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Information on EC 2.1.1.67 - thiopurine S-methyltransferase
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EC Tree
2.1.1.67 thiopurine S-methyltransferaseIUBMB Comments
Also acts, more slowly, on thiopyrimidines and aromatic thiols. Not identical with EC 2.1.1.9 thiol S-methyltransferase.
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Word Map
- 2.1.1.67
- azathioprine
- 6-mercaptopurine
- bowel
-
pharmacogenetics
- children
- lymphoblastic
- leukemia
-
myelosuppression
- erythrocyte
-
tpmt*2
- crohn
- thioguanine
-
dosing
-
s-methylation
- autoimmune
- marrow
-
remission
-
caucasian
- leukopenia
-
myelotoxicity
-
ulcerative
- 6-methylmercaptopurine
- methotrexate
-
ethnic
- inosine
- colitis
-
azathioprine-induced
- medicine
-
allele-specific
-
interindividual
-
nudt15
-
5-aminosalicylic
-
thiopurine-induced
- allopurinol
- pancytopenia
- neutropenia
- dihydropyrimidine
-
infliximab
-
drug-metabolizing
-
pyrophosphohydrolase
-
trimodal
-
hematotoxicity
- analysis
-
nudix
- pemphigus
- diagnostics
- mofetil
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
thiopurine methyltransferase, thiopurine s-methyltransferase, thiopurine methyl transferase, thiopurine-s-methyl-transferase, s-adenosyl-l-methionine:thiopurine s-methyltransferase, 6-thiopurine s-methyltransferase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
6-thiopurine transmethylase
-
-
-
-
mercaptopurine methyltransferase
-
-
-
-
thiopurine methyltransferase
thiopurine S-methyltransferase
TPMT
thiopurine methyltransferase
-
-
-
-
thiopurine methyltransferase
-
-
thiopurine S-methyltransferase
-
-
TPMT
-
-
-
-
TPMT
-
-
657544, 657749, 658653, 658654, 659566, 684266, 684275, 684276, 684279, 684733, 685037, 685852, 686157, 686161, 686184, 686189, 686326, 686351, 686503, 686505, 686507, 686574, 686996, 687195, 687982, 687983, 688126, 688415, 688452, 688777, 689358, 689362, 689365, 689368, 689369, 690115, 690118, 701657, 701941, 702159, 702940, 703266, 703267, 703275, 703355, 703564, 703600, 703931, 704818, 704829, 704932, 705450, 706091, 706092, 706093, 706816, 718804, 718942, 720181, 720847, 755922, 756145, 756497, 756499, 756597, 757309, 757473
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + a thiopurine = S-adenosyl-L-homocysteine + a thiopurine S-methylether
also acts, more slowly, on thiopyrimidines and aromatic thiols. Not identical with EC 2.1.1.9 thiol S-methyltransferase
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
methyl group transfer
methyl group transfer
-
-
-
-
methyl group transfer
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:thiopurine S-methyltransferase
Also acts, more slowly, on thiopyrimidines and aromatic thiols. Not identical with EC 2.1.1.9 thiol S-methyltransferase.
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CAS REGISTRY NUMBER
COMMENTARY
67339-09-7
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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-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-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 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-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-homocysteine + 6-methylmercaptopurine + ?
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
-
-
-
-
?
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-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
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + 6-mercaptopurine
S-adenosyl-L-homocysteine + 6-methylmercaptopurine
-
-
-
-
?
S-adenosyl-L-methionine + 6-thiopurine
S-adenosyl-L-homocysteine + 6-methylthiopurine
-
-
-
-
?
S-adenosyl-L-methionine + a thiopurine
S-adenosyl-L-homocysteine + a thiopurine S-methylether
additional information
?
-
-
S-adenosyl-L-methionine and sinefungin prevent degradation of TPMT by stabilizing ist native structure
-
-
?
