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Literature summary for 1.6.99.1 extracted from

  • Kataoka, M.; Kotaka, A.; Hasegawa, A.; Wada, M.; Yoshizumi, A.; Nakamori, S.; Shimizu, S.
    Old Yellow Enzyme from Candida macedoniensis catalyzes the stereospecific reduction of the C=C bond of ketoisophorone (2002), Biosci. Biotechnol. Biochem., 66, 2651-2657.
    View publication on PubMed

Application

Application Comment Organism
synthesis production of (6R)-levodione in Escherichia coli expressing the enzyme plus glucose dehydrogenase with a molar yield of 95% Candida macedoniensis

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Candida macedoniensis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
42400
-
x * 45890, deduced from gene sequence, x * 42400, SDS-PAGE Candida macedoniensis
45890
-
x * 45890, deduced from gene sequence, x * 42400, SDS-PAGE Candida macedoniensis

Organism

Organism UniProt Comment Textmining
Candida macedoniensis
-
expression in Escherichia coli
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ketoisophorone + NADPH + H+ i.e. 2,6,6-trimethyl-2-cyclohexen-1,4-dione Candida macedoniensis (6R)-levodione + NADP+ i.e.2,6,6-trimethylcycolhexane-1,4-dione ?

Subunits

Subunits Comment Organism
? x * 45890, deduced from gene sequence, x * 42400, SDS-PAGE Candida macedoniensis

Cofactor

Cofactor Comment Organism Structure
NADPH
-
Candida macedoniensis