Steady-state kinetic analysis of phosphotransacetylase from Methanosarcina thermophila

Sarah H. Lawrence, James G. Ferry

Research output: Contribution to journalArticle

17 Scopus citations

Abstract

Phospliotransacetylase (EC 2.3.1.8) catalyzes the reversible transfer of the acetyl group from acetyl phosphate to coenzyme A (CoA), forming acetyl-CoA and inorganic phosphate. A steady-state kinetic analysis of the phosphotransacetylase from Methanosarcina thermophila indicated that there is a ternary complex kinetic mechanism rather than a ping-pong kinetic mechanism. Additionally, inhibition patterns of products and a nonreactive substrate analog suggested that the substrates bind to the enzyme in a random order. Dynamic light scattering revealed that the enzyme is dimeric in solution.

Original languageEnglish (US)
Pages (from-to)1155-1158
Number of pages4
JournalJournal of bacteriology
Volume188
Issue number3
DOIs
StatePublished - Feb 2006

All Science Journal Classification (ASJC) codes

  • Microbiology
  • Molecular Biology

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