S-adenosyl-L-methionine + a thiopurine
S-adenosyl-L-homocysteine + a thiopurine S-methylether
-
-
485519, 485520, 485521, 485522, 485523, 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
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
low levels of methionine can result in low S-adenosyl-L-methionine levels and consequently decreased TPMT activity
-
6-Mercaptopurine
-
TPMT activity and protein levels are diminished in cells incubated with 6-mercaptopurine
benzoic acid
-
substituted benzoic acids, benzoic acid compounds, noncompetitive inhibition
Furosemide
-
IC50: 0.015-0.019 mM, has the potential to inhibit thiopurine S-methyltransferase in patients with chronic inflammatory bowel disease
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
S-adenosyl-L-methionine
-
S-adenosyl-L-methionine acts as a positive modulator of TPMT activity, the effect of S-adenosyl-L-methionine appears to be restricted to protein stabilisation rather than an increase of TPMT expression
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
various thiophenols as substrates, Km 0.0008-0.0078
-
0.0137
6-thioguanine
mutant L69V, cytosolic fraction of yeast cells is incubated with 500 microM of 6-TG and 0-400 microM of SAM
0.0188
6-thioguanine
1.2fold increase in KM-value compared to wild-type variant
0.03435
6-thioguanine
wild-type enzyme, cytosolic fraction of yeast cells is incubated with 500 microM of 6-TG and 0-400 microM of SAM
0.0448
6-thioguanine
2.9fold increase in KM-value compared to wild-type variant
0.0555
6-thioguanine
-
the Km-value of the variant Ser125Leu is 1.6fold higher than the Km-value of the wild-type variant, the ratio of Vmax to Km-value is 27% of the wild-type ratio
0.0562
6-thioguanine
mutant L69V, cytosolic fraction of yeast cells is incubated with 0-350 microM of 6-TG and 1mM of SAM
0.0627
6-thioguanine
wild-type enzyme, cytosolic fraction of yeast cells is incubated with 0-350 microM of 6-TG and 1mM of SAM
0.0635
6-thioguanine
-
the Km-value of the variant Gly144Arg is 1.8fold higher than the Km-value of the wild-type variant, the ratio of Vmax to Km-value is 31% of the wild-type ratio
0.072
6-thioguanine
mutant C212R, cytosolic fraction of yeast cells is incubated with 0-350 microM of 6-TG and 1mM of SAM
0.0759
6-thioguanine
-
the Km-value of the variant Glu28Val is 2.2fold higher than the Km-value of the wild-type variant, the ratio of Vmax to KM-value is 58% of the wild-type ratio
0.07985
6-thioguanine
mutant K119T, cytosolic fraction of yeast cells is incubated with 0-350 microM of 6-TG and 1mM of SAM
0.08305
6-thioguanine
mutant Q179H, cytosolic fraction of yeast cells is incubated with 0-350 microM of 6-TG and 1mM of SAM
0.1799
6-thioguanine
-
the Km-value of the variant Gly144Arg is 5.1fold higher than the Km-value of the wild-type variant, the ratio of Vmax to KM-value is 10.4% of the wild-type ratio
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.015 - 0.019
Furosemide
Homo sapiens
-
IC50: 0.015-0.019 mM, has the potential to inhibit thiopurine S-methyltransferase in patients with chronic inflammatory bowel disease
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00000716
-
TMPT reference activity after recovery of the bone marrow suppression
0.00003033
-
elevated TPMT activity during the recovery phase of a bone marrow suppression, following the pancytopenic period
additional information
additional information
-
determination of thiopurine S-methyltransferase activity in erythrocytes using 6-thioguanine as substrate and a non-extraction liquid chromatographic technique. This method minimzes sample-handling, reduces inherent imprecision, the possibility of laboratory error and has a potential for further automation
additional information
-
activity of TPMT in nmol of the formed 6-mMP/g Hb/h, dialyzed patients, total 30.6, females 30.1, males 31.7, control group, total 28.4, females 28.4, males 28.7
additional information
-
median TPMT activities, Singapore Chinese 16.4 U, Singapore Malays 17.8 U, Singapore Indians 16.4 U, one unit of activity is defined as a formation of 1 nmol of 6-methylmercaptopurine per ml of packed red blood cells per h incubation at 37°C
additional information
-
normal thiopurine methyltransferase activity, 7.5-14 U/ml erythrocytes
additional information
-
thiopurine methyltransferase levels above 23 nmol 6-methylthioguanine/g Hb per h indicates normal enzyme activity
additional information
-
TPMT activity amongst 253 healthy Estonian volunteers varies from 21.5 ng/ml/h to 185.5 ng/ml/h with a median of 86.24 ng/ml/h
additional information
