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S-(5'-adenosyl)-L-methionine-d3 disulfate salt + 6-mercaptopurine
S-adenosyl-L-homocysteine + 6-(d3-methyl)mercaptopurine
-
-
-
-
?
S-adenosyl-L-methionine + 2,8-dihydroxy-6-thiopurine
S-adenosyl-L-homocysteine + 2,8-dihydroxy-6-methylthiopurine
S-adenosyl-L-methionine + 2-amino-6-thiopurine
S-adenosyl-L-homocysteine + 2-amino-6-methylthiopurine
S-adenosyl-L-methionine + 2-aminothiophenol
S-adenosyl-L-homocysteine + 2-methylsulfanylphenylamine
-
-
-
-
?
S-adenosyl-L-methionine + 2-bromothiophenol
S-adenosyl-L-homocysteine + 1-bromo-2-methylsulfanylbenzene
-
-
-
-
?
S-adenosyl-L-methionine + 2-mercaptoethanol
S-adenosyl-L-homocysteine + 2-methylmercaptoethanol
-
-
-
-
?
S-adenosyl-L-methionine + 2-methoxythiophenol
S-adenosyl-L-homocysteine + 1-methoxy-2-methylsulfanylbenzene
-
-
-
-
?
S-adenosyl-L-methionine + 2-thiothymine
S-adenosyl-L-homocysteine + 2-methylthiothymine
S-adenosyl-L-methionine + 2-thiouracil
S-adenosyl-L-homocysteine + thiouracil-2-S-methylether
S-adenosyl-L-methionine + 3-methoxythiophenol
S-adenosyl-L-homocysteine + 1-methylsulfanyl-3-methoxybenzene
-
-
-
-
?
S-adenosyl-L-methionine + 4-(aminomethoxy)thiophenol
S-adenosyl-L-homocysteine + 1-aminomethoxy-4-methylsulfanylbenzene
-
-
-
-
?
S-adenosyl-L-methionine + 4-bromothiophenol
S-adenosyl-L-homocysteine + 1-bromo-4-methylsulfanylbenzene
-
-
-
-
?
S-adenosyl-L-methionine + 4-chlorothiophenol
S-adenosyl-L-homocysteine + 1-chloro-4-methylsulfanylbenzene
-
-
-
-
?
S-adenosyl-L-methionine + 4-fluorothiophenol
S-adenosyl-L-homocysteine + 1-fluoro-4-methylsulfanylbenzene
-
-
-
-
?
S-adenosyl-L-methionine + 4-methoxythiophenol
S-adenosyl-L-homocysteine + 1-methoxy-4-methylsulfanylbenzene
-
-
-
-
?
S-adenosyl-L-methionine + 4-methylthiophenol
S-adenosyl-L-homocysteine + 1-methyl-4-methylsulfanylbenzene
-
-
-
-
?
S-adenosyl-L-methionine + 4-nitrothiophenol
S-adenosyl-L-homocysteine + 1-methylsulfanyl-4-nitrobenzene
-
-
-
-
?
S-adenosyl-L-methionine + 4-thiobenzoate
S-adenosyl-L-homocysteine + 4-methylsulfanyl benzoate
-
-
-
-
?
S-adenosyl-L-methionine + 6-hydroxy-8-mercaptopurine
S-adenosyl-L-homocysteine + 6-hydroxy-8-methylmercaptopurine
-
-
-
-
?
S-adenosyl-L-methionine + 6-mercaptopurine
?
-
-
-
-
?
S-adenosyl-L-methionine + 6-mercaptopurine
S-adenosyl-L-homocysteine + 6-methylmercaptopurine
S-adenosyl-L-methionine + 6-mercaptopurine nucleoside
S-adenosyl-L-homocysteine + 6-methylmercaptopurine nucleoside
-
inactivation
-
-
?
S-adenosyl-L-methionine + 6-mercaptopurine-riboside
S-adenosyl-L-homocysteine + 6-methylmercaptopurine-riboside
-
-
-
-
?
S-adenosyl-L-methionine + 6-mercaptopurine-riboside-5'-monophosphate
S-adenosyl-L-homocysteine + 6-methylmercaptopurine-riboside-5'-monophosphate
-
-
-
-
?
S-adenosyl-L-methionine + 6-mercaptopurine-riboside-5'-triphosphate
S-adenosyl-L-homocysteine + 6-methylmercaptopurine-riboside-5'-triphosphate
-
-
-
-
?
S-adenosyl-L-methionine + 6-selenoguanine-riboside
S-adenosyl-L-homocysteine + 6-methylselenoguanine-riboside
-
-
-
-
?
S-adenosyl-L-methionine + 6-selenopurine
S-adenosyl-L-homocysteine + 6-methylselenopurine
-
-
-
-
?
S-adenosyl-L-methionine + 6-selenopurine-riboside
S-adenosyl-L-homocysteine + 6-methylselenopurine-riboside
-
-
-
-
?
S-adenosyl-L-methionine + 6-thiodeoxyguanosine
S-adenosyl-L-homocysteine + 6-thiodeoxyguanosine S-methylether
-
-
-
-
r
S-adenosyl-L-methionine + 6-thiodeoxyguanosine monophosphate
S-adenosyl-L-homocysteine + 6-methylthiodeoxyguanosine monophosphate
-
-
-
-
?
S-adenosyl-L-methionine + 6-thiodeoxyinosine
S-adenosyl-L-homocysteine + 6-thiodeoxyinosine S-methylether
-
-
-
-
r
S-adenosyl-L-methionine + 6-thiodeoxyinosine monophosphate
S-adenosyl-L-homocysteine + 6-methyl thiodeoxyinosine monophosphate
-
-
-
-
?
S-adenosyl-L-methionine + 6-thioguanine
?
-
-
-
-
?
S-adenosyl-L-methionine + 6-thioguanine
S-adenosyl-L-homocysteine + 6-methylthioguanine
S-adenosyl-L-methionine + 6-thioguanine monophosphate
S-adenosyl-L-homocysteine + 6-methylthioguanine monophosphate
-
-
-
-
?
S-adenosyl-L-methionine + 6-thioguanine-riboside
S-adenosyl-L-homocysteine + 6-methylthioguanine-riboside
-
-
-
-
?
S-adenosyl-L-methionine + 6-thioguanine-riboside-5'-monophosphate
S-adenosyl-L-homocysteine + 6-methylthioguanine-riboside-5'-monophosphate
-
-
-
-
?
S-adenosyl-L-methionine + 6-thioguanosine monophosphate
S-adenosyl-L-homocysteine + 6-methyl thioguanosine monophosphate
-
-
-
-
?
S-adenosyl-L-methionine + 6-thioinosine
S-adenosyl-L-homocysteine + 6-methylmercaptopurine riboside
S-adenosyl-L-methionine + 6-thioinosine 5'-monophosphate
S-adenosyl-L-homocysteine + 6-methylmercaptopurine ribonucleotide
-
-
-
-
?
S-adenosyl-L-methionine + 6-thioinosine diphosphate
S-adenosyl-L-homocysteine + 6-methylthioinosine diphosphate
-
-
-
-
?
S-adenosyl-L-methionine + 6-thioinosine monophosphate
S-adenosyl-L-homocysteine + 6-methyl thioinosine monophosphate
-
-
-
-
?
S-adenosyl-L-methionine + 6-thioinosine monophosphate
S-adenosyl-L-homocysteine + 6-methylthioinosine monophosphate
-
-
-
-
?
S-adenosyl-L-methionine + 6-thioinosine triphosphate
S-adenosyl-L-homocysteine + 6-methylthioinosine triphosphate
-
-
-
-
?
S-adenosyl-L-methionine + 6-thioinosine-monophosphate
S-adenosyl-L-homocysteine + 6-methylmercaptopurine-ribonucleotide
-
-
consisting of 6-methyl-thioinosine-monophosphate, -diphosphate and triphosphate
-
?
