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

Influencing the monophenolase/diphenolase activity ratio in tyrosinase.

Biochimica et biophysica acta - 1 Mar 2013

Goldfeder Mor, Kanteev Margarita, Adir Noam, Fishman Ayelet

Abstract excerpt

Tyrosinase is a type 3 copper enzyme with great potential for production of commercially valuable diphenols from monophenols. However, the use of tyrosinase is limited by its further oxidation of diphenols to quinones. We recently determined the structure of the Bacillus megaterium tyrosinase revealing a residue, V218, which we proposed to take part in positioning of substrates within the active site. In the...

Read the complete abstract on PubMed

Topics

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

Share to Bacillus megaterium
Share to Biocatalysis
Share to Catechol Oxidase

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Copper

Share to Ipomoea batatas

Share to Levodopa

Share to Monophenol Monooxygenase

Share to Valine

Source

Identifiers

PMID: 23305929
DOI: 10.1016/j.bbapap.2012.12.021

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

Influencing the monophenolase/diphenolase activity ratio in tyrosinase.PMID 23305929Read ↗

In crystallo activity tests with latent apple tyrosinase and two mutants reveal the importance of the mutated sites for polyphenol oxidase activity.Semantic proximity Read ↗

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

Identification of active site residues involved in metal cofactor binding and stereospecific substrate recognition in Mammalian tyrosinase. Implications to the catalytic cycle.Semantic proximity Read ↗

Identification of the amino acid position controlling the different enzymatic activities in walnut tyrosinase isoenzymes (jrPPO1 and jrPPO2).Semantic proximity Read ↗

Role of the C-terminal extension in a bacterial tyrosinase.Semantic proximity Read ↗

Considerations on activity determinants of fungal polyphenol oxidases based on mutational and structural studiesSemantic proximity Read ↗

Type-3 copper proteins: recent advances on polyphenol oxidases.Semantic proximity Read ↗

The basicity of an active-site water molecule discriminates between tyrosinase and catechol oxidase activity.Semantic proximity Read ↗

Distal design improves thermostability and enzyme activity of type III tyrosinase from Nitrosospira.Semantic proximity Read ↗

Structure of Human Tyrosinase Related Protein 1 Reveals a Binuclear Zinc Active Site Important for Melanogenesis.Semantic proximity Read ↗

Cloning and molecular characterization of a SDS-activated tyrosinase from Marinomonas mediterranea.Semantic proximity Read ↗

Activation Mechanism of the Streptomyces Tyrosinase Assisted by the Caddie Protein.Semantic proximity Read ↗

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