-
TPMT activity of 0.5% of the patients is low, less than 5 U/ml RBC, for 11.9% intermediate, 5-13.7 U/ml RBC, and for 87.6% high, greater than 13.7 U/ml RBC
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
7.4
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
-
685852, 686157, 686161, 686167, 686184, 686189, 686326, 686328, 686351, 686503, 686505, 686507, 686574, 686996, 687195, 687982, 687983, 688126, 688415, 688452, 688777, 688807, 689274, 689358, 689362, 689365, 689368, 689369, 690115, 690118, 701657, 701941, 702159
-
-
brenda
-
702940, 703266, 703267, 703275, 703355, 703564, 703600, 703931, 704818, 704829, 704932, 705450, 706091, 706092, 706093, 706816, 718804, 718942, 720181, 720847
-
-
brenda
human
485516, 485518, 485519, 485520, 485521, 485522, 485523, 485524, 485525, 485526, 485527, 485528, 485529
-
-
brenda
variant Arg163His, i.e. variant TPMT*16, loss-of function allele of TPMT, patients heterozygous for the Arg163His mutation are intermediate methylators
UniProt
brenda
variant Lys122Thr, i.e. variant TPMT*19, missense mutation in patients with Crohn's disease, patients heterozygous for the Lys122Thr mutation have normal TPMT activity
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
embryonic kidney cell line with inducible thiopurine methyltransferase
brenda
-
-
485516, 485520, 485523, 485524, 485526, 485527, 684265, 684733, 685852, 686157, 686161, 686184, 686326, 686505, 686507, 687983, 688452, 689358, 689368, 689369, 690115, 690118, 701941, 703267, 703275, 703931, 704829, 756499, 756597
brenda
-
-
485516, 485518, 485520, 485522, 485523, 485524, 485525, 485526, 485527, 657544, 659566, 685852, 686157, 686184, 686326, 686351, 686505, 686507, 686574, 687983, 689358, 689362, 689368, 689369, 690115, 690118, 702940, 703355, 704818, 704932, 705450, 706091, 706092, 706093, 706816, 718804, 755922, 756145, 756497, 757309, 757473
brenda
-
TPMT activity is significantly lower in patients with acute lymphoblastic leukemia compared to control. Increase of TPMT activity during maintainance treatment with 6-mercaptopurine and already after induction therapy (treatment with antifolates, e.g. methotrexate and trimethoprim), before the patients receive 6-mercaptopurine
brenda
-
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
-
brenda
-
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
malfunction
-
when thiopurine methyltransferase protein activity is low a greater degree of cytotoxicity and DNA damage can occur after thioguanine exposure
malfunction
-
when thiopurine methyltransferase protein activity is low a greater degree of cytotoxicity and DNA damage can occur after thioguanine exposure
malfunction
intermediate and low enzyme activity may lead to leukopenia following thiopurine treatment
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
two crystal structures of murine TPMT are determined, as a binary complex with the product S-adenosyl-L-homocysteine and as a ternary complex with S-adenosyl-L-homocysteine and the substrate 6-mercaptopurine, to 1.8 and 2.0 A resolution, respectively
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
238G>C
460G>A
719A>G
A154T
A154T/Y240C
A154Y
-
thiopurine S-methyltransferase polymorphism, G to A transition at position 460
A167G
A719G
A80P
C132Y
C212R
C216T
the mutant exhibits reduced activity compared to the wild type enzyme
E28V
G144R
G238C
G36S
G460A
G71R
H227Q
K119T
K122T
K238E
L49S
L69V
M1V
Q42E
R152A/R226A
mutant to probe, whether this residue is important for catalysis
R163H
R163P
R215H
S125L
TPMT*2
TPMT*3A
TPMT*3B
TPMT*3C
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
Y180F
Y240C
additional information
A154T
-
460G>A sequence variant of the TPMT gene, location exon 7, amino acid change A154T
A154T/Y240C
-
polymorphism TPMT*3A, single nucleotide substitutions G460A and A719G
A719G
the mutant exhibits reduced activity compared to the wild type enzyme
A80P
-
238G>C sequence variant of the TPMT gene, location exon 5, amino acid change A80P
A80P
-
thiopurine S-methyltransferase polymorphism, G to C transition at position 238
A80P
-
the mutant is substantially destabilized and shows 47% of wild type activity
G238C
the mutant exhibits reduced activity compared to the wild type enzyme
G460A
the mutant exhibits reduced activity compared to the wild type enzyme
K119T
-
356A>C sequence variant of the TPMT gene, location exon 5, amino acid change K119T
L49S
-
the mutant shows much greater stability comparable to that of wild type enzyme and exhibits 14% of wild type 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