S-adenosyl-L-methionine + 6-thioinosine-monophosphate
S-adenosyl-L-homocysteine + 6-methylthioinosine-monophosphate
-
-
-
-
?
S-adenosyl-L-methionine + 6-thiopurine
S-adenosyl-L-homocysteine + 6-methylthiopurine
S-adenosyl-L-methionine + 6-thiouric acid
S-adenosyl-L-homocysteine + 6-methylthiouric acid
S-adenosyl-L-methionine + 7-methyl-6-mercaptopurine
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + 8-hydroxy-6-mercaptopurine
S-adenosyl-L-homocysteine + 8-hydroxy-6-methylmercaptopurine
-
-
-
-
?
S-adenosyl-L-methionine + 9(n-propyl)6-thioguanine
S-adenosyl-L-homocysteine + 9(n-propyl)6-methylthioguanine
-
-
-
-
?
S-adenosyl-L-methionine + 9-(n-butyl)-6-mercaptopurine
S-adenosyl-L-homocysteine + 9-(n-butyl)-6-methylmercaptopurine
-
-
-
-
?
S-adenosyl-L-methionine + 9-ethyl-6-mercaptopurine
S-adenosyl-L-homocysteine + 9-ethyl-6-methylmercaptopurine
-
-
-
-
?
S-adenosyl-L-methionine + a thiopurine
S-adenosyl-L-homocysteine + a thiopurine S-methylether
S-adenosyl-L-methionine + azathioprine
?
S-adenosyl-L-methionine + azathioprine
S-adenosyl-L-homocysteine + 6-methylmercaptopurine + ?
S-adenosyl-L-methionine + azathioprine
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + mercaptopurine
S-adenosyl-L-homocysteine + methylmercaptopurine
-
-
-
-
?
S-adenosyl-L-methionine + thioguanine nucleotide
S-adenosyl-L-homocysteine + methylthioguanine
S-adenosyl-L-methionine + thioinosine monophosphate
S-adenosyl-L-homocysteine + methylthioinosine monophosphate
S-adenosyl-L-methionine + thioinosine triphosphate
S-adenosyl-L-homocysteine + methylthioinosine triphosphate
-
-
-
-
?
S-adenosyl-L-methionine + thiopurine
S-adenosyl-L-homocysteine + methylthiopurine
-
-
-
-
?
additional information
?
-
S-adenosyl-L-methionine + 2,8-dihydroxy-6-thiopurine
S-adenosyl-L-homocysteine + 2,8-dihydroxy-6-methylthiopurine
-
-
-
-
?
S-adenosyl-L-methionine + 2,8-dihydroxy-6-thiopurine
S-adenosyl-L-homocysteine + 2,8-dihydroxy-6-methylthiopurine
-
-
-
-
?
S-adenosyl-L-methionine + 2-amino-6-thiopurine
S-adenosyl-L-homocysteine + 2-amino-6-methylthiopurine
-
-
-
-
?
S-adenosyl-L-methionine + 2-amino-6-thiopurine
S-adenosyl-L-homocysteine + 2-amino-6-methylthiopurine
-
-
-
-
?
S-adenosyl-L-methionine + 2-thiothymine
S-adenosyl-L-homocysteine + 2-methylthiothymine
-
-
-
-
?
S-adenosyl-L-methionine + 2-thiothymine
S-adenosyl-L-homocysteine + 2-methylthiothymine
-
-
-
-
?
S-adenosyl-L-methionine + 2-thiothymine
S-adenosyl-L-homocysteine + 2-methylthiothymine
-
-
-
-
?
S-adenosyl-L-methionine + 2-thiouracil
S-adenosyl-L-homocysteine + thiouracil-2-S-methylether
-
-
-
-
?
S-adenosyl-L-methionine + 2-thiouracil
S-adenosyl-L-homocysteine + thiouracil-2-S-methylether
-
-
-
-
?
S-adenosyl-L-methionine + 2-thiouracil
S-adenosyl-L-homocysteine + thiouracil-2-S-methylether
-
-
-
-
?
S-adenosyl-L-methionine + 2-thiouracil
S-adenosyl-L-homocysteine + thiouracil-2-S-methylether
-
-
-
-
?
S-adenosyl-L-methionine + 6-mercaptopurine
S-adenosyl-L-homocysteine + 6-methylmercaptopurine
-
-
-
-
?
S-adenosyl-L-methionine + 6-mercaptopurine
S-adenosyl-L-homocysteine + 6-methylmercaptopurine
-
-
485516, 485520, 485521, 485522, 485524, 485525, 485526, 485527, 485528, 485529, 657544, 684266, 685852, 686157, 686161, 686184, 686189, 686326, 686328, 686351, 686505, 686507, 686574, 687982, 687983, 688126, 688415, 688777, 689358, 689362, 689365, 689368, 689369, 690115, 690118, 702159, 703355, 704818, 706091, 706093, 706816, 718804, 718942, 720181, 720847, 755922, 756145, 756499, 756597, 757309, 757473 -
-
?
S-adenosyl-L-methionine + 6-mercaptopurine
S-adenosyl-L-homocysteine + 6-methylmercaptopurine
-
-
-
?
S-adenosyl-L-methionine + 6-mercaptopurine
S-adenosyl-L-homocysteine + 6-methylmercaptopurine
-
-
-
-
?
S-adenosyl-L-methionine + 6-mercaptopurine
S-adenosyl-L-homocysteine + 6-methylmercaptopurine
-
-
-
?
S-adenosyl-L-methionine + 6-mercaptopurine
S-adenosyl-L-homocysteine + 6-methylmercaptopurine
-
-
-
-
?
S-adenosyl-L-methionine + 6-mercaptopurine
S-adenosyl-L-homocysteine + 6-methylmercaptopurine
-
-
-
?
S-adenosyl-L-methionine + 6-mercaptopurine
S-adenosyl-L-homocysteine + 6-methylmercaptopurine
-
-
-
-
?
S-adenosyl-L-methionine + 6-mercaptopurine
S-adenosyl-L-homocysteine + 6-methylmercaptopurine
-
-
-
?
S-adenosyl-L-methionine + 6-mercaptopurine
S-adenosyl-L-homocysteine + 6-methylmercaptopurine
-
immunosuppressant medication
-
-
?
S-adenosyl-L-methionine + 6-mercaptopurine
S-adenosyl-L-homocysteine + 6-methylmercaptopurine
-
inactivation
-
-
?
S-adenosyl-L-methionine + 6-mercaptopurine
S-adenosyl-L-homocysteine + 6-methylmercaptopurine
-
azathioprine is converted via a non-enzymatic reaction to mercaptopurine, which is subsequently metabolized through TPMT
-
-
?
S-adenosyl-L-methionine + 6-mercaptopurine
S-adenosyl-L-homocysteine + 6-methylmercaptopurine
-
TPMT deactivates 6-mercaptopurine by methylation
-
-
?
S-adenosyl-L-methionine + 6-mercaptopurine
S-adenosyl-L-homocysteine + 6-methylmercaptopurine
-
-
-
-
?
S-adenosyl-L-methionine + 6-mercaptopurine
S-adenosyl-L-homocysteine + 6-methylmercaptopurine
-
-
-
-
?
S-adenosyl-L-methionine + 6-mercaptopurine
S-adenosyl-L-homocysteine + 6-methylmercaptopurine
-
-
-
?
S-adenosyl-L-methionine + 6-mercaptopurine
S-adenosyl-L-homocysteine + 6-methylmercaptopurine
-
-
-
-
?
S-adenosyl-L-methionine + 6-thioguanine
S-adenosyl-L-homocysteine + 6-methylthioguanine
-
-
485516, 485519, 485520, 485521, 485522, 485523, 485526, 485527, 485528, 485529, 657749, 658654, 659566, 685852, 686161, 686189, 686351, 686505, 688415, 689358, 689365, 689369, 690115, 701941, 703564, 756145, 756597, 757473 -
-
?
