Biology:Flavanone 3-dioxygenase
| Naringenin 3-dioxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.14.11.9 | ||||||||
| CAS number | 75991-43-4 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Flavanone 3-dioxygenase (EC 1.14.11.9) is an enzyme that catalyzes several chemical reactions of flavanones.[1][2] For example, naringenin is converted to aromadendrin:
- REDIRECT Template:Chemical reaction
The enzyme is a member of a superfamily of alpha-ketoglutarate-dependent hydroxylases. Its substrates are a flavanone such as naringenin and oxygen. These are converted into a flavanonol.[3]
This enzyme is an oxidase, with systematic name flavanone,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating). Other names in common use include naringenin 3-hydroxylase, flavanone 3-hydroxylase, flavanone 3beta-hydroxylase, flavanone synthase I, (2S)-flavanone 3-hydroxylase, and naringenin,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating). It is a non-heme iron protein with ferryl active site where Fe(IV)=O is the species that transfers its oxygen to the substrate.[4]
The mechanism of action requires 2-oxoglutaric acid to activate the iron oxygen complex, and this gives succinic acid and carbon dioxide when the second atom of the molecular oxygen is removed. Ascorbic acid improves the turnover number of the enzyme.[4][5]
- REDIRECT Template:Chemical reaction
References
- ↑ "Anthocyanin biosynthesis in flowers of Matthiola incana flavanone 3- and flavonoid 3'-hydroxylases". Z. Naturforsch. C: Biosci. 35: 691–695. 1980. doi:10.1515/znc-1980-9-1004.
- ↑ "Significance of C-terminal sequence elements for Petunia flavanone 3beta-hydroxylase activity". FEBS Lett. 561 (1–3): 149–54. 2004. doi:10.1016/S0014-5793(04)00159-0. PMID 15013767. Bibcode: 2004FEBSL.561..149W.
- ↑ Enzyme 1.14.11.9 at KEGG Pathway Database.
- ↑ 4.0 4.1 Mbenza, Naasson M.; Vadakkedath, Praveen G.; McGillivray, Duncan J.; Leung, Ivanhoe K.H. (2017). "NMR studies of the non-haem Fe(II) and 2-oxoglutarate-dependent oxygenases". Journal of Inorganic Biochemistry 177: 384–394. doi:10.1016/j.jinorgbio.2017.08.032. PMID 28893416.
- ↑ Clifton, Ian J.; Hsueh, Li-Ching; Baldwin, Jack E.; Harlos, Karl; Schofield, Christopher J. (2001). "Structure of proline 3-hydroxylase". European Journal of Biochemistry 268 (24): 6625–6636. doi:10.1046/j.0014-2956.2001.02617.x. PMID 11737217.
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