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Literature summary extracted from

  • Takakuwa, Y.; Nishino, H.; Ishibe, Y.; Ishibashi, T.
    Properties and kinetics of membrane-bound enzymes when both the enzyme and substrate are components of the same microsomal membrane. Studies on lathosterol 5-desaturase (1994), J. Biol. Chem., 269, 27889-27893.
    View publication on PubMed

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.14.19.20 microsome
-
Rattus norvegicus
-
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.19.20 lathosterol + ferrocytochrome b5 + O2 + H+ Rattus norvegicus
-
7-dehydrocholesterol + ferricytochrome b5 + H2O
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.14.19.20 Rattus norvegicus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.14.19.20 liver
-
Rattus norvegicus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.19.20 lathosterol + ferrocytochrome b5 + O2 + H+
-
Rattus norvegicus 7-dehydrocholesterol + ferricytochrome b5 + H2O
-
?

Synonyms

EC Number Synonyms Comment Organism
1.14.19.20 Lathosterol 5-desaturase
-
Rattus norvegicus

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.19.20 cytochrome b5
-
Rattus norvegicus
1.14.19.20 NADH dependent on Rattus norvegicus
1.14.19.20 NADPH can replace NADH Rattus norvegicus