S-adenosyl-L-methionine + 6-thioguanine
S-adenosyl-L-homocysteine + 6-methylthioguanine
-
-
-
?
S-adenosyl-L-methionine + 6-thioguanine
S-adenosyl-L-homocysteine + 6-methylthioguanine
-
-
-
-
?
S-adenosyl-L-methionine + 6-thioguanine
S-adenosyl-L-homocysteine + 6-methylthioguanine
-
-
-
-
?
S-adenosyl-L-methionine + 6-thioguanine
S-adenosyl-L-homocysteine + 6-methylthioguanine
-
-
-
-
?
S-adenosyl-L-methionine + 6-thioguanine
S-adenosyl-L-homocysteine + 6-methylthioguanine
-
-
-
?
S-adenosyl-L-methionine + 6-thioguanine
S-adenosyl-L-homocysteine + 6-methylthioguanine
-
-
-
-
?
S-adenosyl-L-methionine + 6-thioguanine
S-adenosyl-L-homocysteine + 6-methylthioguanine
-
-
-
-
?
S-adenosyl-L-methionine + 6-thioinosine
S-adenosyl-L-homocysteine + 6-methylmercaptopurine riboside
-
-
-
-
?
S-adenosyl-L-methionine + 6-thioinosine
S-adenosyl-L-homocysteine + 6-methylmercaptopurine riboside
-
-
-
-
?
S-adenosyl-L-methionine + 6-thiopurine
S-adenosyl-L-homocysteine + 6-methylthiopurine
-
-
-
-
?
S-adenosyl-L-methionine + 6-thiopurine
S-adenosyl-L-homocysteine + 6-methylthiopurine
-
preferred substrate
-
-
?
S-adenosyl-L-methionine + 6-thiopurine
S-adenosyl-L-homocysteine + 6-methylthiopurine
-
preferred substrate
-
-
?
S-adenosyl-L-methionine + 6-thiopurine
S-adenosyl-L-homocysteine + 6-methylthiopurine
-
-
-
-
?
S-adenosyl-L-methionine + 6-thiopurine
S-adenosyl-L-homocysteine + 6-methylthiopurine
-
preferred substrate
-
-
?
S-adenosyl-L-methionine + 6-thiouric acid
S-adenosyl-L-homocysteine + 6-methylthiouric acid
-
-
-
-
?
S-adenosyl-L-methionine + 6-thiouric acid
S-adenosyl-L-homocysteine + 6-methylthiouric acid
-
-
-
-
?
S-adenosyl-L-methionine + a thiopurine
S-adenosyl-L-homocysteine + a thiopurine S-methylether
-
-
485516, 485518, 485519, 485520, 485521, 485522, 485523, 485524, 485525, 485526, 485527, 485528, 485529, 684265, 684266, 684267, 684275, 684276, 684279, 684733, 685037, 685852, 686157, 686161, 686167, 686184, 686189, 686326, 686328, 686351, 686503, 686505, 686507, 686574, 687195, 687982, 687983, 688415, 688777, 688807, 689358, 689362, 689365, 689368, 689369, 690115, 690118, 756597, 757473 -
-
?
S-adenosyl-L-methionine + a thiopurine
S-adenosyl-L-homocysteine + a thiopurine S-methylether
-
-
-
?
S-adenosyl-L-methionine + a thiopurine
S-adenosyl-L-homocysteine + a thiopurine S-methylether
-
-
-
-
?
S-adenosyl-L-methionine + a thiopurine
S-adenosyl-L-homocysteine + a thiopurine S-methylether
-
-
-
?
S-adenosyl-L-methionine + a thiopurine
S-adenosyl-L-homocysteine + a thiopurine S-methylether
-
enzyme plays an important role in metabolism of heterocyclic sulfhydryl drugs such as 6-thiopurine and 6-thioguanine
-
-
?
S-adenosyl-L-methionine + a thiopurine
S-adenosyl-L-homocysteine + a thiopurine S-methylether
-
S-methylation, enzyme of major catabolic pathway of thiopurines
-
-
?
S-adenosyl-L-methionine + a thiopurine
S-adenosyl-L-homocysteine + a thiopurine S-methylether
-
-
-
-
?
S-adenosyl-L-methionine + a thiopurine
S-adenosyl-L-homocysteine + a thiopurine S-methylether
-
-
-
-
?
S-adenosyl-L-methionine + a thiopurine
S-adenosyl-L-homocysteine + a thiopurine S-methylether
-
-
-
?
S-adenosyl-L-methionine + a thiopurine
S-adenosyl-L-homocysteine + a thiopurine S-methylether
-
specific for S-adenosyl-L-methionine
-
-
?
S-adenosyl-L-methionine + a thiopurine
S-adenosyl-L-homocysteine + a thiopurine S-methylether
-
specific for S-adenosyl-L-methionine
-
-
?
S-adenosyl-L-methionine + a thiopurine
S-adenosyl-L-homocysteine + a thiopurine S-methylether
-
-
-
-
?
S-adenosyl-L-methionine + a thiopurine
S-adenosyl-L-homocysteine + a thiopurine S-methylether
-
specific for S-adenosyl-L-methionine
-
-
?
S-adenosyl-L-methionine + azathioprine
?
-
-
-
-
?
S-adenosyl-L-methionine + azathioprine
?
-
-
-
-
?
S-adenosyl-L-methionine + azathioprine
S-adenosyl-L-homocysteine + 6-methylmercaptopurine + ?
-
azathioprine is converted via a non-enzymatic reaction to mercaptopurine, which is subsequently metabolized through TPMT
-
-
?
S-adenosyl-L-methionine + azathioprine
S-adenosyl-L-homocysteine + 6-methylmercaptopurine + ?
-
-
-
-
?
S-adenosyl-L-methionine + azathioprine
S-adenosyl-L-homocysteine + 6-methylmercaptopurine + ?
-
-
-
?
S-adenosyl-L-methionine + azathioprine
S-adenosyl-L-homocysteine + 6-methylmercaptopurine + ?
-
azathioprine is converted via a non-enzymatic reaction to mercaptopurine, which is subsequently metabolized through TPMT
684266, 686161, 686189, 686326, 686574, 688126, 688415, 688777, 689358, 689362, 689368, 690115, 690118 -
-
?
S-adenosyl-L-methionine + azathioprine
S-adenosyl-L-homocysteine + 6-methylmercaptopurine + ?
azathioprine is converted via a non-enzymatic reaction to mercaptopurine, which is subsequently metabolized through TPMT
-
-
?
S-adenosyl-L-methionine + azathioprine
S-adenosyl-L-homocysteine + 6-methylmercaptopurine + ?
-
azathioprine is converted via a non-enzymatic reaction to mercaptopurine, which is subsequently metabolized through TPMT
-
-
?
S-adenosyl-L-methionine + azathioprine
S-adenosyl-L-homocysteine + 6-methylmercaptopurine + ?
-
azathioprine is converted to mercaptopurine, which is subsequently metabolized through TPMT
-
-
?
S-adenosyl-L-methionine + thioguanine nucleotide
S-adenosyl-L-homocysteine + methylthioguanine
-
-
-
-
?
S-adenosyl-L-methionine + thioguanine nucleotide
S-adenosyl-L-homocysteine + methylthioguanine
-
-
-
-
?
S-adenosyl-L-methionine + thioinosine monophosphate
S-adenosyl-L-homocysteine + methylthioinosine monophosphate
-
-
-
-
?
S-adenosyl-L-methionine + thioinosine monophosphate
S-adenosyl-L-homocysteine + methylthioinosine monophosphate
-
-
-
-
?
additional information
?
-
-
aliphatic thiol compounds are poor substrates or not methylated, dithiothreitol is no substrate
-
-
?
additional information
?
-
-
S-adenosyl-L-methionine and sinefungin prevent degradation of TPMT by stabilizing ist native structure
-
-
?
additional information
?
-
-
glutathione is no substrate
-
-
?
