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

Human Tyrosinase: Temperature-Dependent Kinetics of Oxidase Activity.

International journal of molecular sciences - 30 Jan 2020

Young Kenneth L, Kassouf Claudia, Dolinska Monika B, Anderson David Eric, Sergeev Yuri V

Abstract excerpt

Human tyrosinase (Tyr) is involved in pigment biosynthesis, where mutations in its corresponding gene TYR have been linked to oculocutaneous albinism 1, an autosomal recessive disorder. Although the enzymatic capabilities of Tyr have been well-characterized, the thermodynamic driving forces underlying melanogenesis remain unknown. Here, we analyze protein binding using the diphenol oxidase behavior of Tyr and van...

Read the complete abstract on PubMed

Topics

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

Share to Dihydroxyphenylalanine
Share to Kinetics
Share to Monophenol Monooxygenase

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutation

Share to Oxidoreductases

Share to Protein Binding

Share to Temperature

Source

Open in PubMed Open full text

Identifiers

PMID: 32019134
DOI: 10.3390/ijms21030895
PMCID: PMC7037427

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Human Tyrosinase: Temperature-Dependent Kinetics of Oxidase Activity.PMID 32019134Read ↗

Characterization of Temperature-Dependent Kinetics of Oculocutaneous Albinism-Causing Mutants of Tyrosinase.Semantic proximity Read ↗

Analysis of Immobilized Protein Unfolding and Molecular Dynamics Shows How pH, Glycosylation, and OCA3-Related Variants Influence Tyrp1's Stability and Function.Semantic proximity Read ↗

Mutational analysis of TYR gene and its structural consequences in OCA1A.Semantic proximity Read ↗

Ampyrone (4-Aminoantipyrine) is a Direct Agonist of Human Tyrosinase and Potential Therapeutic for Oculocutaneous Albinism and Disorders of HypopigmentationSemantic proximity Read ↗

Structure and Function of Human Tyrosinase and Tyrosinase-Related Proteins.Semantic proximity Read ↗

Computational analysis of histidine mutations on the structural stability of human tyrosinases leading to albinism insurgence.Semantic proximity Read ↗

Structural insight with mutational impact on tyrosinase and PKC-β interaction from Homo sapiens: Molecular modeling and docking studies for melanogenesis, albinism and increased risk for melanoma.Semantic proximity Read ↗

Insights from Computational Dynamic Active Site Mapping into Substrate Recognition and Mutation-Induced Dysfunction in Human Tyrosinase.Semantic proximity Read ↗

Albinism-causing mutations in recombinant human tyrosinase alter intrinsic enzymatic activity.Semantic proximity Read ↗

The inhibition effect of starch nanoparticles on tyrosinase activity and its mechanism.Semantic proximity Read ↗

Computational analysis of the deleterious non-synonymous single nucleotide polymorphisms (nsSNPs) in TYR gene impacting human tyrosinase protein and the protein stability.Semantic proximity Read ↗

In silico screening and molecular dynamics simulation of disease-associated nsSNP in TYRP1 gene and its structural consequences in OCA3.Semantic proximity Read ↗

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