当前位置： SCI文献检索 > INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES期刊下所有文献 > Biochemical and biophysical characterization of a mycoredoxin protein glutaredoxin A1 from Corynebacterium pseudotuberculosis.

Biochemical and biophysical characterization of a mycoredoxin protein glutaredoxin A1 from Corynebacterium pseudotuberculosis.

Abstract：

:Glutaredoxin A1 from Corynebacterium pseudotuberculosis was shown to be a mycoredoxin protein. In this study, we established a process to overexpress and purify glutaredoxin A1. The aim of this study was the investigation of the Glutaredoxin A1 from C. pseudotuberculosis behavior under different redox environments and the identification of lead molecules, which can be used for specific inhibitor development for this protein family. A quantitative assay was performed measuring the rate of insulin reduction spectrophotometrically at 640nm through turbidity formation from the precipitation of the free insulin. Glutaredoxin A1, at 5μM concentration, accelerated the reduction process of 0.2mM insulin and 1mM DTT. The pH optimum of the reaction was 7.4. In the presence of DTT and ESH the glutaredoxin A1 presents similar activity, and its activity is reduced by 50% in the presence of GSH. Additional function for ESH in the redox metabolism of C. pseudotuberculosis is suggested. A combined STD and Chemical Shift - NMR approach was employed to study the effects of potential inhibitors on the structure of glutaredoxin A1 from Corynebacterium pseudotuberculosis. The inhibitory potential of four ligands (heparin, suramin, hesperetin - Hst, and hesperidin - Hsp) against glutaredoxin A1 is discussed.

journal_name

Int J Biol Macromol

journal_title

International journal of biological macromolecules

authors

Eberle RJ,Kawai LA,de Moraes FR,Tasic L,Arni RK,Coronado MA

doi

10.1016/j.ijbiomac.2017.10.063

subject

Has Abstract

pub_date

2018-02-01 00:00:00

pages

1999-2007

issue

Pt B

eissn

0141-8130

issn

1879-0003

pii

S0141-8130(17)32733-2

journal_volume

107

pub_type

杂志文章

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