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

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 journal › Article › peer-review

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 language	English (US)
Pages (from-to)	297-304
Number of pages	8
Journal	Protein and Peptide Letters
Volume	7
Issue number	5
State	Published - Dec 1 2000

ASJC Scopus subject areas

Structural Biology
Biochemistry

Cite this

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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.",

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T1 - NAD-Malic Enzyme from Ascaris suum

T2 - Sequence and Structural Studies

AU - Rao, G. S Jagannatha

AU - Coleman, David E.

AU - Kulkarni, G.

AU - Goldsmith, E. J.

AU - Cook, Paul F.

AU - Harris, Ben G.

PY - 2000/12/1

Y1 - 2000/12/1

N2 - 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.

AB - 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.

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JO - Protein and Peptide Letters

JF - Protein and Peptide Letters

IS - 5

ER -

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

Abstract

ASJC Scopus subject areas

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