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Literature summary for 2.1.1.95 extracted from

  • Tewari, K.; Dahuja, A.; Sachdev, A.; Kumar, V.; Ali, K.; Kumar, A.; Kumari, S.
    Molecular cloning, heterologous expression and functional characterization of gamma tocopherol methyl transferase (gamma-TMT) from Glycine max (2017), Protein Expr. Purif., 140, 81-89 .
    View publication on PubMed
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Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Glycine max

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
S-adenosyl-L-methionine + gamma-tocopherol Glycine max
-
 S-adenosyl-L-homocysteine + alpha-tocopherol
-
 ?

Organism

Organism UniProt Comment Textmining
Glycine max
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA column chromatography Glycine max

Source Tissue

Source Tissue Comment Organism Textmining
seed
-
 Glycine max
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + gamma-tocopherol
-
 Glycine max S-adenosyl-L-homocysteine + alpha-tocopherol
-
 ?

Subunits

Subunits Comment Organism
? x * 33300, native enzyme, calculated from amino acid sequence Glycine max
? x * 37900, His6-tagged recombinant enzyme, SDS-PAGE Glycine max

Synonyms

Synonyms Comment Organism
gamma tocopherol methyl transferase
-
 Glycine max
gamma-TMT
-
 Glycine max

pI Value

Organism Comment pI Value Maximum pI Value
Glycine max native enzyme, calculated from amino acid sequence
-
 6.4