Purification and characterization of avian liver mevalonate-5-pyrophosphate decarboxylase

Marysol Alvear, Ana María Jabalquinto, Jaime Eyzaguirre, Emilio Cardemil

Research output: Contribution to journalArticlepeer-review

37 Citations (Scopus)

Abstract

Mevalonate-5-pyrophosphate decarboxylase [ATP:5-diphosphomevalonate carboxy-lyase (dehydrating), EC 4.1.1.33] has been purified 5800 times from chicken liver and obtained in a stable and highly purified form. The protein is a dimer of molecular weight 85 400 ± 1941, and its subunits were not resolved by gel electrophoresis in denaturing conditions. The purified enzyme does not require the presence of SH-containing reagents for either activity or stability. The enzyme shows a high specificity for adenosine 5′-triphosphate (ATP) and requires for activity a divalent metal cation, Mg2+ being most effective. The optimum pH for the enzyme ranges from 4.0 to 6.5. Inhibitory effects for the enzyme activity were detected by citrate, phthalate, and phosphate. The isoelectric point, as determined by column chromatofocusing, is 4.8. The kinetics are hyperbolic for both substrates, showing a sequential mechanism; true Km values of 0.0141 mM and 0.504 mM have been obtained for mevalonate-5-pyrophosphate and ATP, respectively.

Original languageEnglish
Pages (from-to)4646-4650
Number of pages5
JournalBiochemistry
Volume21
Issue number19
Publication statusPublished - 1982

ASJC Scopus subject areas

  • Biochemistry

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