Steady-state kinetic analysis of phosphotransacetylase from Methanosarcina thermophila

Sarah H. Lawrence, James Gregory Ferry

Research output: Contribution to journalArticle

16 Citations (Scopus)

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 1 2006

Fingerprint

Phosphate Acetyltransferase
Methanosarcina
Acetyl Coenzyme A
Enzymes
Coenzyme A
Phosphates

All Science Journal Classification (ASJC) codes

  • Applied Microbiology and Biotechnology
  • Immunology

Cite this

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Steady-state kinetic analysis of phosphotransacetylase from Methanosarcina thermophila. / Lawrence, Sarah H.; Ferry, James Gregory.

In: Journal of bacteriology, Vol. 188, No. 3, 01.02.2006, p. 1155-1158.

Research output: Contribution to journalArticle

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AB - 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.

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