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Literature summary extracted from

  • Wennerstrand, P.; Dametto, P.; Hennig, J.; Klingstedt, T.; Skoglund, K.; Lindqvist Appell, M.; Martensson, L.G.
    Structural characteristics determine the cause of the low enzyme activity of two thiopurine S-methyltransferase allelic variants: a biophysical characterization of TPMT*2 and TPMT*5 (2012), Biochemistry, 51, 5912-5920.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.1.67 expressed in Escherichia coli BL21-Codon Plus (DE3)-RIL cells Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
2.1.1.67 A80P the mutant is substantially destabilized and shows 47% of wild type activity Homo sapiens
2.1.1.67 L49S the mutant shows much greater stability comparable to that of wild type enzyme and exhibits 14% of wild type activity Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.67 Homo sapiens
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.1.67 Ni-NTA column chromatography and Superdex 200 gel filtration Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.67 S-adenosyl-L-methionine + 6-mercaptopurine
-
 Homo sapiens S-adenosyl-L-homocysteine + 6-methylmercaptopurine
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.1.1.67 TPMT
-
 Homo sapiens

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.1.1.67 55
-
 the melting temperature of the wild type enzyme is at 55°C Homo sapiens