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

G. S Jagannatha Rao, David E. Coleman, G. Kulkarni, E. J. Goldsmith, Paul F. Cook, Ben G. Harris

Research output: Contribution to journalArticle

10 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)297-304
Number of pages8
JournalProtein and Peptide Letters
Volume7
Issue number5
StatePublished - Dec 1 2000

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry

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    Rao, G. S. J., Coleman, D. E., Kulkarni, G., Goldsmith, E. J., Cook, P. F., & Harris, B. G. (2000). NAD-Malic Enzyme from Ascaris suum: Sequence and Structural Studies. Protein and Peptide Letters, 7(5), 297-304.