EC 1.14.15.33 - Pikromycin synthase

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IntEnz Enzyme Nomenclature
EC 1.14.15.33

Names

Accepted name:
pikromycin synthase
Other names:
PikC
CYP107L1
Systematic name:
narbomycin,reduced ferredoxin:oxygen oxidoreductase (pikromycin-forming)

Reactions

Cofactor

Comments:

A cytochrome P450 (heme-thiolate) protein. Involved in the biosynthesis of a number of bacterial macrolide antibiotics containing a desosamine glycoside unit. With narbomycin it hydroxylates at either C-12 to give pikromycin or C-14 to give neopikromycin or both positions to give narvopikromycin. With 10-deoxymethymycin it hydroxylates at either C-10 to give methymycin or C-12 to give neomethymycin or both positions to give novamethymycin. Formerly EC 1.14.13.185.

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. Xue, Y., Wilson, D., Zhao, L., Liu, H., Sherman, D. H.
    Hydroxylation of macrolactones YC-17 and narbomycin is mediated by the pikC-encoded cytochrome P450 in Streptomyces venezuelae.
    Chem. Biol. 5 : 661-667 (1998). [PMID: 9831532]
  2. Sherman, D. H., Li, S., Yermalitskaya, L. V., Kim, Y., Smith, J. A., Waterman, M. R., Podust, L. M.
    The structural basis for substrate anchoring, active site selectivity, and product formation by P450 PikC from Streptomyces venezuelae.
    J. Biol. Chem. 281 : 26289-26297 (2006). [PMID: 16825192]
  3. Li, S., Ouellet, H., Sherman, D. H., Podust, L. M.
    Analysis of transient and catalytic desosamine-binding pockets in cytochrome P-450 PikC from Streptomyces venezuelae.
    J. Biol. Chem. 284 : 5723-5730 (2009). [PMID: 19124459]

[EC 1.14.15.33 created 2014 as EC 1.14.13.185, transferred 2018 to EC 1.14.15.33]