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Literature summary for 2.1.1.285 extracted from

  • Gomez Garcia, I.; Stevenson, C.E.; Uson, I.; Freel Meyers, C.L.; Walsh, C.T.; Lawson, D.M.
    The crystal structure of the novobiocin biosynthetic enzyme NovP: the first representative structure for the TylF O-methyltransferase superfamily (2010), J. Mol. Biol., 395, 390-407.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
high resolution crystal structure of NovP as a binary complex with its desmethylated co-substrate, S-adenosyl-L-homocysteine. The structure includes a helical lid region that gates access to the co-substrate binding pocket, and an active centre that contains a 3-Asp putative metal-binding site. A further conserved Asp likely acts as the general base that initiates the reaction by deprotonating the 4-OH group of the noviose unit. Models suggest that NovP is unlikely to tolerate significant modifications at the noviose moiety, but could show increasing substrate promiscuity as a function of the distance of the modification from the methylation site. These observations could inform future attempts to utilise NovP for methylating a range of glycosylated compounds Streptomyces niveus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
66000
-
gel filtration Streptomyces niveus

Organism

Organism UniProt Comment Textmining
Streptomyces niveus Q9L9F2
-
-

Purification (Commentary)

Purification (Comment) Organism
N-terminally His-tagged enzyme Streptomyces niveus

Subunits

Subunits Comment Organism
dimer
-
Streptomyces niveus

Synonyms

Synonyms Comment Organism
NovP
-
Streptomyces niveus