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MODIFICATION OF α‐CHYMOTRYPSIN USING A WATER‐SOLUBLE PHOTO‐FENTON REAGENT
Author(s) -
Kitano Hiromi,
Maeda Yasushi,
Furukawa Kanae,
Yamamoto Takahiro,
Izumida Rie,
Matsugo Seiichi
Publication year - 1995
Publication title -
photochemistry and photobiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.818
H-Index - 131
eISSN - 1751-1097
pISSN - 0031-8655
DOI - 10.1111/j.1751-1097.1995.tb09140.x
Subject(s) - reagent , chemistry , chymotrypsin , enzyme kinetics , enzyme , amide , substrate (aquarium) , tryptophan , residue (chemistry) , catalysis , biomolecule , active site , organic chemistry , stereochemistry , combinatorial chemistry , biochemistry , amino acid , trypsin , biology , ecology
— ‐Modification of an enzyme, α‐chymotrypsin, was examined by using a water‐soluble photo‐Fenton reagent. By photoirradiation of the enzyme with the reagent, which can occupy a binding site of the enzyme, a tryptophan residue in the vicinity of the active site was oxidized to N ‐formylkynurenine. Concurrently, the catalytic properties of the enzyme were largely changed: the K m was increased and the k cat was decreased. The decrease in k cat for a specific amide substrate was the most significant among the esters and amides examined. The water‐soluble photo‐Fenton reagent would be useful to chemically modify relatively limited regions in biomolecules.