Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Roles of cysteinyl residues of phosphoribulokinase as examined by site-directed mutagenesis.

The Journal of biological chemistry - 5 Jun 1991

Milanez S, Mural R J, Hartman F C

Abstract excerpt

The Calvin Cycle enzyme phosphoribulokinase is activated in higher plants by the reversible reduction of a disulfide bond, which is located at the active site. To determine the possible contribution of the two regulatory residues (Cys16 and Cys55) to catalysis, site-directed mutagenesis has been used to replace each of them in the spinach enzyme with serine or alanine. The only other cysteinyl residues of the...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Base Sequence
Share to Blotting, Western
Share to DNA

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Electrophoresis, Polyacrylamide Gel

Share to Kinetics

Share to Molecular Sequence Data

Share to Mutagenesis, Site-Directed

Share to Mutation

Source

Identifiers

PMID: 1645355

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Roles of cysteinyl residues of phosphoribulokinase as examined by site-directed mutagenesis.PMID 1645355Read ↗

Oxidation-reduction properties of the regulatory site of spinach phosphoribulokinase.Semantic proximity Read ↗

C172S substitution in the chloroplast-encoded large subunit affects stability and stress-induced turnover of ribulose-1,5-bisphosphate carboxylase/oxygenase.Semantic proximity Read ↗

Characterization of Chlamydomonas Ribulose-1,5-bisphosphate carboxylase/oxygenase variants mutated at residues that are post-translationally modified.Semantic proximity Read ↗

Structure/function analysis of a critical disulfide bond in the active site of L-xylulose reductase.Semantic proximity Read ↗

Chloroplast fructose 1,6-bisphosphatase with changed redox modulation: comparison of the Galdieria enzyme with cysteine mutants from spinach.Semantic proximity Read ↗

Gene-enzyme relationship in the sulfate assimilation pathway of Saccharomyces cerevisiae. Study of the 3'-phosphoadenylylsulfate reductase structural gene.Semantic proximity Read ↗

Kinetic characterization of Synechocystis sp. PCC6803 1-deoxy-D-xylulose 5-phosphate reductoisomerase mutants.Semantic proximity Read ↗

Structural and functional consequences of the replacement of proximal residues Cys(172) and Cys(192) in the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase from Chlamydomonas reinhardtii.Semantic proximity Read ↗

Structural and functional roles of cysteine 90 and cysteine 240 in S-adenosylmethionine synthetase.Semantic proximity Read ↗

Structural analysis of the regulatory dithiol-containing domain of the chloroplast ATP synthase gamma subunit.Semantic proximity Read ↗

Mutation of the regulatory phosphorylation site of tobacco nitrate reductase results in constitutive activation of the enzyme in vivo and nitrite accumulation.Semantic proximity Read ↗

Biochemical and X-ray crystallographic studies on shikimate kinase: the important structural role of the P-loop lysine.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.