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

Disulfide Bonds Are Not Necessary for Intrinsic TNSALP Activity.

The journal of physical chemistry. B - 2 Mar 2023

Melkonian Arek V, Gilboa Tal, Walt David R

Abstract excerpt

Recent developments in single-molecule enzymology (SME) have allowed for the observation of subpopulations present in enzyme ensembles. Tissue-nonspecific alkaline phosphatase (TNSALP), a homodimeric monophosphate esterase central to bone metabolism, has become a model enzyme for SME studies. TNSALP contains two internal disulfide bonds that are critical for its effective dimerization; mutations in its disulfide...

Read the complete abstract on PubMed

Topics

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

Share to Mutation
Share to Alkaline Phosphatase
Share to Chlorocebus aethiops

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to COS Cells

Share to Disulfides

Share to Hypophosphatasia

Source

Identifiers

PMID: 36795426
DOI: 10.1021/acs.jpcb.2c08392

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Disulfide Bonds Are Not Necessary for Intrinsic TNSALP Activity.PMID 36795426Read ↗

Disulfide bonds are critical for tissue-nonspecific alkaline phosphatase function revealed by analysis of mutant proteins bearing a C(201)-Y or C(489)-S substitution associated with severe hypophosphatasia.Semantic proximity Read ↗

Elucidation and control of low and high active populations of alkaline phosphatase molecules for quantitative digital bioassaySemantic proximity Read ↗

Elucidation and control of low and high active populations of alkaline phosphatase molecules for quantitative digital bioassaySemantic proximity Read ↗

Aberrant interchain disulfide bridge of tissue-nonspecific alkaline phosphatase with an Arg433-->Cys substitution associated with severe hypophosphatasia.Semantic proximity Read ↗

Molecular analysis of SUMF1 mutations: stability and residual activity of mutant formylglycine-generating enzyme determine disease severity in multiple sulfatase deficiency.Semantic proximity Read ↗

An efficient, multiply promiscuous hydrolase in the alkaline phosphatase superfamily.Semantic proximity Read ↗

An asparagine at position 417 of tissue-nonspecific alkaline phosphatase is essential for its structure and function as revealed by analysis of the N417S mutation associated with severe hypophosphatasia.Semantic proximity Read ↗

Structural evidence of functional divergence in human alkaline phosphatases.Semantic proximity Read ↗

Engineered disulfide bonds increase active-site local stability and reduce catalytic activity of a cold-adapted alkaline phosphatase.Semantic proximity Read ↗

Molecular basis of Salla Disease: R39C Mutation Effects on the Lysosomal Transporter SialinSemantic proximity Read ↗

Recognition and ER Quality Control of Misfolded Formylglycine-Generating Enzyme by Protein Disulfide Isomerase.Semantic proximity Read ↗

Kinetic characterization of hypophosphatasia mutations with physiological substrates.Semantic proximity Read ↗

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