EC 1.14.14.124 - Dihydromonacolin L hydroxylase

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IntEnz Enzyme Nomenclature
EC 1.14.14.124

Names

Accepted name:
dihydromonacolin L hydroxylase
Other name:
LovA [ambiguous]
Systematic name:
dihydromonacolin L acid,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (3-hydroxylating)

Reaction

Cofactor

Comments:

A cytochrome P450 (heme-thiolate) protein. The dehydration of 3α-hydroxy-3,5-dihydromonacolin L acid is believed to be spontaneous [1,2]. The enzyme from fungi also catalyses the reaction of EC 1.14.14.125, monacolin L hydroxylase [3].

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. Treiber, L. R., Reamer, R. A., Rooney, C. S., Ramjit, H. G.
    Origin of monacolin L from Aspergillus terreus cultures.
    J. Antibiot. 42 : 30-36 (1989). [PMID: 2921224]
  2. Nakamura, T., Komagata, D., Murakawa, S., Sakai, K., Endo, A.
    Isolation and biosynthesis of 3 alpha-hydroxy-3,5-dihydromonacolin L.
    J. Antibiot. 43 : 1597-1600 (1990). [PMID: 2276977]
  3. Barriuso, J., Nguyen, D. T., Li, J. W., Roberts, J. N., MacNevin, G., Chaytor, J. L., Marcus, S. L., Vederas, J. C., Ro, D. K.
    Double oxidation of the cyclic nonaketide dihydromonacolin L to monacolin J by a single cytochrome P450 monooxygenase, LovA.
    J. Am. Chem. Soc. 133 : 8078-8081 (2011). [PMID: 21495633]

[EC 1.14.14.124 created 2014 as EC 1.14.13.197, transferred 2018 to EC 1.14.14.124]