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show all sequences of 2.1.1.236

Production of a novel N-monomethylated dideoxysugar

Thoden, J.B.; Holden, H.M.; Biochemistry 53, 1105-1107 (2014)

Data extracted from this reference:

Crystallization (Commentary)
Crystallization
Organism
enzyme in complex with S-adenosyl-L-homocysteine and dTDP-3-N-methylamino-3,6-dideoxygalactose., X-ray diffraction structure determination and analysis at 2.2 A resolution
Streptomyces fradiae
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.54
-
dTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose
pH and temperature not specified in the publication
Streptomyces fradiae
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2 S-adenosyl-L-methionine + dTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose
Streptomyces fradiae
-
2 S-adenosyl-L-homocysteine + dTDP-3-dimethylamino-3,6-dideoxy-alpha-D-galactopyranose
-
-
?
additional information
Streptomyces fradiae
the enzyme also catalyzes the methylation of dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose, EC 2.1.1.235
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Streptomyces fradiae
P95748
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2 S-adenosyl-L-methionine + dTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose
-
735676
Streptomyces fradiae
2 S-adenosyl-L-homocysteine + dTDP-3-dimethylamino-3,6-dideoxy-alpha-D-galactopyranose
-
-
-
?
2 S-adenosyl-L-methionine + dTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose
-
735676
Streptomyces fradiae
2 S-adenosyl-L-homocysteine + dTDP-3-dimethylamino-3,6-dideoxy-alpha-D-galactopyranose
analysis of the binding structure of the dTDP-sugar in enzyme TylM1 active site, overview. Only a water molecule is expelled from the active site to accommodate one of the methyl substituents on the C-3' amino group
-
-
?
additional information
the enzyme also catalyzes the methylation of dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose, EC 2.1.1.235
735676
Streptomyces fradiae
?
-
-
-
-
additional information
modeling of substrate binding
735676
Streptomyces fradiae
?
-
-
-
-
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.61
-
dTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose
pH and temperature not specified in the publication
Streptomyces fradiae
Cofactor
Cofactor
Commentary
Organism
Structure
S-adenosyl-L-methionine
-
Streptomyces fradiae
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
S-adenosyl-L-methionine
-
Streptomyces fradiae
Crystallization (Commentary) (protein specific)
Crystallization
Organism
enzyme in complex with S-adenosyl-L-homocysteine and dTDP-3-N-methylamino-3,6-dideoxygalactose., X-ray diffraction structure determination and analysis at 2.2 A resolution
Streptomyces fradiae
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.54
-
dTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose
pH and temperature not specified in the publication
Streptomyces fradiae
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2 S-adenosyl-L-methionine + dTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose
Streptomyces fradiae
-
2 S-adenosyl-L-homocysteine + dTDP-3-dimethylamino-3,6-dideoxy-alpha-D-galactopyranose
-
-
?
additional information
Streptomyces fradiae
the enzyme also catalyzes the methylation of dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose, EC 2.1.1.235
?
-
-
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2 S-adenosyl-L-methionine + dTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose
-
735676
Streptomyces fradiae
2 S-adenosyl-L-homocysteine + dTDP-3-dimethylamino-3,6-dideoxy-alpha-D-galactopyranose
-
-
-
?
2 S-adenosyl-L-methionine + dTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose
-
735676
Streptomyces fradiae
2 S-adenosyl-L-homocysteine + dTDP-3-dimethylamino-3,6-dideoxy-alpha-D-galactopyranose
analysis of the binding structure of the dTDP-sugar in enzyme TylM1 active site, overview. Only a water molecule is expelled from the active site to accommodate one of the methyl substituents on the C-3' amino group
-
-
?
additional information
the enzyme also catalyzes the methylation of dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose, EC 2.1.1.235
735676
Streptomyces fradiae
?
-
-
-
-
additional information
modeling of substrate binding
735676
Streptomyces fradiae
?
-
-
-
-
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.61
-
dTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose
pH and temperature not specified in the publication
Streptomyces fradiae
General Information
General Information
Commentary
Organism
additional information
structure model of TylM1 with bound S-adenosyl-L-methionine and dTDP-phenol: Model of the Michaelis complex in stereo. The C-3' amino group is positioned to attack the methyl group of S-adenoyl-L-methionine. dTDP-mycaminose binding pocket structure, overview
Streptomyces fradiae
physiological function
enzyme TylM1 is a dimethyltransferase from Streptomyces fradiae involved in the production of dTDP-mycaminose
Streptomyces fradiae
General Information (protein specific)
General Information
Commentary
Organism
additional information
structure model of TylM1 with bound S-adenosyl-L-methionine and dTDP-phenol: Model of the Michaelis complex in stereo. The C-3' amino group is positioned to attack the methyl group of S-adenoyl-L-methionine. dTDP-mycaminose binding pocket structure, overview
Streptomyces fradiae
physiological function
enzyme TylM1 is a dimethyltransferase from Streptomyces fradiae involved in the production of dTDP-mycaminose
Streptomyces fradiae
Other publictions for EC 2.1.1.236
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)
735676
Thoden
Production of a novel N-monome ...
Streptomyces fradiae
Biochemistry
53
1105-1107
2014
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2
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716410
Kharel
Characterization of the TDP-D- ...
Streptomyces ravidus
Org. Biomol. Chem.
9
1799-1808
2011
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