Literature summary for 2.1.1.67 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.

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Cloned(Commentary)

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

Protein Variants

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

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Synonyms

Synonyms	Comment	Organism
TPMT	-	Homo sapiens

Temperature Stability [°C]

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

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Release 2023.1 (January 2023)