor activity with lanosterol, 24,25-dihydrolanosterol, and 24-methylenedihydrolanosterol, the regio- and stereospecific 14alpha-demethylation CYP51 reaction proceeds in three steps, each requiring one molecule of oxygen and two NADPH-derived reducing equivalents, via 14alpha-carboxyalcohol and 14alpha-carboxyaldehyde intermediates, cleavage of the the C-C bond by radical or Bayer-Villiger mechanism, DELTA14,15 double bond introduction into the sterol core
-
-
?
additional information
?
-
-
the organism can specifically regulate gene expression, e.g. for the sterol C14-demethylase, in response to derangements in its cellular functions
-
-
?
additional information
?
-
substrate specificity, the Trypanosoma cruzi enzyme prefers C4-dimethylsterols substrates, overview
-
-
?
additional information
?
-
-
substrate specificity, the Trypanosoma cruzi enzyme prefers C4-dimethylsterols substrates, overview
-
-
?
additional information
?
-
-
the regio- and stereospecific 14alpha-demethylation CYP51 reaction proceeds in three steps, each requiring one molecule of oxygen and two NADPH-derived reducing equivalents, via 14alpha-carboxyalcohol and 14alpha-carboxyaldehyde intermediates, cleavage of the the C-C bond by radical or Bayer-Villiger mechanism, DELTA14,15 double bond introduction into the sterol core
-
-
?
additional information
?
-
-
enzyme of sterol biosynthesis, sterol 14-demethylation occurs in all organism exhibiting de novo sterol biosynthesis
-
-
?
additional information
?
-
-
the regio- and stereospecific 14alpha-demethylation CYP51 reaction proceeds in three steps, each requiring one molecule of oxygen and two NADPH-derived reducing equivalents, via 14alpha-carboxyalcohol and 14alpha-carboxyaldehyde intermediates, cleavage of the the C-C bond by radical or Bayer-Villiger mechanism, DELTA14,15 double bond introduction into the sterol core
-
-
?
additional information
?
-
-
no activity with 31-norlanosterol, cycloeucalenol, 4alpha,14alpha-dimethyl-5alpha-ergost-9(11)-en-3beta-ol, 4alpha,14alpha-dimethyl-5alpha-ergost-7-en-3beta-ol, 8(9),24(25)-tetrahydro-31-norlanosterol, 24-methylenelanosterol, 24,28-dihydro-4beta-methyl-30-norobtusifoliol, 24,25-dihydrolanosterol, lanosterol, obtusifoliyl-3beta-methoxy, obtusifoliyl-3beta-acetoxy, obtusifoliyl-3beta-amino
-
-
?
additional information
?
-
-
biosynthetic enzyme with very narrow substrate specificity
-
-
?
additional information
?
-
-
biosynthetic enzyme with very narrow substrate specificity
-
-
?
additional information
?
-
-
P-450OBT 14DM has probably a specific apolar binding site for the side chain. DELTA8-double bond is absolute required for substrate demethylation and the 3-hydroxy group plays a critical role in enzyme-substrate interaction
-
-
?
additional information
?
-
-
enzyme with high degree of substrate and product specificity
-
-
?
additional information
?
-
-
plant sterol 14alpha-demethylase have high substrate specificity
-
-
?
additional information
?
-
-
plant sterol 14alpha-demethylase have high substrate specificity
-
-
?
additional information
?
-
-
enzyme of plant sterol, phytosterol, biosynthesis
-
-
?
additional information
?
-
-
enzyme of plant sterol, phytosterol, biosynthesis
-
-
?
additional information
?
-
-
no activity with 31-norlanosterol, cycloeucalenol, 4alpha,14alpha-dimethyl-5alpha-ergost-9(11)-en-3beta-ol, 4alpha,14alpha-dimethyl-5alpha-ergost-7-en-3beta-ol, 8(9),24(25)-tetrahydro-31-norlanosterol, 24-methylenelanosterol, 24,28-dihydro-4beta-methyl-30-norobtusifoliol, 24,25-dihydrolanosterol, lanosterol, obtusifoliyl-3beta-methoxy, obtusifoliyl-3beta-acetoxy, obtusifoliyl-3beta-amino
-
-
?
additional information
?
-
-
biosynthetic enzyme with very narrow substrate specificity
-
-
?
additional information
?
-
-
P-450OBT 14DM has probably a specific apolar binding site for the side chain. DELTA8-double bond is absolute required for substrate demethylation and the 3-hydroxy group plays a critical role in enzyme-substrate interaction
-
-
?
additional information
?
-
-
enzyme with high degree of substrate and product specificity
-
-
?
additional information
?
-
-
residues Ile381 and Leu321 are involved in substrate recognition
-
-
?