TPMT*2
-
polymorphism, single nucleotide substitution G238C, inactivating mutation
TPMT*3A
-
polymorphism, single nucleotide substitutions, G460A at codon 154 and A719G at codon 240
TPMT*3B
-
polymorphism, single nucleotide substitution G460A, inactivating mutation
TPMT*3C
-
polymorphism, single nucleotide substitution A719G, inactivating mutation
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
-
thiopurine S-methyltransferase polymorphism, A to G transition at position 719
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
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45 - 56
46.8
melting temperature of the wild type enzyme in complex with S-adenosyl-L-methionine
45 - 56
-
heat inactivation, 23% of the activity is lost after 20 min at 45°C, 95% activity is lost after 6 min at 56°C
45 - 56
-
heat inactivation, 23% of the activity is lost after 20 min at 45°C, 95% activity is lost after 6 min at 56°C
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
cytosolic fractions of transformed Saccharomyces cerevisiae cells are prepared
Ni-NTA column chromatography and Superdex 200 gel filtration
using a Ni2+-NTA resin and a gel-filtration column
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
a 8.7 kb fragment encompassing part of exon III through a portion of intron 6 is subcloned into the pZERO-2 vector
-
cDNA cloned and heterologous expressed in rabbit reticulocytes and wheat germ lysate
enhanced green fluorescent protein-tagged enzyme is expressed in Escherichia coli, Jurkat, Hep-G2, and HEK-293 cells
-
expressed in Escherichia coli BL21-Codon Plus (DE3)-RIL cells
into the pCR2.1-TOPO vector, used as a template to generate point mutations, the variants are sequenced and cloned into the mammalian expression vector pCMV6-XL5, into the pENTR/D-TOPO vector and subsequently into the pcDNA-DEST40 vector
-
into the yeast expression vector pYeDP60 for transformation of Saccharomyces cerevisiae cells
the full-length coding region is amplified by PCR from a eukaryotic expression plasmid and cloned into the pET-28a vector for expression in Escherichia coli BL21DE3 cells
to assess the functional effect of the trinucleotide repeat variants in the promoter, the wild-type and variant TPMT promoters are amplified and cloned into the promoter-less pGL3-Basic vector
-
the full-length coding region is amplified by PCR from a eukaryotic expression plasmid and cloned into the pET-28a vector for expression in Escherichia coli BL21DE3 cells
the full-length coding region is amplified by PCR from a eukaryotic expression plasmid and cloned into the pET-28a vector for expression in Escherichia coli BL21DE3 cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
decreased activity of TPMT is associated with hematopoietic toxicity after administration of standard doses of 6- mercaptopurine or azathioprine
-
longitudinal induction of thiopurine methyltransferase activity is observed during 6-thioguanine treatment
-
the restriction of L-methionine in cell growth media reversibly decreases enzyme activity and protein levels
-
TPMT activity is significantly higher in wild type children than in wild type adults (18-68 years), wild type infants from 0.08-5 years has a 9% higher average TPMT activity than the other wild type groups, only in children from 0.08-2 years is the TPMT activity higher in males than in females
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
diagnostics
medicine
analysis
-
determination of thiopurine S-methyltransferase activity in erythrocytes using 6-thioguanine as substrate and a non-extraction liquid chromatographic technique. This method minimzes sample-handling, reduces inherent imprecision, the possibility of laboratory error and with the potential for further automation, makes it ideal for use in a regional refferal laboratory
analysis
-
monitoring of 6-thiopurine S-methyltransferase activity is especially important when patients are treated with 6-thiopurine drugs (drugs in treatment of acute lymphoblastic leukemia), since severe bone marrow toxicity may be induced if patients have deficient 6-thiopurine S-methyltransferase activity. The HPLC-based method enables the rapid screening of 6-6-thiopurine S-methyltransferase activities in patients treated with 6-thiopurines
analysis
-
monitoring of TPMT activity may be of benefit to improve thiopurine therapy
diagnostics
-
the chip-based miniaturization provides a clinically feasible genotyping platform for one-at-a-time testing
diagnostics
-
thiopurine S-methyltransferase genotypes or phenotypes may be a predictive factor for azathioprine-induced toxicities
