Enzymatic Activity of the Arabidopsis Sulfurtransferase Resides in the C-Terminal Domain But Is Boosted by the N-Terminal Domain and the Linker Peptide in the Full- Length Enzyme-Reference-Cited by-同舟云学术

Enzymatic Activity of the Arabidopsis Sulfurtransferase Resides in the C-Terminal Domain But Is Boosted by the N-Terminal Domain and the Linker Peptide in the Full- Length Enzyme

Published:2002-01-17 Issue:9 Volume:383 Page:
ISSN:1431-6730
Container-title:Biological Chemistry
language:
Short-container-title:

Author:

Burow M.,Kessler D.,Papenbrock J.

Publisher

Walter de Gruyter GmbH

Subject

Clinical Biochemistry,Molecular Biology,Biochemistry

Link

https://www.degruyter.com/document/doi/10.1515/BC.2002.155/pdf

Reference36 articles.

1. Properties of an Escherichia coli rhodanese.

2. Rhodanese-Mediated Sulfur Transfer to Succinate Dehydrogenase

3. The crystal structure of a sulfurtransferase from Azotobacter vinelandii highlights the evolutionary relationship between the rhodanese and phosphatase enzyme families

4. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

5. Rhodanese in higher plants

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