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460G>A/719A>G
-
TPMT*3A polymorphism, low or no TPMT activity
A154Y
-
thiopurine S-methyltransferase polymorphism, G to A transition at position 460
A179G/G460A
the variant is associated with low enzyme activity
A180P
-
the mutation affects TMPT activity
C216T
the mutant exhibits reduced activity compared to the wild type enzyme
E98X
-
the mutation affects TMPT activity
F208L
-
the mutation is associated with a decrease in enzyme activity
Q179H
polymorphism c.537G>T, TPMT*24
R152A
mutant to probe, whether this residue is important for catalysis
R152A/R226A
mutant to probe, whether this residue is important for catalysis
R152E
mutant to probe, whether this residue is important for catalysis
R152H
mutant to probe, whether this residue is important for catalysis
R226A
mutant to probe, whether this residue is important for catalysis
R226E
mutant to probe, whether this residue is important for catalysis
R226H
mutant to probe, whether this residue is important for catalysis
TPMT*23
-
polymorphism, single nucleotide substitution, C500G
Y107D
the mutant shows less than 10% activity compared to the wild type enzyme, the variant allozyme shows a striking decrease in both immunoreactive protein level and enzyme activity after transient expression in COS-1 cells, the mutant is less stable than the wild type TPMT allozyme
A154T
-
polymorphism TPMT*3B
A154T/Y240C
-
polymorphism TPMT*3A
A154T/Y240C/E98STOP
-
polymorphism TPMT*3D
A80P
-
polymorphism TPMT*2
C132Y
-
polymorphism TPMT*11
E28V
-
polymorphism TPMT*13
G144R
-
polymorphism TPMT*10
G36S/K238E
-
polymorphism TPMT*20
G71R
-
polymorphism TPMT*18
H227E
-
polymorphism TPMT*7
K122T
-
polymorphism TPMT*19
L49S
-
polymorphism TPMT*5
L69V
-
polymorphism TPMT*21
Q42E
-
polymorphism TPMT*17
R163H
-
polymorphism TPMT*16
R163P
-
polymorphism TPMT*22
R215H
-
polymorphism TPMT*8
S125L
-
polymorphism TPMT*12
Y180F
-
polymorphism TPMT*6
Y240C
-
polymorphism TPMT*3C
238G>C
-
TPMT variant
238G>C
-
TPMT variant, inactivating mutation in exon 5
460G>A
-
TPMT variant
460G>A
-
TPMT variant, inactivating mutation in exon 7
719A>G
-
TPMT variant
719A>G
-
TPMT variant, inactivating mutation in exon 10
A154T
-
460G>A sequence variant of the TPMT gene, location exon 7, amino acid change A154T
A154T
-
polymorphism TPMT*3B
A154T
-
polymorphism TPMT*3B, single nucleotide substitution G460A
A154T
-
variant TPMT*3B, G460A polymorphismus
A154T
-
mutant shows decreased TPMT activity
A154T
-
the mutation affects TMPT activity
A154T/Y240C
-
mutant with reduced activity
A154T/Y240C
-
polymorphism TPMT*3A
A154T/Y240C
-
polymorphism TPMT*3A, single nucleotide substitutions G460A and A719G
A154T/Y240C
-
TPMT*3A polymorphismus
A154T/Y240C
-
variant TPMT*3A
A154T/Y240C
-
mutant shows decreased TPMT activity
A167G
-
variant TPMT*23
A167G
-
mutant shows decreased TPMT activity
A167G
-
the mutation affects TMPT activity
A719G
the mutant exhibits reduced activity compared to the wild type enzyme
A719G
the variant is associated with low enzyme activity
A80P
-
mutant with reduced activity
A80P
-
238G>C sequence variant of the TPMT gene, location exon 5, amino acid change A80P
A80P
-
polymorphism TPMT*2
A80P
-
polymorphism TPMT*2, single nucleotide substitution G238C
A80P
-
thiopurine S-methyltransferase polymorphism, G to C transition at position 238
A80P
-
TPMT*2 polymorphismus
A80P
-
mutant shows decreased TPMT activity
A80P
-
the mutant is substantially destabilized and shows 47% of wild type activity
C132Y
-
variant TPMT*11
C132Y
-
mutant shows decreased TPMT activity
C132Y
-
the mutation affects TMPT activity
C212R
polymorphism c.634T>C, TPMT*25
C212R
-
mutant shows decreased TPMT activity
E28V
-
variant TPMT*13
E28V
-
mutant shows decreased TPMT activity
E28V
-
the mutation affects TMPT activity
G144R
-
variant TPMT*10
G144R
-
mutant shows decreased TPMT activity
G144R
-
the mutation affects TMPT activity
G238C
the mutant exhibits reduced activity compared to the wild type enzyme
G238C
the variant is associated with low enzyme activity
G36S
-
variant TPMT*24
G36S
-
mutant shows decreased TPMT activity
G460A
the mutant exhibits reduced activity compared to the wild type enzyme
G460A
the variant is associated with low enzyme activity
G71R
-
variant TPMT*18
G71R
-
mutant shows decreased TPMT activity
G71R
-
the mutation affects TMPT activity
H227Q
-
variant TPMT*7
H227Q
-
mutant shows decreased TPMT activity
H227Q
-
the mutation affects TMPT activity
K119T
-
356A>C sequence variant of the TPMT gene, location exon 5, amino acid change K119T
K119T
polymorphism c.356A>C, TPMT*9
K119T
-
mutant shows decreased TPMT activity
K119T
-
the mutation affects TMPT activity
K122T
-
variant TPMT*19
K122T
-
mutant shows normal TPMT activity
K238E
-
variant TPMT*20
K238E
-
mutant shows decreased TPMT activity
K238E
-
the mutation affects TMPT activity
L49S
-
variant TPMT*5
L49S
-
mutant shows decreased TPMT activity
L49S
-
the mutation affects TMPT activity
L49S
-
the mutant shows much greater stability comparable to that of wild type enzyme and exhibits 14% of wild type activity
L69V
polymorphism c.205C>G, TPMT*21
L69V
-
mutant shows decreased TPMT activity
L69V
-
the mutation affects TMPT activity
M1V
-
variant TPMT*14
M1V
-
the mutation affects TMPT activity
Q42E
-
variant TPMT*17
Q42E
-
mutant shows decreased TPMT activity
Q42E
-
the mutation affects TMPT activity
R163H
-
variant TPMT*16
R163H
-
mutant shows decreased TPMT activity
R163H
-
the mutation affects TMPT activity
R163P
-
variant TPMT*22
R163P
-
mutant shows decreased TPMT activity
R163P
-
the mutation affects TMPT activity
R215H
-
variant TPMT*8
R215H
-
mutant shows decreased TPMT activity
R215H
-
the mutation affects TMPT activity
R215H
the mutant shows intermediate in vivo activity compared to the wild type enzyme
S125L
-
374C>T sequence variant of the TPMT gene, location exon 6, amino acid change S125L
S125L
-
mutant shows decreased TPMT activity
S125L
-
the mutation affects TMPT activity
TPMT*2
-
polymorphism, single nucleotide substitution G238C
TPMT*2
-
polymorphism, single nucleotide substitution G238C, inactivating mutation
TPMT*2
-
polymorphism, single nucleotide substitution, G238C at codon 80
TPMT*3A
-
polymorphism, single nucleotide substitutions G460A and A719G
TPMT*3A
-
polymorphism, single nucleotide substitutions, G460A and A719G
TPMT*3A
-
polymorphism, single nucleotide substitutions, G460A at codon 154 and A719G at codon 240
TPMT*3B
-
polymorphism, single nucleotide substitution G460A
TPMT*3B
-
polymorphism, single nucleotide substitution G460A, inactivating mutation
TPMT*3B
-
polymorphism, single nucleotide substitution, G460A at codon 154
TPMT*3C
-
polymorphism, single nucleotide substitution A719G
TPMT*3C
-
polymorphism, single nucleotide substitution A719G, inactivating mutation
TPMT*3C
-
polymorphism, single nucleotide substitution, A719G at codon 240
Y180F
-
variant TPMT*6
Y180F
-
mutant shows decreased TPMT activity
Y180F
-
the mutation affects TMPT activity
Y180F
the mutant shows low in vivo activity compared to the wild type enzyme
Y240C
-
719A>G sequence variant of the TPMT gene, location exon 10, amino acid change Y240C
Y240C
-
polymorphism TPMT*3C
Y240C
-
polymorphism TPMT*3C, single nucleotide substitution A719G
Y240C
-
thiopurine S-methyltransferase polymorphism, A to G transition at position 719
Y240C
-
TPMT*3C polymorphismus
Y240C
-
variant TPMT*3C, A719G polymorphismus
Y240C
-
mutant shows decreased TPMT activity
Y240C
-
the mutation affects TMPT activity
additional information
-
at least 23 single nucleotide polymorphisms in the TPMT gene have been identified that are associated with decreased or absent TPMT activity
additional information
-
genetic polymorphisms of thiopurine methyltransferase are responsible for the variable expression of enzyme activity translating into variable efficacy and toxicity
additional information
-
more than 20 variant alleles leading to deficient methylation phenotype have been described, four of them, TPMT*2, TPMT*3A, TPMT*3B and TPMT*3C, account for 80-95% of low activity alleles in various populations
additional information
PCR amplification generates a DNA fragment of 197 bp spanning the TPMT*2, 12225G>C transversion, polymorphism
additional information
-
no amino acid substitutions in the polymorphisms TPMT*4 and TPMT*15, Met-Val substitution in the start codon of TPMT*14
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Remy, C.N.
