4.2.1.95: kievitone hydratase
This is an abbreviated version!
For detailed information about kievitone hydratase, go to the full flat file.
Reaction
Synonyms
FsKHS, hydratase, kievitone, KHase, NhKHS
ECTree
Advanced search results
General Information
General Information on EC 4.2.1.95 - kievitone hydratase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
evolution
physiological function
the enzyme belongs to the hydro-lyases, which are able to catalyze the highly selective, reversible addition of water to non-activated carbon-carbon double bonds and, thereby, generate primary, secondary or tertiary alcohols
evolution
the enzyme is a member of the hydrolyase enzyme group
evolution
the enzyme is a member of the hydrolyase enzyme group. Hydro-lyases are able to catalyze the highly selective, reversible addition of water to non-activated carbon-carbon double bonds and, thereby, generate primary, secondary or tertiary alcohols
evolution
Fusarium solani 77-13-4 / ATCC MYA-4622 / FGSC 9596 / MPVI
-
the enzyme belongs to the hydro-lyases, which are able to catalyze the highly selective, reversible addition of water to non-activated carbon-carbon double bonds and, thereby, generate primary, secondary or tertiary alcohols
-
evolution
Fusarium solani 77-13-4 / ATCC MYA-4622 / FGSC 9596 / MPVI
-
the enzyme is a member of the hydrolyase enzyme group
-
kievitone hydratase catalyzes the addition of water to the double bond of the prenyl moiety of plant isoflavonoid kievitone and, thereby, forms the tertiary alcohol hydroxy-kievitone. In nature, this conversion is associated with a defense mechanism of fungal pathogens against phytoalexins generated by host plants after infection
physiological function
Fusarium solani 77-13-4 / ATCC MYA-4622 / FGSC 9596 / MPVI
-
kievitone hydratase catalyzes the addition of water to the double bond of the prenyl moiety of plant isoflavonoid kievitone and, thereby, forms the tertiary alcohol hydroxy-kievitone. In nature, this conversion is associated with a defense mechanism of fungal pathogens against phytoalexins generated by host plants after infection
-