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Covalently bound pyruvate in phosphopantothenoylcysteine decarboxylase from horse liver
Author(s) -
Scandurra R.,
Politi L.,
Santoro L.,
Consalvi V.
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)81560-0
Subject(s) - chemistry , covalent bond , tritium , biochemistry , substrate (aquarium) , pyruvate decarboxylase , enzyme , silicic acid , pyruvate decarboxylation , chromatography , hydrolysis , pyruvate dehydrogenase complex , organic chemistry , biology , ecology , physics , nuclear physics , alcohol dehydrogenase
Horse liver phosphopantothenoylcysteine decarboxylase (EC 4.1.1.36) incorporates nonexchangeable tritium from borotritide with a decrease of the activity. Substrate prevents both tritium incorporation and the decrease in activity. Acid and base hydrolysis of the tritiated protein releases labeled lactate identified by highvoltage paper electrophoresis, paper chromatography and silicic acid chromatography. These results indicate the presence of pyruvate covalently bound through an ester linkage to phosphopantothenoylcysteine decarboxylase which is then another example of a mammalian enzyme in which pyruvate is involved in a catalytic activity.