Covalently bound pyruvate in phosphopantothenoylcysteine decarboxylase from horse liver

FEBS Letters

Scandurra, R.¹  Consalvi, V.²  Santoro, L.¹  Politi, L.¹ 

[1] Deparment of Biochemical Sciences, University ‘La Sapienza’, Roma, Italy;Deparment of Biomedical Sciences, University ‘La Sapienza’, L'Aquila, Italy

关键词: Phosphopantothenoylcysteine;    Decarboxylase;    Pyruvate;    (Horse liver);   

DOI  :  10.1016/0014-5793(87)81560-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown