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Q52560036-8C0F90E9-9495-427E-8D67-76009F170C8C
Q52560036-8C0F90E9-9495-427E-8D67-76009F170C8C
BestRank
Statement
http://www.wikidata.org/entity/statement/Q52560036-8C0F90E9-9495-427E-8D67-76009F170C8C
Catalytic mechanism and role of hydroxyl residues in the active site of theta class glutathione S-transferases. Investigation of Ser-9 and Tyr-113 in a glutathione S-transferase from the Australian sheep blowfly, Lucilia cuprina.
P2860
Q52560036-8C0F90E9-9495-427E-8D67-76009F170C8C
BestRank
Statement
http://www.wikidata.org/entity/statement/Q52560036-8C0F90E9-9495-427E-8D67-76009F170C8C
rank
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type
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wasDerivedFrom
cff7e21e8d06ae602a737f8a83d0a21934bf6f6a
P2860
Mutagenesis of the active site of the human Theta-class glutathione transferase GSTT2-2: catalysis with different substrates involves different residues.