2.1.1.235: dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose N,N-dimethyltransferase

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For detailed information about dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose N,N-dimethyltransferase, go to the full flat file.

Reaction

2 S-adenosyl-L-methionine +

Synonyms

deoxyamino sugar methyltransferase, N-methyltransferase, TylM1

ECTree

     2 Transferases

         2.1 Transferring one-carbon groups

             2.1.1 Methyltransferases

                2.1.1.235 dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose N,N-dimethyltransferase

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Results	in table
90	AA Sequence
1	Application
3	Cloned(Commentary)
3	Cofactor
3	Crystallization (Commentary)
6	General Information
4	General Stability
8	kcat/KM [mM/s]
10	KM Value [mM]
1	Metals/Ions
4	Molecular Weight [Da]
5	Natural Substrates/ Products (Substrates)
5	Organism
4	Pathway
12	PDB ID
2	pH Optimum
4	Protein Variants
2	Purification (Commentary)
1	Reaction
5	Reference
1	Storage Stability
11	Substrates and Products (Substrate)
3	Subunits
6	Synonyms
1	Systematic Name
3	Temperature Optimum [°C]
9	Turnover Number [1/s]

Engineering

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Engineering on EC 2.1.1.235 - dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose N,N-dimethyltransferase

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PROTEIN VARIANTS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

H123A

Streptomyces fradiae

P95748

mutant protein retains catalytic activity, the kcat/Km is reduced to 1.8% compared to the wild-type enzyme

714271

H123N

Streptomyces fradiae

P95748

mutant protein retains catalytic activity, the kcat/Km is reduced to 0.37% compared to the wild-type enzyme

714271

S120A

Streptomyces fradiae

P95748

site-directed mutagenesis, the mutant exhibits a modest decrease in its catalytic efficiency compared to wild-type

756061

Y14F

Streptomyces fradiae

P95748

site-directed mutagenesis, the mutation results in an approximately 30fold decrease in catalytic efficiency compared to wild-type

756061