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Journal of Bacteriology, February 2006, p. 1155-1158, Vol. 188, No. 3
0021-9193/06/$08.00+0     doi:10.1128/JB.188.3.1155-1158.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Steady-State Kinetic Analysis of Phosphotransacetylase from Methanosarcina thermophila

Sarah H. Lawrence{dagger} and James G. Ferry*

Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802-4500

Received 15 September 2005/ Accepted 14 November 2005

Phosphotransacetylase (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.

* Corresponding author. Mailing address: Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA 16802-4500. Phone: (814) 863-5721. Fax: (814) 863-6217. E-mail: jgf3{at}psu.edu.

{dagger} Present address: Fox Chase Cancer Center, Philadelphia, PA 19111-2497.

Journal of Bacteriology, February 2006, p. 1155-1158, Vol. 188, No. 3
0021-9193/06/$08.00+0     doi:10.1128/JB.188.3.1155-1158.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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