Metabolism of thiopyrimidines and thiopurines
J. Biol. Chem.
238
1078-1084
1963
Mus musculus, Rattus norvegicus, Mus musculus Swiss-Webster
brenda
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Human kidney thiopurine methyltransferase. Purification and biochemical properties
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32
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1983
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Glutathione: an endogenous substrate for thiopurine methyltransferase?
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126
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1985
Rattus norvegicus
brenda
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Thiopurine methyltransferase: structure-activity relationships for benzoic acid inhibitors and thiophenol substrates
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29
354-358
1986
Homo sapiens
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Van Loon, J.A.; Weinshilboum, R.M.
Thiopurine methyltransferase isozymes in human renal tissue
Drug Metab. Dispos.
18
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1990
Homo sapiens, Mus musculus
brenda
Szumlanski, C.L.; Honchel, R.; Scott, M.C.; Weinshilboum, R.M.
Human liver thiopurine methyltransferase pharmacogenetics: biochemical properties, liver-erythrocyte correlation and presence of isozymes
Pharmacogenetics
2
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1992
Homo sapiens, Mus musculus
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Purine substrates for human thiopurine methyltransferase
Biochem. Pharmacol.
48
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Homo sapiens
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Krynetski, E.Y.; Krynetskaia, N.F.; Yanishevski, Y.; Evans, W.E.
Methylation of mercaptopurine, thioguanine, and their nucleotide metabolites by heterologously expressed human thiopurine S-methyltransferase
Mol. Pharmacol.
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1995
Homo sapiens
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A single point mutation leading to loss of catalytic activity in human thiopurine S-methyltransferase
Proc. Natl. Acad. Sci. USA
92
949-953
1995
Homo sapiens
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Lysaa, R.A.; Giverhaug, T.; Wold, H.L.; Aarbakke, J.
Inhibition of human thiopurine methyltransferase by furosemide, bendroflumethiazide and trichlormethiazide
Eur. J. Clin. Pharmacol.
49
393-396
1996
Homo sapiens
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Human thiopurine methyltransferase: no evidence of activation by its substrates
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62
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Molecular cloning and functional characterization of the cDNA encoding the murine thiopurine S-methyltransferase (TPMT)
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424
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1998
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brenda
Kroeplin, T.; Iven, H.
Methylation of 6-mercaptopurine and 6-thioguanine by thiopurine S-methyltransferase. A comparison of activity in red blood cell samples of 199 blood donors
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56
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61
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Weinshilboum, R.
Thiopurine pharmacogenetics: Clinical and molecular studies of thiopurine methyltransferase
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29
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2001
Homo sapiens
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Measurement of thiopurine S-methyltransferase activity in human blood samples based on high-performance liquid chromatography: reference values in erythrocytes from children
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40
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Homo sapiens
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In vitro characterization of four novel non-functional variants of the thiopurine S-methyltransferase
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309
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2003
Homo sapiens
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Identification and functional analysis of two rare allelic variants of the thiopurine S-methyltransferase gene, TPMT*16 and TPMT*19
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69
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Homo sapiens (P51580), Homo sapiens
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Thiopurine methyltransferase in acute lymphoblastic leukaemia: biochemical and molecular biological aspects
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41
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2005
Homo sapiens
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Xin, H.W.; Fischer, C.; Schwab, M.; Klotz, U.
Thiopurine S-methyltransferase as a target for drug interactions
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61
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2005
Homo sapiens
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Ford, L.T.; Berg, J.D.
Determination of thiopurine S-methyltransferase activity in erythrocytes using 6-thioguanine as substrate and a non-extraction liquid chromatographic technique
J. Chromatogr. B
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2003
Homo sapiens
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Assessment of thiopurine methyltransferase enzyme activity is superior to genotype in predicting myelosuppression following azathioprine therapy in patients with inflammatory bowel disease
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25
1069-1077
2007
Homo sapiens
brenda
Winter, J.W.; Marinaki, A.M.; Sanderson, J.D.; Mills, P.R.
TPMT genotype and the response to azathioprine in inflammatory bowel disease: authors reply to comments
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26
1084-1085
2007
Homo sapiens
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Palmieri, O.; Latiano, A.; Bossa, F.; Vecchi, M.; DInca, R.; Guagnozzi, D.; Tonelli, F.; Cucchiara, S.; Valvano, M.R.; Latiano, T.; Andriulli, A.; Annese, V.
Sequential evaluation of thiopurine methyltransferase, inosine triphosphate pyrophosphatase, and HPRT1 genes polymorphisms to explain thiopurines toxicity and efficacy
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26
737-745
2007
Homo sapiens
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Roblin, X.; Biroulet, L.P.; Phelip, J.M.; Nancey, S.; Flourie, B.
A 6-Thioguanine Nucleotide Threshold Level of 400 pmol/8 x 10(8) Erythrocytes Predicts Azathioprine Refractoriness in Patients With Inflammatory Bowel Disease and Normal TPMT Activity
Am. J. Gastroenterol.
102
1-8
2007
Homo sapiens
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Tumer, T.B.; Ulusoy, G.; Adali, O.; Sahin, G.; Gozdasoglu, S.; Arinc, E.
The low frequency of defective TPMT alleles in Turkish population: a study on pediatric patients with acute lymphoblastic leukemia
Am. J. Hematol.
82
906-910
2007
Homo sapiens
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Yenson, P.R.; Forrest, D.; Schmiegelow, K.; Dalal, B.I.
Azathioprine-associated acute myeloid leukemia in a patient with Crohns disease and thiopurine S-methyltransferase deficiency
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83
80-83
2008
Homo sapiens
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Litos, I.K.; Emmanouilidou, E.; Glynou, K.M.; Laios, E.; Ioannou, P.C.; Christopoulos, T.K.; Kampa, M.; Castanas, E.; Gravanis, A.
Rapid genotyping of CYP2D6, CYP2C19 and TPMT polymorphisms by primer extension reaction in a dipstick format
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389
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Homo sapiens (P51580)
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Role of thiopurine methyltransferase activity in the safety and efficacy of azathioprine in the treatment of pemphigus vulgaris
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144
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2008
Homo sapiens
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Hogarth, L.A.; Redfern, C.P.; Teodoridis, J.M.; Hall, A.G.; Anderson, H.; Case, M.C.; Coulthard, S.A.
