Work

An NADH-Dependent Acetoacetyl-CoA Reductase from Euglena gracilis

Year: 1986

Type: article

Abstract: An NADH-dependent acetoacetyl-CoA reductase from Euglena gracilis variety bacillaris was extensively purified and characterized. Two different isoelectric forms of the reductase with identical characteristics otherwise were found. The reductase was noncompetitively inhibited by acyl carrier protein, K(i) 5.6 micromolar at pH 5.4; this inhibition decreased with increasing pH or ionic strength. Coenzyme A was a competitive inhibitor, K(i) 230 micromolar. Kinetic parameters with respect to acetoacetyl-CoA and NADH were sensitive to changes in pH and ionic strength.

Source: PLANT PHYSIOLOGY

DOI: 10.1104/pp.82.4.978

Author: Mary Lou Ernst-Fonberg

Institution: East Tennessee State University

Language: English

Topic: Lipid metabolism and biosynthesis

Subfield: Biochemistry

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funder: National Science Foundation

OpenAlex ID: W2047123670