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 high-voltage paper electrophoresis, paper chromatography and silicic acid chromatography. These results indicate the presence of pyruvate covalently bound through an ester to phosphopantothenoylcysteine decarboxylase which is then another example of a mammalian enzyme in which pyruvate is involved in a catalytic activity.
COVALENTLY BOUND PYRUVATE IN PHOSPHOPANTOTHENOYLCYSTEINE DECARBOXYLASE FROM HORSE LIVER / Scandurra, Roberto; Politi, Laura; L., Santoro; Consalvi, Valerio. - In: FEBS LETTERS. - ISSN 0014-5793. - 212:1(1987), pp. 79-82. [10.1016/0014-5793(87)81560-0]
COVALENTLY BOUND PYRUVATE IN PHOSPHOPANTOTHENOYLCYSTEINE DECARBOXYLASE FROM HORSE LIVER
SCANDURRA, Roberto;POLITI, Laura;CONSALVI, Valerio
1987
Abstract
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 high-voltage paper electrophoresis, paper chromatography and silicic acid chromatography. These results indicate the presence of pyruvate covalently bound through an ester to phosphopantothenoylcysteine decarboxylase which is then another example of a mammalian enzyme in which pyruvate is involved in a catalytic activity.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
