This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Lawrence, S. H.
Right arrow Articles by Ferry, J. G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Lawrence, S. H.
Right arrow Articles by Ferry, J. G.

 Previous Article  |  Next Article 

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.



This article has been cited by other articles:

  • Lawrence, S. H., Luther, K. B., Schindelin, H., Ferry, J. G. (2006). Structural and Functional Studies Suggest a Catalytic Mechanism for the Phosphotransacetylase from Methanosarcina thermophila. J. Bacteriol. 188: 1143-1154 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»