2-hydroxyisoflavanone dehydratase

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2-hydroxyisoflavanone dehydratase
Identifiers
EC no.4.2.1.105
CAS no.56022-25-4
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

In enzymology, a 2-hydroxyisoflavanone dehydratase (EC 4.2.1.105) is an enzyme that catalyzes the chemical reaction

2,7,4'-trihydroxyisoflavanone daidzein + H2O

Hence, this enzyme has one substrate, , and two products, daidzein and H2O.

This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is 2,7,4'-trihydroxyisoflavanone hydro-lyase (daidzein-forming). This enzyme is also called 2,7,4'-trihydroxyisoflavanone hydro-lyase. This enzyme participates in isoflavonoid biosynthesis.

The variant GmHID1 from Glycine max converts to isoflavones, mostly daidzein and genistein.[1]

References[]

  1. ^ Bauters, Lander; Lander Bauers; Stojilković, Boris; Gheysen, Godelieve (2021-08-19). "Pathogens pulling the strings: Effectors manipulating salicylic acid and phenylpropanoid biosynthesis in plants". Molecular Plant Pathology. British Society for Plant Pathology (Wiley): 1–13. doi:10.1111/mpp.13123. ISSN 1464-6722. PMID 34414650.
  • Hakamatsuka T, Mori K, Ishida S, Ebizuka Y, Sankawa U (1998). "Purification of 2-hydroxyisoflavanone dehydratase from the cell cultures of Pueraria lobata". Phytochemistry. 49 (2): 497–505. doi:10.1016/S0031-9422(98)00266-0.


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