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Literature summary for 1.14.14.154 extracted from

  • Aoyama, Y.; Yoshida, Y.; Sonoda, Y.; Sato, Y.
    Role of the 8-double bond of lanosterol in the enzyme-substrate interaction of cytochrome P-45014DM (lanosterol 14alpha-demethylase) (1989), Biochim. Biophys. Acta, 1001, 196-200.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
7-lanostene-3beta,32-diol activation Saccharomyces cerevisiae
7-lanostene-3beta-ol activation Saccharomyces cerevisiae
8-lanostene-3beta,32-diol activation Saccharomyces cerevisiae
8-lanostene-3beta-ol activation Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetics Saccharomyces cerevisiae
additional information
-
additional information enzyme shows higher affinity for 8-lanostene conformation, such as lanosterol and 24,25-dihydrolanosterol, than for 7-lanostene one Saccharomyces cerevisiae
additional information
-
additional information affinity and activity for 7-lanosten-3beta-ol is very low, no exact Km Saccharomyces cerevisiae
0.0001
-
8-lanostene-3beta,32-diol
-
Saccharomyces cerevisiae
0.003
-
7-lanostene-3beta,32-diol
-
Saccharomyces cerevisiae
0.02
-
24,25-dihydrolanosterol 8-lanosten-3beta-ol Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2 Saccharomyces cerevisiae 8-lanosta-3beta-ol 4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2 Saccharomyces cerevisiae DHL 4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2 Saccharomyces cerevisiae 8-lanosten-3beta-ol 4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2 Saccharomyces cerevisiae 4,4,14alpha-trimethyl-5alpha-cholesta-8-en-3beta-ol 4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2 Saccharomyces cerevisiae lanosta-8,24-dien-3beta-ol 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2 Saccharomyces cerevisiae 4,4,14alpha-trimethyl-5alpha-cholesta-8,24-dien-3beta-ol 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Saccharomyces cerevisiae

Reaction

Reaction Comment Organism Reaction ID
a 14alpha-methylsteroid + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = a DELTA14-steroid + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O mechanism Saccharomyces cerevisiae

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2 8-lanosta-3beta-ol Saccharomyces cerevisiae 4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2 DHL Saccharomyces cerevisiae 4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2 8-lanosten-3beta-ol Saccharomyces cerevisiae 4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2 4,4,14alpha-trimethyl-5alpha-cholesta-8-en-3beta-ol Saccharomyces cerevisiae 4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
?
7-lanosten-3beta-ol + [reduced NADPH-hemoprotein reductase] + O2 very low activity Saccharomyces cerevisiae 4,4-dimethylcholesta-7,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
?
7-lanostene-3beta,32-diol + [reduced NADPH-hemoprotein reductase] + O2 very low activity Saccharomyces cerevisiae 4,4-dimethylcholesta-7,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
?
8-lanostene-3beta,32-diol + [reduced NADPH-hemoprotein reductase] + O2
-
Saccharomyces cerevisiae 4,4-dimethylcholesta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2 best substrate Saccharomyces cerevisiae 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2 lanosta-8,24-dien-3beta-ol Saccharomyces cerevisiae 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2 4,4,14alpha-trimethyl-5alpha-cholesta-8,24-dien-3beta-ol Saccharomyces cerevisiae 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
?
additional information 8-double bond of lanosterol plays an important critical role in enzyme-substrate interaction of cytochrome P-45014DM Saccharomyces cerevisiae ?
-
?
additional information no activity with 6-lanostene-3beta,32-diol and lanostane-3beta,32-diol Saccharomyces cerevisiae ?
-
?
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 Saccharomyces cerevisiae ?
-
?
additional information narrow substrate selectivity Saccharomyces cerevisiae ?
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Saccharomyces cerevisiae
30
-
aerobic conditions Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
cytochrome P450
-
Saccharomyces cerevisiae
heme heme-thiolate enzyme Saccharomyces cerevisiae