NAD-Malic Enzyme from Ascaris suum: Sequence and Structural Studies

Title:NAD-Malic Enzyme from Ascaris suum: Sequence and Structural Studies

Volume: 7 Issue: 5

Author(s): G.S. Jagannatha Rao, David E. Coleman, G. Kulkarni, E.J. Goldsmith, Paul F. Cook and Ben G. Harris*

Affiliation:

• Department of Molecular Biology and Immunology, University of North Texas Health Science Center, Fort Worth, TX 76107, Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX 75206, and Department of Chemistry and Biochemistry, University of Oklahoma, Norman, OK 73019

Abstract: Ascaris suum malic enzyme belongs to the class of oxidative decarboxylases and converts L-malate to pyruvate utilizing NAD and a divalent metal cofactor. It plays a key role in the energy metabolism of the parasite and hence is a target for chemotherapy. It has been extensively characterized from the standpoint of its kinetic, regulatory and chemical mechanisms. Recent studies involving site specific mutants and the determination of its complete sequence as well as quaternary structure have greatly facilitated elucidation of its catalytic mechanism.

Cite this article as:

Rao Jagannatha G.S., Coleman E. David, Kulkarni G., Goldsmith E.J., Cook F. Paul and Harris G. Ben*, NAD-Malic Enzyme from Ascaris suum: Sequence and Structural Studies, Protein & Peptide Letters 2000; 7 (5) . https://dx.doi.org/10.2174/092986650705221207142546

DOI https://dx.doi.org/10.2174/092986650705221207142546	Print ISSN 0929-8665
Publisher Name Bentham Science Publisher	Online ISSN 1875-5305