Article · Wikipedia archive · Last revised Jul 19, 2026

2-hydroxyisoflavanone dehydratase

The enzyme 2-hydroxyisoflavanone dehydratase catalyzes the chemical reaction

Last revised
Jul 19, 2026
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2-hydroxyisoflavanone dehydratase
Identifiers
EC no.4.2.1.105
CAS no.56022-25-4
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The enzyme 2-hydroxyisoflavanone dehydratase (EC 4.2.1.105) catalyzes the chemical reaction

2D representation of the chemical structure of Q27123131.
2,4',7-trihydroxyisoflavanone
 
 
H2O
Rightward reaction arrow with minor product(s) to top right
 
 
 


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.1 This enzyme forms part of the pathway to isoflavones from flavonoids.23 The starting material, 2,4',7-trihydroxyisoflavanone, is produced from liquiritigenin by the enzyme isoflavonoid synthase4

Synthase
 
 
Rightward reaction arrow
 
 
 
2D representation of the chemical structure of Q27123131.
2,4',7-trihydroxyisoflavanone


2-hydroxyisoflavanone dehydratase also acts on the intermediate tetrahydroxyisoflavanone produced from naringenin, leading to genistein.5

Synthase
 
 
Rightward reaction arrow
 
 
 
2,4',5,7-tetrahydroxyisoflavanone
 
Dehydratase
 
H2O
Rightward reaction arrow with minor product(s) to top right
 
 
 


The variant GmHID1 from Glycine max shows both these activities.5

References

References

  1. Enzyme 4.2.1.105 at KEGG Pathway Database.
  2. 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.
  3. Ververidis Filippos, F; Trantas Emmanouil; Douglas Carl; Vollmer Guenter; Kretzschmar Georg; Panopoulos Nickolas (October 2007). "Biotechnology of flavonoids and other phenylpropanoid-derived natural products. Part I: Chemical diversity, impacts on plant biology and human health". Biotechnology Journal. 2 (10): 1214–34. doi:10.1002/biot.200700084. PMID 17935117.
  4. Sawada Y, Kinoshita K, Akashi T, Aoki T, Ayabe S (September 2002). "Key amino acid residues required for aryl migration catalysed by the cytochrome P450 2-hydroxyisoflavanone synthase". The Plant Journal. 31 (5): 555–64. doi:10.1046/j.1365-313x.2002.01378.x. PMID 12207646.
  5. 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. 22 (11). British Society for Plant Pathology (Wiley): 1436–1448. Bibcode:2021MolPP..22.1436B. doi:10.1111/mpp.13123. ISSN 1464-6722. PMC 8518561. PMID 34414650.