medicine
-
enzyme may be a target for clinically significant drug interactions, the common genetic polymorphism might be a risk factor for the occurence of therapy-dependent secondary leukemia
medicine
-
enzyme activity might represent one factor responsible for variations in the therapeutic or toxic effects of thiopurine and thiopyrimidine drugs used clinically to treat recipients of transplanted kidneys and patients with renal disease such as glomerulonephritis
medicine
identification of a novel non-functional allele of the thiopurine S-methyltransferase gene enhances the efficiency of genotyping methods to predict patients at risk of an inadequate response to thiopurine therapy
medicine
-
the knowledge of the genetic basis of interindividual variability in thiopurine S-methyltransferase activity could enhance the efficiency of genotyping methods to preduct patients at risk of inadequate response to thiopurine therapy
medicine
-
the knowledge of the genetic basis of interindividual variability in thiopurine S-methyltransferase activity could enhance the efficiency of genotyping methods to product patients at risk of inadequate response to thiopurine therapy
medicine
-
azathioprine sodium is a purine antagonist commonly used as an adjuvant immunosuppressive agent in treating Pemphigus Vulgaris, mercaptopurine is the active compound, TPMT is the principal inactivation enzyme for this cytotoxic metabolite in hematopoietic tissues
medicine
-
detecting TPMT genetic variants before the administration of azathioprine has the potential to prevent serious and costly adverse drug reactions, such as neutropenia
medicine
-
evaluation of a possible long-term effect of mesalazine or azathioprine on thiopurine methyltransferase activity is of particular clinical importance because both drugs can to be given for several years in inflammatory bowel disease
medicine
-
first case of azathioprine-associated AML linked to low thiopurine S-methyltransferase enzyme activity
medicine
-
genetic variation in thiopurine S-methyltransferase is a major factor for wide variation in the metabolism and safety of thiopurine drugs
medicine
-
genotyping at diagnosis identifies patients with a homozygous mutant TPMT and may prevent severe and life-threatening toxicity, ALL treatment monitoring should preferentially be based on repeated determinations of intracellular active metabolites, 6-TGN, and methylated metabolites
medicine
-
individuals with decreased TPMT activity are at great risk for adverse reactions if treated with conventional thiopurine doses
medicine
-
individuals with decreased TPMT activity are at high risk of fatal adverse reactions if treated with conventional thiopurine doses
medicine
-
myelosuppression occurs in 2-7% of inflammatory bowel disease patients treated with azothioprine, and can be associated with reduced activity of thiopurine methyltransferase in some patients
medicine
-
patients carrying a variant genotype have low TPMT activity and produce elevated levels of 6-thioguanine nucleotides in their red blood cells, 6-TGN accumulation may result in azathioprine-induced bone marrow myelosuppression in the course of treatment with the drug in a standard dosage regimen in patients following renal transplantation
medicine
-
patients carrying defective mutations in TMPT gene have elevated thioguanine nucleotides concentrations that finally result in severe or even fatal hematopoietic toxicities when they are treated with standard doses of 6-mercaptopurine
medicine
-
patients with inflammatory bowel disease may have different thiopurine dose requirements in relation to thiopurine methyltransferase genotype or phenotype
medicine
-
polymorphisms at the thiopurine S-methyltransferase coding gene determine enzyme activity and consequently, the development of toxicity secondary to thiopurines
medicine
single nucleotide polymorphisms are known to be responsible for variations in the metabolism of numerous drugs in humans, thiopurine S-methyltransferase displays polymorphisms with varying prevalence among different populations
medicine
-
the goal is to determine which metabolite of azathioprine has the most antiviral activity and to gain a better understanding of how this compound may act in vitro
medicine
-
the goal is to determine which metabolite of azathioprine has the most antiviral activity and to gain a better understanding of how this compound may act in vitro
medicine
-
