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

Exploring O-acetylserine sulfhydrylase-B isoenzyme from Salmonella typhimurium by fluorescence spectroscopy.

Archives of biochemistry and biophysics - 15 Jan 2011

Salsi Enea, Guan Rong, Campanini Barbara, Bettati Stefano, Lin Jianling, Cook Paul F, Mozzarelli Andrea

Abstract excerpt

The pyridoxal 5'-phosphate (PLP)-dependent enzyme O-acetylserine sulfhydrylase (OASS) catalyzes the synthesis of cysteine in bacteria and plants. In bacteria two isoenzymes are present, OASS-A and OASS-B, with distinct structural, functional, and regulatory properties. In order to gain a deeper i...

Read the complete abstract on PubMed

Topics

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

Share to Isoenzymes
Share to Kinetics
Share to Lyases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutagenesis, Site-Directed

Share to Protein Conformation

Share to Salmonella typhimurium

Share to Spectrometry, Fluorescence

Share to Substrate Specificity

Source

Identifiers

PMID: 20937239
DOI: 10.1016/j.abb.2010.10.005

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-20937239-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Exploring O-acetylserine sulfhydrylase-B isoenzyme from Salmonella typhimurium by fluorescence spectroscopy.PMID 20937239Read ↗

Tryptophan luminescence as a probe of enzyme conformation along the O-acetylserine sulfhydrylase reaction pathway.Semantic proximity Read ↗

Role of conserved active site tryptophan-101 in functional activity and stability of phosphoserine aminotransferase from an enteric human parasite.Semantic proximity Read ↗

Spectroscopic studies of the AppA BLUF domain from Rhodobacter sphaeroides: addressing movement of tryptophan 104 in the signaling state.Semantic proximity Read ↗

Identification of the structural determinants for the stability of substrate and aminoacrylate external Schiff bases in O-acetylserine sulfhydrylase-A.Semantic proximity Read ↗

Three-dimensional structure of a new enzyme, O-phosphoserine sulfhydrylase, involved in l-cysteine biosynthesis by a hyperthermophilic archaeon, Aeropyrum pernix K1, at 2.0A resolution.Semantic proximity Read ↗

Fluorescence spectroscopy of soluble E. coli SPase I Δ2-75 reveals conformational changes in response to ligand binding.Semantic proximity Read ↗

Energy landscape of the intact and destabilized FMO antennas from C. tepidum and the L122Q mutant: Low temperature spectroscopy and modeling study.Semantic proximity Read ↗

Effect of mutation of lysine-120, located at the entry to the active site of O-acetylserine sulfhydrylase-A from Salmonella typhimurium.Semantic proximity Read ↗

Molecular basis of cysteine biosynthesis in plants: structural and functional analysis of O-acetylserine sulfhydrylase from Arabidopsis thaliana.Semantic proximity Read ↗

Structure-based mutational studies of O-acetylserine sulfhydrylase reveal the reason for the loss of cysteine synthase complex formation in Brucella abortus.Semantic proximity Read ↗

Essential roles of buried phenylalanine in the structural stability of thioredoxin from a psychrophilic Arctic bacterium Sphingomonas sp.Semantic proximity Read ↗

Copper-sulfenate complex from oxidation of a cavity mutant of Pseudomonas aeruginosa azurin.Semantic proximity Read ↗

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