<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Fukui K</submitter><funding>Japan Society for the Promotion of Science</funding><pagination>855-868</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC9199185</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>63(6)</volume><pubmed_abstract>Phosphoribulokinase (PRK), one of the enzymes in the Calvin-Benson cycle, is a well-known target of thioredoxin (Trx), which regulates various enzyme activities by the reduction of disulfide bonds in a light-dependent manner. PRK has two Cys pairs conserved in the N-terminal and C-terminal regions, and the N-terminal one near the active site is thought to be responsible for the regulation. The flexible clamp loop located between the N-terminal two Cys residues has been deemed significant to Trx-mediated regulation. However, cyanobacterial PRK is also subject to Trx-dependent activation despite the lack of this clamp loop. We, therefore, compared Trx-mediated regulation of PRK from the cyanobacterium Anabaena sp. PCC 7120 (A.7120_PRK) and that from the land plant Arabidopsis thaliana (AtPRK</pubmed_abstract><journal>Plant &amp; cell physiology</journal><pubmed_title>The Importance of the C-Terminal Cys Pair of Phosphoribulokinase in Phototrophs in Thioredoxin-Dependent Regulation.</pubmed_title><pmcid>PMC9199185</pmcid><funding_grant_id>KAKENHI Grant Number [16H06556] and [21H02502]</funding_grant_id><pubmed_authors>Yokochi Y</pubmed_authors><pubmed_authors>Sekiguchi T</pubmed_authors><pubmed_authors>Wakabayashi KI</pubmed_authors><pubmed_authors>Mihara S</pubmed_authors><pubmed_authors>Fukui K</pubmed_authors><pubmed_authors>Yoshida K</pubmed_authors><pubmed_authors>Hisabori T</pubmed_authors></additional><is_claimable>false</is_claimable><name>The Importance of the C-Terminal Cys Pair of Phosphoribulokinase in Phototrophs in Thioredoxin-Dependent Regulation.</name><description>Phosphoribulokinase (PRK), one of the enzymes in the Calvin-Benson cycle, is a well-known target of thioredoxin (Trx), which regulates various enzyme activities by the reduction of disulfide bonds in a light-dependent manner. PRK has two Cys pairs conserved in the N-terminal and C-terminal regions, and the N-terminal one near the active site is thought to be responsible for the regulation. The flexible clamp loop located between the N-terminal two Cys residues has been deemed significant to Trx-mediated regulation. However, cyanobacterial PRK is also subject to Trx-dependent activation despite the lack of this clamp loop. We, therefore, compared Trx-mediated regulation of PRK from the cyanobacterium Anabaena sp. PCC 7120 (A.7120_PRK) and that from the land plant Arabidopsis thaliana (AtPRK</description><dates><release>2022-01-01T00:00:00Z</release><publication>2022 Jun</publication><modification>2026-04-08T10:32:04.02Z</modification><creation>2025-02-19T02:57:26.314Z</creation></dates><accession>S-EPMC9199185</accession><cross_references><pubmed>35413120</pubmed><doi>10.1093/pcp/pcac050</doi></cross_references></HashMap>