Structural studies of a human malic enzyme

Zhiru      Yang; Liang      Tong

doi:10.2174/092986650705221207142319

Abstract

Structural studies of the human mitochondrial NAD(Pt-dependent malic enzyme (m-NAD-ME) establish that malic enzymes belong to a new class of oxidative decarboxylases: An open and a closed form of the enzyme have been observed from the crystallographic analysis, with the closed form also revealing the binding modes of the divalent cation and the transition-state analog inhibitor oxalate. The structures show that E255, D256 and D279 are the ligands of the cation, and suggest that Y112 and K183 may be the catalytic residues of the enzyme.

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Protein & Peptide Letters

Title:Structural studies of a human malic enzyme

Volume: 7 Issue: 5

Author(s): Zhiru Yang and Liang Tong*

Affiliation:

Department of Biological Sciences, Columbia University, New York, NY 10027, USA

Abstract: Structural studies of the human mitochondrial NAD(Pt-dependent malic enzyme (m-NAD-ME) establish that malic enzymes belong to a new class of oxidative decarboxylases: An open and a closed form of the enzyme have been observed from the crystallographic analysis, with the closed form also revealing the binding modes of the divalent cation and the transition-state analog inhibitor oxalate. The structures show that E255, D256 and D279 are the ligands of the cation, and suggest that Y112 and K183 may be the catalytic residues of the enzyme.

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Yang Zhiru and Tong Liang*, Structural studies of a human malic enzyme, Protein & Peptide Letters 2000; 7 (5) . https://dx.doi.org/10.2174/092986650705221207142319

DOI https://dx.doi.org/10.2174/092986650705221207142319	Print ISSN 0929-8665
Publisher Name Bentham Science Publisher	Online ISSN 1875-5305