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1.14.15.34: 20-oxo-5-O-mycaminosyltylactone 23-monooxygenase

This is an abbreviated version!
For detailed information about 20-oxo-5-O-mycaminosyltylactone 23-monooxygenase, go to the full flat file.

Reaction

20-oxo-5-O-beta-mycaminosyltylactone
+ 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ +
O2
=
5-O-beta-mycaminosyltylonolide
+ 2 oxidized ferredoxin [iron-sulfur] cluster +
H2O

Synonyms

chmH, EC 1.14.13.186, TylH, tylH1

ECTree

     1 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.15 With reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen into the other donor
                1.14.15.34 20-oxo-5-O-mycaminosyltylactone 23-monooxygenase

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Resultsin table
3AA Sequence
1General Information
1Natural Substrates/ Products (Substrates)
2Organism
4Pathway
1Reaction
2Reference
2Substrates and Products (Substrate)
4Synonyms
1Systematic Name

General Information

General Information on EC 1.14.15.34 - 20-oxo-5-O-mycaminosyltylactone 23-monooxygenase

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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
the tylH mutant, which is blocked in the oxidation of C-23 methyl to hydroxymethyl, is capable of carrying out all other biosynthetic steps except addition of 6-deoxy-D-allose and subsequent O-methylations and produces the biologically active compound 23-deoxydemycinosyl tylosine. A tyID tylH lacking double mutant, blocked specifically in the biosynthesis of 6-deoxy-D-allose and in specific oxidation of tylactone, accumulates 23-deoxydemycinosyl tylosin and therefore cannot oxidize the C-23 methyl position of lactone