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show all sequences of 2.1.1.101

Two distinctive O-methyltransferases catalyzing penultimate and terminal reactions of macrolide antibiotic (tylosin) biosynthesis. Substrate specificity, enzyme inhibition, and kinetic mechanism

Kreuzman, A.J.; Turner, J.R.; Yeh, W.K.; J. Biol. Chem. 263, 15626-15633 (1988)

Data extracted from this reference:

Application
Application
Commentary
Organism
pharmacology
tylosin fermentation, antibiotic biosynthesis, enzyme catalyzes conversion of macrocin to tylosin in vivo
Streptomyces fradiae
Inhibitors
Inhibitors
Commentary
Organism
Structure
A9145C
-
Streptomyces fradiae
demethyllactenocin
-
Streptomyces fradiae
Demethylmacrocin
-
Streptomyces fradiae
Desmycosin
weak inhibition
Streptomyces fradiae
Relomycin
weak inhibition
Streptomyces fradiae
S-adenosyl-L-homocysteine
not D-enantiomer
Streptomyces fradiae
sinefungin
competitive inhibition, potent inhibitor
Streptomyces fradiae
tylosin
weak inhibition
Streptomyces fradiae
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.005
-
macrocin
-
Streptomyces fradiae
0.007
-
lactenocin
-
Streptomyces fradiae
0.022
-
S-adenosyl-L-methionine
lactenocin as substrate
Streptomyces fradiae
0.023
-
S-adenosyl-L-methionine
macrocin as substrate
Streptomyces fradiae
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Co2+
can substitute Mg2+
Streptomyces fradiae
Mg2+
required for maximal activity
Streptomyces fradiae
Mn2+
can substitute Mg2+
Streptomyces fradiae
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
32000
-
2 * 32000, SDS-PAGE
Streptomyces fradiae
65000
-
-
Streptomyces fradiae
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
S-adenosyl-L-methionine + macrocin
Streptomyces fradiae
enzyme catalyzes 3'''-O-methylation of bound 2'''-O-methylated 6-deoxy-D-allose
S-adenosylhomocysteine + tylosin
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Streptomyces fradiae
-
-
-
Purification (Commentary)
Commentary
Organism
-
Streptomyces fradiae
Storage Stability
Storage Stability
Organism
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
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
S-adenosyl-L-methionine + lactenocin
-
485050
Streptomyces fradiae
S-adenosyl-L-homocysteine + desmycosin
-
-
-
-
S-adenosyl-L-methionine + macrocin
-
485050
Streptomyces fradiae
S-adenosyl-L-homocysteine + tylosin
-
-
-
?
S-adenosyl-L-methionine + macrocin
enzyme catalyzes 3'''-O-methylation of bound 2'''-O-methylated 6-deoxy-D-allose
485050
Streptomyces fradiae
S-adenosylhomocysteine + tylosin
-
-
-
?
Subunits
Subunits
Commentary
Organism
dimer
2 * 32000, SDS-PAGE
Streptomyces fradiae
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
31
-
-
Streptomyces fradiae
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.8
8
-
Streptomyces fradiae
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.00006
-
sinefungin
-
Streptomyces fradiae
Application (protein specific)
Application
Commentary
Organism
pharmacology
tylosin fermentation, antibiotic biosynthesis, enzyme catalyzes conversion of macrocin to tylosin in vivo
Streptomyces fradiae
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
A9145C
-
Streptomyces fradiae
demethyllactenocin
-
Streptomyces fradiae
Demethylmacrocin
-
Streptomyces fradiae
Desmycosin
weak inhibition
Streptomyces fradiae
Relomycin
weak inhibition
Streptomyces fradiae
S-adenosyl-L-homocysteine
not D-enantiomer
Streptomyces fradiae
sinefungin
competitive inhibition, potent inhibitor
Streptomyces fradiae
tylosin
weak inhibition
Streptomyces fradiae
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.00006
-
sinefungin
-
Streptomyces fradiae
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.005
-
macrocin
-
Streptomyces fradiae
0.007
-
lactenocin
-
Streptomyces fradiae
0.022
-
S-adenosyl-L-methionine
lactenocin as substrate
Streptomyces fradiae
0.023
-
S-adenosyl-L-methionine
macrocin as substrate
Streptomyces fradiae
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Co2+
can substitute Mg2+
Streptomyces fradiae
Mg2+
required for maximal activity
Streptomyces fradiae
Mn2+
can substitute Mg2+
Streptomyces fradiae
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
32000
-
2 * 32000, SDS-PAGE
Streptomyces fradiae
65000
-
-
Streptomyces fradiae
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
S-adenosyl-L-methionine + macrocin
Streptomyces fradiae
enzyme catalyzes 3'''-O-methylation of bound 2'''-O-methylated 6-deoxy-D-allose
S-adenosylhomocysteine + tylosin
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
-
Streptomyces fradiae
Storage Stability (protein specific)
Storage Stability
Organism
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
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
S-adenosyl-L-methionine + lactenocin
-
485050
Streptomyces fradiae
S-adenosyl-L-homocysteine + desmycosin
-
-
-
-
S-adenosyl-L-methionine + macrocin
-
485050
Streptomyces fradiae
S-adenosyl-L-homocysteine + tylosin
-
-
-
?
S-adenosyl-L-methionine + macrocin
enzyme catalyzes 3'''-O-methylation of bound 2'''-O-methylated 6-deoxy-D-allose
485050
Streptomyces fradiae
S-adenosylhomocysteine + tylosin
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
2 * 32000, SDS-PAGE
Streptomyces fradiae
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
31
-
-
Streptomyces fradiae
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.8
8
-
Streptomyces fradiae
Other publictions for EC 2.1.1.101
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
485048
Bauer
Purification, characterization ...
Streptomyces fradiae
J. Biol. Chem.
263
15619-15625
1988
-
2
-
-
-
-
7
-
-
3
2
1
-
2
-
-
1
-
-
-
1
1
6
1
1
-
-
-
1
-
-
-
10
-
-
-
2
-
-
-
-
-
-
7
10
-
-
3
2
1
-
-
-
1
-
-
1
1
6
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
485050
Kreuzman
Two distinctive O-methyltransf ...
Streptomyces fradiae
J. Biol. Chem.
263
15626-15633
1988
-
1
-
-
-
-
8
4
-
3
2
1
-
2
-
-
1
-
-
-
-
1
3
1
1
-
-
-
1
-
-
-
1
-
-
-
1
-
-
-
-
-
-
8
1
4
-
3
2
1
-
-
-
1
-
-
-
1
3
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
485049
Yeh
High-performance liquid chroma ...
Streptomyces fradiae
J. Chromatogr.
288
157-165
1984
-
-
-
-
-
-
1
2
-
5
-
1
-
2
-
-
-
-
-
-
-
2
2
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
2
-
5
-
1
-
-
-
-
-
-
-
2
2
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
485047
Seno
Properties of S-adenosyl-L-met ...
Streptomyces fradiae
Antimicrob. Agents Chemother.
20
370-377
1981
-
-
-
-
-
-
2
-
-
1
-
1
-
2
-
-
-
-
-
-
-
-
2
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
1
-
1
-
-
-
-
-
-
-
-
2
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-