EC 1.14.14.126 - β-amyrin 28-monooxygenase

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IntEnz Enzyme Nomenclature
EC 1.14.14.126

Names

Accepted name:
β-amyrin 28-monooxygenase
Other names:
CYP716A52v2
CYP716A12
β-amyrin 28-oxidase
CYP16A75
Systematic name:
β-amyrin,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (28-hydroxylating)

Reaction

Comments:

A cytochrome P450 (heme-thiolate) protein found in plants. The enzyme is involved in the biosynthesis of oleanane-type triterpenoids, such as ginsenoside Ro. The enzyme from Medicago truncatula (barrel medic) (CYP716A12) can also convert α-amyrin and lupeol to ursolic acid and betulinic acid, respectively. The enzyme from Maesa lanceolata (false assegai) (CYP16A75) does not catalyse the reaction to completion, resulting in accumulation of both intermediates. Formerly EC 1.14.13.201.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot:

References

  1. Fukushima, E. O., Seki, H., Ohyama, K., Ono, E., Umemoto, N., Mizutani, M., Saito, K., Muranaka, T.
    CYP716A subfamily members are multifunctional oxidases in triterpenoid biosynthesis.
    Plant Cell Physiol. 52 : 2050-2061 (2011). [PMID: 22039103]
  2. Han, J. Y., Kim, M. J., Ban, Y. W., Hwang, H. S., Choi, Y. E.
    The involvement of ?-amyrin 28-oxidase (CYP716A52v2) in oleanane-type ginsenoside biosynthesis in Panax ginseng.
    Plant Cell Physiol. 54 : 2034-2046 (2013). [PMID: 24092881]
  3. Moses, T., Pollier, J., Faizal, A., Apers, S., Pieters, L., Thevelein, J. M., Geelen, D., Goossens, A.
    Unraveling the triterpenoid saponin biosynthesis of the African shrub Maesa lanceolata.
    Mol Plant 8 : 122-135 (2015). [PMID: 25578277]

[EC 1.14.14.126 created 2015 as EC 1.14.13.201, transferred 2018 to EC 1.14.14.126]