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

Rational Design of a Yeast-derived 3',5'-bisphosphate Nucleotidase with Improved Substrate Specificity.

The Journal of general and applied microbiology - 6 Nov 2024

Jiang Jipeng, Sun Yanqing, Sun Yanan, Lu Fuping, Liu Fufeng, Zhang Huitu

Abstract excerpt

In recent years, a convenient phosphatase-coupled sulfotransferase assay method has been proven to be applicable to most sulfotransferases. The central principle of the method is that phosphatase specifically degrades 3'-phosphoadenosine-5'-phosphate (PAP) and leaves 3'-phosphoadenosine-5'-phosphosulfate (PAPS). Our group previously acquired a yeast 3',5'-bisphosphate nucleotidase (YND), which showed a higher...

Read the complete abstract on PubMed

Topics

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

Share to Adenosine Diphosphate
Share to Arylsulfotransferase

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Catalytic Domain

Share to Mutation

Share to Saccharomyces cerevisiae

Share to Substrate Specificity

Source

Identifiers

PMID: 38897942
DOI: 10.2323/jgam.2024.05.006

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Rational Design of a Yeast-derived 3',5'-bisphosphate Nucleotidase with Improved Substrate Specificity.PMID 38897942Read ↗

Crystal structures of SULT1A2 and SULT1A1 *3: insights into the substrate inhibition and the role of Tyr149 in SULT1A2.Semantic proximity Read ↗

The molecular basis for the broad substrate specificity of human sulfotransferase 1A1.Semantic proximity Read ↗

From sequence and structure of sulfotransferases and dihydropyrimidinases to an understanding of their mechanisms of action and function.Semantic proximity Read ↗

Structural and Dynamic Characterizations Highlight the Deleterious Role of SULT1A1 R213H Polymorphism in Substrate Binding.Semantic proximity Read ↗

Pharmacogenetics of soluble sulfotransferases (SULTs).Semantic proximity Read ↗

Human HAD phosphatases: structure, mechanism, and roles in health and diseaseSemantic proximity Read ↗

Mechanism of sulfotransferase pharmacogenetics in altered xenobiotic metabolism.Semantic proximity Read ↗

Crystal structures of herbicide-detoxifying esterase reveal a lid loop affecting substrate binding and activity.Semantic proximity Read ↗

Resequencing the sulfotransferase SULT1 gene provides new insights, while illuminating challenges that lie ahead for pharmacogenomics.Semantic proximity Read ↗

Rational engineering of a native hyperthermostable lactonase into a broad spectrum phosphotriesterase.Semantic proximity Read ↗

Amino acid residue 247 in canine sulphotransferase SULT1D1: a new determinant of substrate selectivity.Semantic proximity Read ↗

Bioinformatic analysis of sulfotransferases from an unexplored gut microbe, <i>Sutterella wadsworthensis 3_1_45B</i> : Possible roles towards detoxification via sulfation by the members of the human gut microbiomeSemantic proximity Read ↗

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