Pig liver phosphomevalonate kinase. 1. Purification and properties

Sergio Bazaes, Enrique Beytía, Ana María Jabalquinto, Francisco Solís De Ovando, Isabel Gómez, Jaime Eyzaguirre

Research output: Contribution to journalArticlepeer-review

21 Citations (Scopus)

Abstract

Pig liver phosphomevalonate kinase (EC 2.7.4.2) has been purified to homogeneity as shown by polyacrylamide gel electrophoresis. The molecular weight estimates range from 21 000 to 22 500. Each molecule is composed of one polypeptide chain. The presence of SH-containing reagents is essential for the preservation of enzyme activity at all steps in the purification. The enzyme shows absolute specificity for ATP and requires for activity a divalent metal cation, Mg2+ being most effective. The optimum pH for the enzyme ranges from 7.5 to over 9.5. Kinetics are hyperbolic for both substrates, showing a sequential mechanism; true Km values of 0.075 mM and 0.46 mM have been obtained for phosphomevalonate and ATP, respectively. Amino acid composition shows a high content of acid amino acids, one cysteine residue per molecule of enzyme, and the absence of methionine. The results obtained suggest that the enzyme plays no regulatory function in cholesterol biosynthesis in pig liver, although a variable enzyme content was detected in different livers.

Original languageEnglish
Pages (from-to)2300-2304
Number of pages5
JournalBiochemistry
Volume19
Issue number11
Publication statusPublished - 1980

ASJC Scopus subject areas

  • Biochemistry

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