Dihydrocoumarin hydrolase

Dihydrocoumarin hydrolase
Identifiers
EC no.3.1.1.35
CAS no.37278-47-0
Databases
BRENDAenzyme data
ExPASyNiceZyme view
KEGGenzyme entry
MetaCycmetabolic pathway
Rheareactions
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

Dihydrocoumarin hydrolase (EC 3.1.1.35) is an enzyme that catalyzes the reaction

2D representation of the chemical structure of Q27098403.
2-chromanone
 
H2O
 
Rightward reaction arrow with minor substrate(s) from top left
 
 
 
2D representation of the chemical structure of Q11751633.
melilotic acid

The enzyme characterised from Melilotus alba hydrolyses 2-chromanone to melilotic acid.[1] The enzyme is part of a pathway that degrades the aromatic hydrocarbon, fluorene.[2][3]

This enzyme is a hydrolase, specifically one acting on carboxylic ester bonds. The systematic name is dihydrocoumarin lactonohydrolase.[4]

References

  1. ↑ Kosuge, T.; Conn, Eric E. (1962). "The Metabolism of Aromatic Compounds in Higher Plants". Journal of Biological Chemistry. 237 (5): 1653–1656. doi:10.1016/S0021-9258(19)83757-2.
  2. ↑ Kataoka, Michihiko; Honda, Kohsuke; Shimizu, Sakayu (2000). "3,4-Dihydrocoumarin hydrolase with haloperoxidase activity from Acinetobacter calcoaceticus F46". European Journal of Biochemistry. 267 (1): 3–10. doi:10.1046/j.1432-1327.2000.00889.x. PMID 10601844.
  3. ↑ Gu, Yichao; Li, Tao; Zhou, Ning-Yi (2023). "Redundant and scattered genetic determinants for coumarin biodegradation in Pseudomonas sp. Strain NyZ480". Applied and Environmental Microbiology. 89 (10) e01109-23. doi:10.1128/aem.01109-23. PMC 10617510. PMID 37815346.
  4. ↑ Enzyme 3.1.1.35 at KEGG Pathway Database.