Determination of tyrosinase substrate-binding modes reveals mechanistic differences between type-3 copper proteins (Q27694659)

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11 March 2020

title

Determination of tyrosinase substrate-binding modes reveals mechanistic differences between type-3 copper proteins (English)

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11 March 2020

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5

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11 March 2020

author name string

Mor Goldfeder

1

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11 March 2020

Margarita Kanteev

2

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11 March 2020

Sivan Isaschar-Ovdat

3

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11 March 2020

Noam Adir

4

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11 March 2020

language of work or name

English

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publication date

30 July 2014

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11 March 2020

published in

Nature Communications

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11 March 2020

volume

5

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11 March 2020

page(s)

4505

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Bacterial tyrosinases: old enzymes with new relevance to biotechnology.

11 March 2020

cites work

1 reference

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New insights into the active site structure and catalytic mechanism of tyrosinase and its related proteins.

21 January 2018

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Structural mechanism of SDS-induced enzyme activity of scorpion hemocyanin revealed by electron cryomicroscopy

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Crystal structure of a plant catechol oxidase containing a dicopper center

21 January 2018

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Crystal structure of Manduca sexta prophenoloxidase provides insights into the mechanism of type 3 copper enzymes

21 January 2018

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Crystallographic evidence that the dinuclear copper center of tyrosinase is flexible during catalysis

21 January 2018

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First structures of an active bacterial tyrosinase reveal copper plasticity

21 January 2018

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Crystal structure of Agaricus bisporus mushroom tyrosinase: identity of the tetramer subunits and interaction with tropolone

21 January 2018

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Tyrosinase: the four oxidation states of the active site and their relevance to enzymatic activation, oxidation and inactivation

21 January 2018

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The inhibition kinetics and thermodynamic changes of tyrosinase via the zinc ion.

21 January 2018

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Structural and mechanistic insights into the oxy form of tyrosinase from molecular dynamics simulations

21 January 2018

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Influencing the monophenolase/diphenolase activity ratio in tyrosinase

21 January 2018

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Copper-O2 reactivity of tyrosinase models towards external monophenolic substrates: molecular mechanism and comparison with the enzyme

21 January 2018

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The mechanism of copper uptake by tyrosinase from Bacillus megaterium

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Structural consequences of effector protein complex formation in a diiron hydroxylase

21 January 2018

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X-ray crystallographic structures of D-xylose isomerase-substrate complexes position the substrate and provide evidence for metal movement during catalysis

21 January 2018

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Ribozyme catalysis revisited: is water involved?

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Active site electronic structure and dynamics during metalloenzyme catalysis.

21 January 2018

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Crystallization and preliminary X-ray crystallographic analysis of a bacterial tyrosinase from Bacillus megaterium

21 January 2018

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Isolation, cloning and characterization of a tyrosinase with improved activity in organic solvents from Bacillus megaterium

21 January 2018

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Solving structures of protein complexes by molecular replacement with Phaser

21 January 2018

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PHENIX: a comprehensive Python-based system for macromolecular structure solution

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Coot: model-building tools for molecular graphics

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The first crystal structure of tyrosinase: all questions answered?

21 January 2018

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inferred from DOI database lookup

7 January 2021

based on heuristic

Comparison of QM-only and QM/MM models for the mechanism of tyrosinase

1 reference

https://api.crossref.org/works/10.1038%2FNCOMMS5505

inferred from DOI database lookup

7 January 2021

based on heuristic

Identifiers

DOI

10.1038/NCOMMS5505

2 references

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

3047676

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:25074014%20AND%20SRC:MED&resulttype=core&format=json

Dimensions Publication ID

11 March 2020

ADS bibcode

2014NatCo...5.4505G

0 references

1023703100

0 references

OpenCitations bibliographic resource ID

3047676

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:25074014%20AND%20SRC:MED&resulttype=core&format=json