The effect of thiopurine drugs on DNA methylation in relation to TPMT expression
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76
1024-1035
2008
Homo sapiens
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Garat, A.; Cauffiez, C.; Renault, N.; Lo-Guidice, J.M.; Allorge, D.; Chevalier, D.; Houdret, N.; Chavatte, P.; Loriot, M.A.; Gala, J.L.; Broly, F.
Characterisation of novel defective thiopurine S-methyltransferase allelic variants
Biochem. Pharmacol.
76
404-415
2008
Homo sapiens (P51580), Homo sapiens
brenda
Peng, Y.; Feng, Q.; Wilk, D.; Adjei, A.A.; Salavaggione, O.E.; Weinshilboum, R.M.; Yee, V.C.
Structural basis of substrate recognition in thiopurine s-methyltransferase
Biochemistry
47
6216-6225
2008
Mus musculus (O55060), Mus musculus, Homo sapiens (P51580), Homo sapiens
brenda
Haglund, S.; Taipalensuu, J.; Peterson, C.; Almer, S.
IMPDH activity in thiopurine-treated patients with inflammatory bowel disease - relation to TPMT activity and metabolite concentrations
Br. J. Clin. Pharmacol.
65
69-77
2008
Homo sapiens
brenda
Hartford, C.; Vasquez, E.; Schwab, M.; Edick, M.J.; Rehg, J.E.; Grosveld, G.; Pui, C.H.; Evans, W.E.; Relling, M.V.
Differential effects of targeted disruption of thiopurine methyltransferase on mercaptopurine and thioguanine pharmacodynamics
Cancer Res.
67
4965-4972
2007
Mus musculus
brenda
Tamm, R.; Oselin, K.; Kallassalu, K.; Magi, R.; Anier, K.; Remm, M.; Metspalu, A.
Thiopurine S-methyltransferase (TPMT) pharmacogenetics: three new mutations and haplotype analysis in the Estonian population
Clin. Chem. Lab. Med.
46
974-979
2008
Homo sapiens
brenda
Zhang, L.; Song, D.; Zhang, W.; Zhao, J.; Jia, L.; Xing, D.
Efficient screening method of the thiopurine methyltransferase polymorphisms for patients considering taking thiopurine drugs in a Chinese Han population in Henan Province (central China)
Clin. Chim. Acta
376
45-51
2007
Homo sapiens
brenda
Lee, S.S.; Kim, W.Y.; Jang, Y.J.; Shin, J.G.
Duplex pyrosequencing of the TPMT3C and TPMT6 alleles in Korean and Vietnamese populations
Clin. Chim. Acta
398
82-85
2008
Homo sapiens
brenda
Gardiner, S.J.; Gearry, R.B.; Begg, E.J.; Zhang, M.; Barclay, M.L.
Thiopurine dose in intermediate and normal metabolizers of thiopurine methyltransferase may differ three-fold
Clin. Gastroenterol. Hepatol.
6; 654-60
quiz 604
2008
Homo sapiens
brenda
Jones, T.S.; Yang, W.; Evans, W.E.; Relling, M.V.
Using HapMap tools in pharmacogenomic discovery: the thiopurine methyltransferase polymorphism
Clin. Pharmacol. Ther.
81
729-734
2007
Homo sapiens
brenda
Zhou, S.; Chowbay, B.
Clinical significance of thiopurine S-methyltransferase gene polymorphisms
Curr. Pharmacogenomics
5
103-115
2007
Mammalia
-
brenda
Gisbert, J.P.; Gomollon, F.; Cara, C.; Luna, M.; Gonzalez-Lama, Y.; Pajares, J.M.; Mate, J.; Guijarro, L.G.
Thiopurine methyltransferase activity in Spain: a study of 14,545 patients
Dig. Dis. Sci.
52
1262-1269
2007
Homo sapiens
brenda
Kwan, L.Y.; Devlin, S.M.; Mirocha, J.M.; Papadakis, K.A.
Thiopurine methyltransferase activity combined with 6-thioguanine metabolite levels predicts clinical response to thiopurines in patients with inflammatory bowel disease
Dig. Liver Dis.
40
425-432
2008
Homo sapiens
brenda
Oselin, K.; Anier, K.
Inhibition of human thiopurine S-methyltransferase by various nonsteroidal anti-inflammatory drugs in vitro: a mechanism for possible drug interactions
Drug Metab. Dispos.
35
1452-1454
2007
Homo sapiens
brenda
Oliveira, E.; Quental, S.; Alves, S.; Amorim, A.; Prata, M.J.
Do the distribution patterns of polymorphisms at the thiopurine S-methyltransferase locus in sub-Saharan populations need revision? Hints from Cabinda and Mozambique
Eur. J. Clin. Pharmacol.
63
703-706
2007
Homo sapiens
brenda
Kham, S.K.; Soh, C.K.; Liu, T.C.; Chan, Y.H.; Ariffin, H.; Tan, P.L.; Yeoh, A.E.
Thiopurine S-methyltransferase activity in three major Asian populations: a population-based study in Singapore
Eur. J. Clin. Pharmacol.
64
373-379
2008
Homo sapiens
brenda
Bezier, M.; Reguiai, Z.; Vitry, F.; Broly, F.; Bernard, P.
Thiopurine S-methyltransferase genotypic analysis in autoimmune bullous diseases
Eur. J. Dermatol.
18
512-517
2008
Homo sapiens
brenda
Perri, D.; Cole, D.E.; Friedman, O.; Piliotis, E.; Mintz, S.; Adhikari, N.K.
Azathioprine and diffuse alveolar haemorrhage: the pharmacogenetics of thiopurine methyltransferase
Eur. Respir. J.
30
1014-1017
2007
Homo sapiens
brenda
Richard, V.S.; Al-Ismail, D.; Salamat, A.
Should we test TPMT enzyme levels before starting azathioprine?
Hematology
12
359-360
2007
Homo sapiens
brenda
Compagni, A.; Bartoli, S.; Buehrlen, B.; Fattore, G.; Ibarreta, D.; de Mesa, E.G.
Avoiding adverse drug reactions by pharmacogenetic testing: a systematic review of the economic evidence in the case of TPMT and AZA-induced side effects
Int. J. Technol. Assess. Health Care
24
294-302
2008
Homo sapiens
brenda
Fargher, E.A.; Tricker, K.; Newman, W.; Elliott, R.; Roberts, S.A.; Shaffer, J.L.; Bruce, I.; Payne, K.
Current use of pharmacogenetic testing: a national survey of thiopurine methyltransferase testing prior to azathioprine prescription
J. Clin. Pharm. Ther.
32
187-195
2007
Homo sapiens
brenda
Fakhoury, M.; Andreu-Gallien, J.; Mahr, A.; Medard, Y.; Azougagh, S.; Vilmer, E.; Jacqz-Aigrain, E.
Should TPMT genotype and activity be used to monitor 6-mercaptopurine treatment in children with acute lymphoblastic leukaemia?
J. Clin. Pharm. Ther.
32
633-639
2007
Homo sapiens
brenda
Hoover, S.; Striker, R.
Thiopurines inhibit bovine viral diarrhea virus production in a thiopurine methyltransferase-dependent manner
J. Gen. Virol.
89
1000-1009
2008
Bos taurus, Homo sapiens
brenda
Rutherford, K.; Daggett, V.
Four human thiopurine s-methyltransferase alleles severely affect protein structure and dynamics
J. Mol. Biol.
379
803-814
2008
Homo sapiens
brenda
Chowdhury, J.; Kagiala, G.V.; Pushpakom, S.; Lauzon, J.; Makin, A.; Atrazhev, A.; Stickel, A.; Newman, W.G.; Backhouse, C.J.; Pilarski, L.M.
