Optimization of Expression and Properties of the Recombinant Acetohydroxyacid Synthase of Thermotoga Maritima

Overview

Journal Data Brief

Date 2015 Dec 3

PMID 26629492

Citations 2

Authors

Mohammad S Eram

Benozir Sarafuddin

Frank Gong

Kesen Ma

Affiliations

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Abstract

The data provide additional support of the characterization of the biophysical and biochemical properties of the enzyme acetohydroxyacid synthase from the hyperthermophilic bacterium Thermotoga maritima (Eram et al., 2015) [1]. The genes encoding the enzyme subunits have been cloned and expressed in the mesophilic host Escherichia coli. Detailed data include information about the optimization of the expression conditions, biophysical properties of the enzyme and reconstitution of the holoenzyme from individually expressed and purified subunits.

Citing Articles

Characterization of acetohydroxyacid synthase from the hyperthermophilic bacterium .

Eram M, Sarafuddin B, Gong F, Ma K Biochem Biophys Rep. 2017; 4:89-97.

PMID: 29124191 PMC: 5668897. DOI: 10.1016/j.bbrep.2015.08.014.

Pyruvate decarboxylase activity of the acetohydroxyacid synthase of .

Eram M, Ma K Biochem Biophys Rep. 2017; 7:394-399.

PMID: 28955930 PMC: 5613635. DOI: 10.1016/j.bbrep.2016.07.008.

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