English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Sulfurtransferases/rhodaneses are a group of enzymeswidely distributed in plants, animals, and bacteria that catalyze the transferof sulfur from a donor molecule to a thiophilic acceptor substrate.Sulfurtransferases (STs) consist of two globular domains of nearly identicalsize and conformation connected by a short linker sequence. In plant STs thislinker sequence is exceptionally longer than in sequences from other species.The Arabidopsis ST1 protein (AJ131404) contains five cysteine residues: oneresidue is universally conserved in all STs and considered to be catalyticallyessential; a second one, closely located in the primary sequence, is conservedonly in sequences from eukaryotic species. Of the remaining three cysteineresidues two are conserved in the so far known plant STs and one is unique tothe Arabidopsis ST1. The aim of our study was to investigate the role of thetwodomain structure, of the unique plant linker sequence and of each cysteineresidue. The N and Cterminal domains of the Arabidopsis ST1, the fulllengthprotein with a shortened linker sequence and several pointmutated proteins wereoverexpressed in E. coli, purified and used for enzyme activity measurements.The Cterminal domain itself displayed ST activity which could be increased byadding the separately prepared Nterminal domain. The activity of an ST1derivative with a shortened linker sequence was reduced by more than 60% of thewildtype activity, probably because of a drastically reduced protein stability.The replacement of each cysteine residue resulted in mutant forms whichdiffered significantly in their stability, in the specific ST activities, andin their kinetic parameters which were determined for 3-mercaptopyruvate aswell as thiosulfate as sulfur substrates: mutation of the putative active sitecysteine (C332) essentially abolished activity; for C339 a crucial role atleast for the turnover of thiosulfate could be identified.

biological chemistry

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