Microfluidic platform for single nucleotide polymorphism genotyping of the thiopurine S-methyltransferase gene to evaluate risk for adverse drug events
J. Mol. Diagn.
9
521-529
2007
Homo sapiens
brenda
Tamori, A.; Shinzaki, M.; Kosaka, S.; Hayashi, T.; Iwai, S.; Enomoto, M.; Habu, D.; Sakaguchi, H.; Kawada, N.; Hino, M.; Shiomi, S.; Nishiguchi, S.
Thiopurine S-methyltransferase gene polymorphism in Japanese patients with autoimmune liver diseases
Liver Int.
27
95-100
2007
Homo sapiens
brenda
Taja-Chayeb, L.; Vidal-Millan, S.; Gutierrez, O.; Ostrosky-Wegman, P.; Duenas-Gonzalez, A.; Candelaria, M.
Thiopurine S-methyltransferase gene (TMPT) polymorphisms in a Mexican population of healthy individuals and leukemic patients
Med. Oncol.
25
56-62
2008
Homo sapiens
brenda
Slanar, O.; Bortlik, M.; Buzkova, H.; Donoval, R.; Pechandova, K.; Sebesta, I.; Lukas, M.; Perlik, F.
Polymorphisms of the TPMT gene in the Czech healthy population and patients with inflammatory bowel disease
Nucleosides Nucleotides Nucleic Acids
27
835-838
2008
Homo sapiens
brenda
Lindqvist, M.; Skoglund, K.; Karlgren, A.; Soederkvist, P.; Peterson, C.; Kidhall, I.; Almer, S.
Explaining TPMT genotype/phenotype discrepancy by haplotyping of TPMT*3A and identification of a novel sequence variant, TPMT*23
Pharmacogenet. Genomics
17
891-895
2007
Homo sapiens
brenda
Roberts, R.L.; Gearry, R.B.; Bland, M.V.; Sies, C.W.; George, P.M.; Burt, M.; Marinaki, A.M.; Arenas, M.; Barclay, M.L.; Kennedy, M.A.
Trinucleotide repeat variants in the promoter of the thiopurine S-methyltransferase gene of patients exhibiting ultra-high enzyme activity
Pharmacogenet. Genomics
18
434-438
2008
Homo sapiens
brenda
Ujiie, S.; Sasaki, T.; Mizugaki, M.; Ishikawa, M.; Hiratsuka, M.
Functional characterization of 23 allelic variants of thiopurine S-methyltransferase gene (TPMT*2 - *24)
Pharmacogenet. Genomics
18
887-893
2008
Homo sapiens
brenda
Cooper, S.C.; Ford, L.T.; Berg, J.D.; Lewis, M.J.
Ethnic variation of thiopurine S-methyltransferase activity: a large, prospective population study
Pharmacogenomics
9
303-309
2008
Homo sapiens
brenda
Chrzanowska, M.; Kurzawski, M.; Dro?dzik, M.; Mazik, M.; Oko, A.; Czekalski, S.
Thiopurine S-methyltransferase phenotype-genotype correlation in hemodialyzed patients
Pharmacol. Rep.
58
973-978
2006
Homo sapiens
brenda
Dilger, K.; Schaeffeler, E.; Lukas, M.; Strauch, U.; Herfarth, H.; Mueller, R.; Schwab, M.
Monitoring of thiopurine methyltransferase activity in postsurgical patients with Crohns disease during 1 year of treatment with azathioprine or mesalazine
Ther. Drug Monit.
29
1-5
2007
Homo sapiens
brenda
de Boer, N.K.; van Bodegraven, A.A.; de Graaf, P.; van der Hulst, R.W.; Zoetekouw, L.; van Kuilenburg, A.B.
Paradoxical elevated thiopurine S-methyltransferase activity after pancytopenia during azathioprine therapy: potential influence of red blood cell age
Ther. Drug Monit.
30
390-393
2008
Homo sapiens
brenda
Alvarez Beltran, M.; Infante Pina, D.; Tormo Carnice, R.; Segarra Canton, O.; Redecillas Ferreiro, S.
Optimising azathioprine treatment: determination of thiopurine methyltransferase activity and thiopurine metabolites
An. Pediatr. (Barc. )
70
126-131
2009
Homo sapiens
brenda
el-Azhary, R.A.; Farmer, S.A.; Drage, L.A.; Rogers, R.S.; McEvoy, M.T.; Davis, M.D.; Bridges, A.G.; Gibson, L.E.
Thioguanine nucleotides and thiopurine methyltransferase in immunobullous diseases: optimal levels as adjunctive tools for azathioprine monitoring
Arch. Dermatol.
145
644-652
2009
Homo sapiens
brenda
Milek, M.; Karas Kuzelicki, N.; Smid, A.; Mlinaric-Rascan, I.
S-adenosylmethionine regulates thiopurine methyltransferase activity and decreases 6-mercaptopurine cytotoxicity in MOLT lymphoblasts
Biochem. Pharmacol.
77
1845-1853
2009
Homo sapiens
brenda
Feng, Q.; Vannaprasaht, S.; Peng, Y.; Angsuthum, S.; Avihingsanon, Y.; Yee, V.C.; Tassaneeyakul, W.; Weinshilboum, R.M.
Thiopurine S-methyltransferase pharmacogenetics: Functional characterization of a novel rapidly degraded variant allozyme
Biochem. Pharmacol.
79
1053-1061
2009
Homo sapiens (P51580), Homo sapiens
brenda
Kham, S.K.; Soh, C.K.; Aw, D.C.; Yeoh, A.E.
TPMT*26 (208F-->L), a novel mutation detected in a Chinese
Br. J. Clin. Pharmacol.
68
120-123
2009
Homo sapiens
brenda
Tsui, N.
Multiple thiopurine S-methyltransferase variation detection: A step toward personalized medicine
Clin. Chem.
54
1598-1599
2008
Homo sapiens
brenda
Schaeffeler, E.; Zanger, U.M.; Eichelbaum, M.; Asante-Poku, S.; Shin, J.G.; Schwab, M.
Highly multiplexed genotyping of thiopurine S-methyltransferase variants using MALD-TOF mass spectrometry: reliable genotyping in different ethnic groups
Clin. Chem.
54
1637-1647
2008
Homo sapiens
brenda
Vestergaard, T.; Bygum, A.
An audit of thiopurine methyltransferase genotyping and phenotyping before intended azathioprine treatment for dermatological conditions
Clin. Exp. Dermatol.
35
140-144
2010
Homo sapiens
brenda
Gisbert, J.
Role of monitoring thiopurine methyltransferase (TPMT) activity in the individualized therapy with azathioprine or 6-mercaptopurine
Curr. Pharmacogenomics Person. Med.
6
33-44
2008
Homo sapiens
-
brenda
Egle, R.; Milek, M.; Mlinaric-Rascan, I.; Fahr, A.; Kristl, J.
A novel gene delivery system for stable transfection of thiopurine-S-methyltransferase gene in versatile cell types
Eur. J. Pharm. Biopharm.
69
23-30
2008
Homo sapiens
brenda
Stocco, G.; Crews, K.R.; Evans, W.E.
Genetic polymorphism of inosine-triphosphate-pyrophosphatase influences mercaptopurine metabolism and toxicity during treatment of acute lymphoblastic leukemia individualized for thiopurine-S-methyl-transferase status
Expert. Opin. Drug Saf.
9
23-37
2010
Homo sapiens
brenda
Cheon, J.H.; Kim, J.H.; Kim, B.Y.; Kim, S.W.; Hong, S.Y.; Eun, C.S.; Hong, S.S.; Byeon, J.S.; Kim, T.I.; Han, D.S.; Yang, S.K.; Lee, K.R.; Kim, W.H.
Allele frequency of thiopurine methyltransferase and inosine triphosphate pyrophosphatase gene polymorphisms in Korean patients with inflammatory bowel diseases
Hepatogastroenterology
56
421-423
2009
Homo sapiens
brenda
Tomkova, J.; Friedecky, D.; Polynkova, A.; Adam, T.