the knowledge of the TPMT activity distribution in each population seems relevant, the incidence of hematologic adverse effects associated with azathioprine and 6-mercaptopurine treatment probably depends on that distribution
medicine
-
the murine model recapitulates many clinical features of the human polymorphism and provides a preclinical system for establishing safer regimens of genetically influenced antileukemic drug therapy
medicine
-
the remarkable change in enzyme activity of TPMT may be explained by differences in the age of red blood cells, as younger erythrocytes have a higher TPMT activity
medicine
-
the results suggest that coadministration of thiopurines and various nonsteriodal anti-inflammatory drugs may lead to drug interactions
medicine
-
the use of azothioprine and mercaptopurine is limited by toxicity, especially myelosuppression, which is related to activity of the enzyme thiopurine S-methyltransferase
medicine
-
thiopurine methyltransferase activity inversely correlated with clinical response to thiopurine treatment in inflammatory bowel disease
medicine
-
thiopurine methyltransferase is a genetically moderated key enzyme involved in the metabolism of azathioprine that can be used to stratify individuals into different levels of risk of developing neutropaenia
medicine
-
thiopurine methyltransferase is the main enzyme responsible for inactivating toxic products of azathioprine metabolism
medicine
-
thiopurine methyltransferase metabolises thiopurine drugs and influences their cytotoxic activity
medicine
-
thiopurine S-methyltransferase activity is inversely related to the risk of developing severe hematopoietic toxicity in patients treated with azathioprine
medicine
thiopurine S-methyltransferase is a key enzyme in the detoxification of thiopurine drugs widely used in the treatment of various diseases, such as inflammatory bowel diseases, acute lymphoblastic leukaemia and rheumatic diseases
medicine
-
thiopurine S-methyltransferase is an enzyme responsible for the detoxification of the widely used thiopurine drugs
medicine
thiopurine S-methyltransferase modulates the cytotoxic effects of thiopurine prodrugs such as 6-mercaptopurine by methylating them in a reaction using S-adenosyl-L-methionine as the donor
medicine
thiopurine S-methyltransferase modulates the cytotoxic effects of thiopurine prodrugs such as 6-mercaptopurine by methylating them in a reaction using S-adenosyl-L-methionine as the donor
medicine
-
while factors other than TPMT status are likely to be involved in azathioprine toxicity, the majority of evidence suggests that TPMT deficiency is a significant independent risk factor for myelotoxicity
medicine
-
determination of TPMT and monitoring of thiopurine metabolites allows azathioprine treatment to be optimised
medicine
-
induction of thiopurine methyltransferase is associated with recalcitrant disease
medicine
-
mercaptopurine dose can be adjusted on the basis of TPMT genotype to mitigate toxicity in pediatric patients with acute lymphoblastic leukemia
medicine
-
TPMT activity is a good prediction factor for the toxicity and efficacy of the antileukemic thiopurine therapy
medicine
-
low enzyme level can lead to greater sensitivity to thiopurine therapy in astroglial cells
medicine
-
low enzyme level can lead to greater sensitivity to thiopurine therapy in astroglial cells
medicine
-
thiopurine S-methyltransferase gene polymorphisms are pharmacogenetic markers which enable the individualization of thiopurine drug therapy
medicine
-
enzyme polymorphisms are associated with 6-thioguanine levels in patients using azathioprine
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REF.
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JOURNAL
VOL.
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ORGANISM (UNIPROT)
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A single point mutation leading to loss of catalytic activity in human thiopurine S-methyltransferase
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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
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49
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1996
Homo sapiens
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Human thiopurine methyltransferase: no evidence of activation by its substrates
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1997
Homo sapiens
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Fessing, M.Y.; Belkov, V.M.; Krynetski, E.Y.; Evans, W.E.
Molecular cloning and functional characterization of the cDNA encoding the murine thiopurine S-methyltransferase (TPMT)
FEBS Lett.
