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Literature summary extracted from

  • Kreuzman, A.J.; Turner, J.R.; Yeh, W.K.
    Two distinctive O-methyltransferases catalyzing penultimate and terminal reactions of macrolide antibiotic (tylosin) biosynthesis. Substrate specificity, enzyme inhibition, and kinetic mechanism (1988), J. Biol. Chem., 263, 15626-15633.
    View publication on PubMed

Application

EC Number Application Comment Organism
2.1.1.101 pharmacology tylosin fermentation, antibiotic biosynthesis, enzyme catalyzes conversion of macrocin to tylosin in vivo Streptomyces fradiae
2.1.1.102 pharmacology tylosin fermentation, antibiotic biosynthesis Streptomyces fradiae

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.1.1.101 A9145C
-
Streptomyces fradiae
2.1.1.101 demethyllactenocin
-
Streptomyces fradiae
2.1.1.101 Demethylmacrocin
-
Streptomyces fradiae
2.1.1.101 Desmycosin weak inhibition Streptomyces fradiae
2.1.1.101 Relomycin weak inhibition Streptomyces fradiae
2.1.1.101 S-adenosyl-L-homocysteine not D-enantiomer Streptomyces fradiae
2.1.1.101 sinefungin competitive inhibition, potent inhibitor Streptomyces fradiae
2.1.1.101 tylosin weak inhibition Streptomyces fradiae
2.1.1.102 20-Dihydro-23-deoxymycaminosyltylonolide
-
Streptomyces fradiae
2.1.1.102 20-dihydrolactenocin inhibition of macrocin formation Streptomyces fradiae
2.1.1.102 20-Dihydromacrocin
-
Streptomyces fradiae
2.1.1.102 23-demycinosyloxytylosin
-
Streptomyces fradiae
2.1.1.102 23-Deoxy-O-mycaminosyltylonolide
-
Streptomyces fradiae
2.1.1.102 A9145C
-
Streptomyces fradiae
2.1.1.102 demycinosyltylosin
-
Streptomyces fradiae
2.1.1.102 Fe2+
-
Streptomyces fradiae
2.1.1.102 lactenocin inhibition of macrocin formation Streptomyces fradiae
2.1.1.102 macrocin inhibition of lactenocin formation Streptomyces fradiae
2.1.1.102 mycaminosyltylactone
-
Streptomyces fradiae
2.1.1.102 mycaminosyltylonolide
-
Streptomyces fradiae
2.1.1.102 O-Mycaminosyltylonolide
-
Streptomyces fradiae
2.1.1.102 S-adenosyl-L-homocysteine not D-enantiomer Streptomyces fradiae
2.1.1.102 sinefungin competitive inhibition, poor inhibitor Streptomyces fradiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.1.1.101 0.005
-
macrocin
-
Streptomyces fradiae
2.1.1.101 0.007
-
lactenocin
-
Streptomyces fradiae
2.1.1.101 0.022
-
S-adenosyl-L-methionine lactenocin as substrate Streptomyces fradiae
2.1.1.101 0.023
-
S-adenosyl-L-methionine macrocin as substrate Streptomyces fradiae
2.1.1.102 0.006
-
Demethylmacrocin
-
Streptomyces fradiae
2.1.1.102 0.01
-
demethyllactenocin
-
Streptomyces fradiae
2.1.1.102 0.111
-
S-adenosylmethionine
-
Streptomyces fradiae

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.1.1.101 Co2+ can substitute Mg2+ Streptomyces fradiae
2.1.1.101 Mg2+ required for maximal activity Streptomyces fradiae
2.1.1.101 Mn2+ can substitute Mg2+ Streptomyces fradiae
2.1.1.102 Mg2+ required for maximal activity Streptomyces fradiae

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.1.1.101 32000
-
2 * 32000, SDS-PAGE Streptomyces fradiae
2.1.1.101 65000
-
-
Streptomyces fradiae
2.1.1.102 42000
-
3 * 42000, SDS-PAGE Streptomyces fradiae
2.1.1.102 122000 126000 gel filtration Streptomyces fradiae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.1.101 S-adenosyl-L-methionine + macrocin Streptomyces fradiae enzyme catalyzes 3'''-O-methylation of bound 2'''-O-methylated 6-deoxy-D-allose S-adenosylhomocysteine + tylosin
-
?
2.1.1.102 S-adenosyl-L-methionine + demethylmacrocin Streptomyces fradiae enzyme catalyzes 2'''-O-methylation of bound 6-deoxy-D-allose S-adenosyl-L-homocysteine + macrocin
-
?
2.1.1.102 S-adenosyl-L-methionine + demethylmacrocin Streptomyces fradiae penultimate step in tylosin biosynthesis S-adenosyl-L-homocysteine + macrocin
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.101 Streptomyces fradiae
-
-
-
2.1.1.102 Streptomyces fradiae
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.1.101
-
Streptomyces fradiae
2.1.1.102
-
Streptomyces fradiae