Capillary electrophoresis determination of thiopurine methyl transferase activity in erythrocytes
J. Chromatogr. B
877
1943-1945
2009
Homo sapiens
brenda
Gonzalez-Del Angel, A.; Bermadez-Lapez, C.; Alcantara-Ortigoza, M.; Vela-Amieva, M.; Castillo-Cruz, R.; Martinez, V.; Torres-Espadola, L.
Thiopurine S-methyltransferase (TPMT) genetic polymorphisms in Mexican newborns
J. Clin. Pharm. Ther.
34
703-708
2009
Homo sapiens
brenda
Hindorf, U.; Jahed, K.; Bergquist, A.; Verbaan, H.; Prytz, H.; Wallerstedt, S.; Werner, M.; Olsson, R.; Bjoernsson, E.; Peterson, C.; Almer, S.H.
Characterisation and utility of thiopurine methyltransferase and thiopurine metabolite measurements in autoimmune hepatitis
J. Hepatol.
52
106-111
2010
Homo sapiens
brenda
Schmiegelow, K.; Forestier, E.; Kristinsson, J.; Soederhaell, S.; Vettenranta, K.; Weinshilboum, R.; Wesenberg, F.; Wesenberg, F.
Thiopurine methyltransferase activity is related to the risk of relapse of childhood acute lymphoblastic leukemia: results from the NOPHO ALL-92 study
Leukemia
23
557-564
2009
Homo sapiens
brenda
Sheffield, L.J.; Irving, P.; Gupta, A.; Byron, K.; Macrae, F.A.; Phillimore, H.; Dronavalli, M.; Rose, R.; George, P.; Walmsley, T.; Dixon, B.; Poole, S.; Dooley, M.; Sparrow, M.
Thiopurine methyltransferase and thiopurine metabolite testing in patients with inflammatory bowel disease who are taking thiopurine drugs
Pharmacogenomics
10
1091-1099
2009
Homo sapiens
brenda
Karas-Kuzelicki, N.; Mlinaric-Rascan, I.
Individualization of thiopurine therapy: thiopurine S-methyltransferase and beyond
Pharmacogenomics
10
1309-1322
2009
Homo sapiens
brenda
Serpe, L.; Calvo, P.L.; Muntoni, E.; DAntico, S.; Giaccone, M.; Avagnina, A.; Baldi, M.; Barbera, C.; Curti, F.; Pera, A.; Eandi, M.; Zara, G.P.; Canaparo, R.
Thiopurine S-methyltransferase pharmacogenetics in a large-scale healthy Italian-Caucasian population: differences in enzyme activity
Pharmacogenomics
10
1753-1765
2009
Homo sapiens
brenda
Silva, M.R.; de Oliveira, B.M.; Viana, M.B.; Murao, M.; Romanha, A.J.
Thiopurine S-methyltransferase (TPMT) gene polymorphism in Brazilian children with acute lymphoblastic leukemia: association with clinical and laboratory data
Ther. Drug Monit.
30
700-704
2008
Homo sapiens
brenda
Milek, M.; Smid, A.; Tamm, R.; Kuzelicki, N.K.; Metspalu, A.; Mlinaric-Rascan, I.
Post-translational stabilization of thiopurine S-methyltransferase by S-adenosyl-L-methionine reveals regulation of TPMT*1 and *3C allozymes
Biochem. Pharmacol.
83
969-976
2012
Homo sapiens
brenda
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
Biochemistry
51
5912-5920
2012
Homo sapiens
brenda
Pavlovic, S.; Zukic, B.
Individualized therapy: Role of thiopurine S-methyltransferase protein and genetic variants
J. Med. Biochem.
29
150-155
2010
Homo sapiens
-
brenda
Hosni-Ahmed, A.; Barnes, J.D.; Wan, J.; Jones, T.S.
Thiopurine methyltransferase predicts the extent of cytotoxicty and DNA damage in astroglial cells after thioguanine exposure
PLoS ONE
6
e29163
2011
Homo sapiens, Mus musculus
brenda
Kasirer, Y.; Mevorach, R.; Renbaum, P.; Algur, N.; Soiferman, D.; Beeri, R.; Rachman, Y.; Segel, R.; Turner, D.
Thiopurine S-methyltransferase (TPMT) activity is better determined by biochemical assay versus genotyping in the Jewish population
Digest. Dis. Sci.
59
1207-1212
2014
Homo sapiens (P51580)
brenda
Wennerstrand, P.; Martensson, L.G.; Soederhaell, S.; Zimdahl, A.; Appell, M.L.
Methotrexate binds to recombinant thiopurine S-methyltransferase and inhibits enzyme activity after high-dose infusions in childhood leukaemia
Eur. J. Clin. Pharmacol.
69
1641-1649
2013
Homo sapiens (P51580), Homo sapiens
brenda
Roberts, R.L.; Wallace, M.C.; Drake, J.M.; Stamp, L.K.
Identification of a novel thiopurine S-methyltransferase allele (TPMT 37)
Pharmacogenet. Genomics
24
320-323
2014
Homo sapiens (P51580)
brenda
Wennerstrand, P.; Blissing, A.; Martensson, L.G.
In vitro protein stability of two naturally occurring thiopurine S-methyltransferase variants biophysical characterization of TPMT*6 and TPMT*8
ACS Omega
2
4991-4999
2017
Homo sapiens (P51580)
brenda
Citterio-Quentin, A.; El Mahmoudi, A.; Perret, T.; Conway, A.; Ryan, A.; Beringer, A.; Lachaux, A.; Boulieu, R.
Red Blood cell IMPDH activity in adults and children with or without azathioprine Relationship between thiopurine metabolites, ITPA and TPMT activities
Basic Clin. Pharmacol. Toxicol.
124
600-606
2019
Homo sapiens
brenda
Mei, S.; Li, X.; Gong, X.; Zhang, X.; Li, X.; Yang, L.; Zhu, L.; Zhou, H.; Liu, Y.; Zhou, A.; Zhang, X.; Zhao, Z.
Comparison of 6-mercaptopurine with 6-thioguanine for the analysis of thiopurine S-methyltransferase activity in human erythrocyte by LC-MS/MS
Biomed. Chromatogr.
31
e3959
2017
Homo sapiens
brenda
Ma, J.; Sies, C.W.; Pike, L.S.
Analytical and clinical validation of an LC-MS/MS method to measure thiopurine S-methyltransferase activity by quantifying d3-6-MMP
Clin. Biochem.
54
100-105
2018
Homo sapiens
brenda
Rieger, H.; Schmidt, P.; Schaeffeler, E.; Abe, M.; Schiffhauer, M.; Schwab, M.; von Ahsen, N.; Zurek, G.; Kirchherr, H.; Shipkova, M.; Wieland, E.
Validation of a high-performance liquid chromatography method for thiopurine S-methyltransferase activity in whole blood using 6-mercaptopurine as substrate
Clin. Chem. Lab. Med.
56
803-809
2018
Homo sapiens
brenda
Pashazadeh, P.; Marjani, A.; Asadi, J.; Khoshnia, M.
Thiopurine methyltransferase genetic polymorphisms and activity and metabolic products of azathioprine in patients with inflammatory bowel disease
Endocr. Metab. Immune Disord. Drug Targets
19
541-547
2019
Homo sapiens
brenda
Illamola, S.M.; Echaabi, A.K.; Mazeron, C.; Deshayes, S.; Loriot, M.A.; Pallet, N.
Development and validation of a UPLC-UV method for the quantification of thiopurine methyltransferase enzyme activity in human erythrocytes
J. Chromatogr. B Analyt. Technol. Biomed. Life Sci.
1113
91-97
2019
Homo sapiens
brenda
Pecher, D.; Dokupilova, S.; Zelinkova, Z.; Peppelenbosch, M.; Mikusova, V.; Mikus, P.
Determination of thiopurine S-methyltransferase activity by hydrophilic interaction liquid chromatography hyphenated with mass spectrometry
J. Pharm. Biomed. Anal.
142
244-251
2017
Homo sapiens
brenda