424
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1998
Homo sapiens, Mus musculus (O55060), Mus musculus
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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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2000
Homo sapiens
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Dervieux, T.; Blanco, J.G.; Krynetski, E.Y.; Vanin, E.F.; Roussel, M.F.; Relling, M.V.
Differing contribution of thiopurine methyltransferase to mercaptopurine versus thioguanine effects in human leukemic cells
Cancer Res.
61
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2001
Homo sapiens, Mus musculus
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Weinshilboum, R.
Thiopurine pharmacogenetics: Clinical and molecular studies of thiopurine methyltransferase
Drug Metab. Dispos.
29
601-605
2001
Homo sapiens
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Keizer-Garritsen, J.J.; Brouwer, C.; Lambooy, L.H.; Ter Riet, P.; Bokkerink, J.P.; Trijbels, F.J.; De Abreu, R.A.
Measurement of thiopurine S-methyltransferase activity in human blood samples based on high-performance liquid chromatography: reference values in erythrocytes from children
Ann. Clin. Biochem.
40
86-93
2003
Homo sapiens
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Hamdan-Khalil, R.; Allorge, D.; Lo-Guidice, J.M.; Cauffiez, C.; Chevalier, D.; Spire, C.; Houdret, N.; Libersa, C.; Lhermitte, M.; Colombel, J.F.; Gala, J.L.; Broly, F.
In vitro characterization of four novel non-functional variants of the thiopurine S-methyltransferase
Biochem. Biophys. Res. Commun.
309
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2003
Homo sapiens
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Hamdan-Khalil, R.; Gala, J.L.; Allorge, D.; Lo-Guidice, J.M.; Horsmans, Y.; Houdret, N.; Broly, F.
Identification and functional analysis of two rare allelic variants of the thiopurine S-methyltransferase gene, TPMT*16 and TPMT*19
Biochem. Pharmacol.
69
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2005
Homo sapiens (P51580), Homo sapiens
brenda
Brouwer, C.; de Abreu, R.A.; Keizer-Garritsen, J.J.; Lambooy, L.H.; Ament, K.; ter Riet, P.G.; van Wering, E.R.; Trijbels, F.J.; Veerman, A.J.; Hoogerbrugge, P.M.; Bokkerink, J.P.
Thiopurine methyltransferase in acute lymphoblastic leukaemia: biochemical and molecular biological aspects
Eur. J. Cancer
41
613-623
2005
Homo sapiens
brenda
Xin, H.W.; Fischer, C.; Schwab, M.; Klotz, U.
Thiopurine S-methyltransferase as a target for drug interactions
Eur. J. Clin. Pharmacol.
61
395-398
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
798
111-115
2003
Homo sapiens
brenda
Winter, J.W.; Gaffney, D.; Shapiro, D.; Spooner, R.J.; Marinaki, A.M.; Sanderson, J.D.; Mills, P.R.
Assessment of thiopurine methyltransferase enzyme activity is superior to genotype in predicting myelosuppression following azathioprine therapy in patients with inflammatory bowel disease
Aliment. Pharmacol. Ther.
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
Aliment. Pharmacol. Ther.
26
1084-1085
2007
Homo sapiens
brenda
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
Aliment. Pharmacol. Ther.
26
737-745
2007
Homo sapiens
brenda
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
brenda
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
brenda
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
Am. J. Hematol.
83
80-83
2008
Homo sapiens
brenda
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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2007
Homo sapiens (P51580)
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Firooz, A.; Ghandi, N.; Hallaji, Z.; Chams-Davatchi, C.; Valikhani, M.; Karbakhsh Davari, M.
Role of thiopurine methyltransferase activity in the safety and efficacy of azathioprine in the treatment of pemphigus vulgaris
Arch. Dermatol.
144
1143-1147
2008
Homo sapiens
brenda
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
Biochem. Pharmacol.
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
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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
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IMPDH activity in thiopurine-treated patients with inflammatory bowel disease - relation to TPMT activity and metabolite concentrations
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65
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Homo sapiens
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Hartford, C.; Vasquez, E.; Schwab, M.; Edick, M.J.; Rehg, J.E.; Grosveld, G.; Pui, C.H.; Evans, W.E.; Relling, M.V.
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67
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Mus musculus
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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
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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
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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
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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
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