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.1.1.102 0.25
-
-
Streptomyces fradiae

Storage Stability

EC Number Storage Stability Organism
2.1.1.101 4°C, quite stable in presence of 0.2 mM S-adenosyl-L-methionine and 10% ethanol, pH 7.0, stable over 6 months Streptomyces fradiae
2.1.1.102 4°C, quite stable in presence of S-adenosylmethionine and 10% ethanol, pH 7.0-8.0, stable for a minimum of 2 months Streptomyces fradiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.101 S-adenosyl-L-methionine + lactenocin
-
Streptomyces fradiae S-adenosyl-L-homocysteine + desmycosin
-
?
2.1.1.101 S-adenosyl-L-methionine + macrocin
-
Streptomyces fradiae S-adenosyl-L-homocysteine + tylosin
-
?
2.1.1.101 S-adenosyl-L-methionine + macrocin enzyme catalyzes 3'''-O-methylation of bound 2'''-O-methylated 6-deoxy-D-allose Streptomyces fradiae S-adenosylhomocysteine + tylosin
-
?
2.1.1.102 S-adenosyl-L-methionine + demethyllactenocin
-
Streptomyces fradiae S-adenosyl-L-homocysteine + lactenocin
-
?
2.1.1.102 S-adenosyl-L-methionine + demethylmacrocin
-
Streptomyces fradiae S-adenosyl-L-homocysteine + macrocin
-
?
2.1.1.102 S-adenosyl-L-methionine + demethylmacrocin enzyme catalyzes 2'''-O-methylation of bound 6-deoxy-D-allose Streptomyces fradiae S-adenosyl-L-homocysteine + macrocin
-
?
2.1.1.102 S-adenosyl-L-methionine + demethylmacrocin penultimate step in tylosin biosynthesis Streptomyces fradiae S-adenosyl-L-homocysteine + macrocin
-
?

Subunits

EC Number Subunits Comment Organism
2.1.1.101 dimer 2 * 32000, SDS-PAGE Streptomyces fradiae
2.1.1.102 trimer 3 * 42000, SDS-PAGE Streptomyces fradiae

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.1.1.101 31
-
-
Streptomyces fradiae
2.1.1.102 42
-
-
Streptomyces fradiae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.1.1.101 7.8 8
-
Streptomyces fradiae
2.1.1.102 7.8 8.5
-
Streptomyces fradiae

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.1.1.101 0.00006
-
sinefungin
-
Streptomyces fradiae
2.1.1.102 0.022
-
lactenocin fixed substrate demethylmacrocin Streptomyces fradiae
2.1.1.102 0.024
-
lactenocin fixed substrate S-adenosylmethionine Streptomyces fradiae
2.1.1.102 0.037
-
macrocin fixed substrate S-adenosylmethionine Streptomyces fradiae
2.1.1.102 0.057
-
A9145C fixed substrate demethylmacrocin Streptomyces fradiae
2.1.1.102 0.065
-
mycaminosyltylonolide
-
Streptomyces fradiae
2.1.1.102 0.067
-
macrocin fixed substrate demethyllactenocin Streptomyces fradiae
2.1.1.102 0.073
-
23-Deoxy-O-mycaminosyltylonolide
-
Streptomyces fradiae
2.1.1.102 0.077
-
sinefungin
-
Streptomyces fradiae
2.1.1.102 0.108
-
A9145C fixed substrate S-adenosylmethionine Streptomyces fradiae
2.1.1.102 0.11
-
S-adenosyl-L-homocysteine fixed substrate demethylmacrocin Streptomyces fradiae
2.1.1.102 0.186
-
23-demycinosyloxytylosin
-
Streptomyces fradiae
2.1.1.102 0.226
-
S-adenosyl-L-homocysteine fixed substrate S-adenosylmethionine Streptomyces fradiae