Isotope effects in the study of enzymatic phosphoryl transfer reactions (Q34317886)

1 August 2017

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title

Isotope effects in the study of enzymatic phosphoryl transfer reactions (English)

1 reference

1 August 2017

A C Hengge

1

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PubMed ID

11470264

1 August 2017

language of work or name

English

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publication date

1 July 2001

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1 August 2017

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1 August 2017

501

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1 August 2017

2-3

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1 August 2017

99-102

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Protein kinases and phosphatases: the yin and yang of protein phosphorylation and signaling

1 August 2017

1 reference

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Crystal structure of Yersinia protein tyrosine phosphatase at 2.5 A and the complex with tungstate

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902638-2

Nature of the transition state of the protein-tyrosine phosphatase-catalyzed reaction

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902638-2

Effects on general acid catalysis from mutations of the invariant tryptophan and arginine residues in the protein tyrosine phosphatase from Yersinia

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902638-2

A ligand-induced conformational change in the Yersinia protein tyrosine phosphatase

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902638-2

Isotope effects on the mechanism of calcineurin catalysis: kinetic solvent isotope and isotope exchange studies

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902638-2

Isotope effect studies on the calcineurin phosphoryl-transfer reaction: transition state structure and effect of calmodulin and Mn2+.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902638-2

Comparison of the reaction progress of calcineurin with Mn2+ and Mg2+.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902638-2

Kinetic and spectroscopic analyses of mutants of a conserved histidine in the metallophosphatases calcineurin and lambda protein phosphatase.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902638-2

Structure of the bacteriophage lambda Ser/Thr protein phosphatase with sulfate ion bound in two coordination modes

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902638-2

The quest for free metaphosphate in solution. Racemization at phosphorus in the transfer of the phospho group from aryl phosphate monoesters to tert-butyl alcohol in acetonitrile or in tert-butyl alcohol

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902638-2

Catalysis of the hydrolysis of phosphorylated pyridines by Mg(OH)+: a possible model for enzymatic phosphoryl transfer

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902638-2

Pyruvate kinase: is the mechanism of phospho transfer associative or dissociative?

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902638-2

Transition-state structures for the native dual-specific phosphatase VHR and D92N and S131A mutants. Contributions to the driving force for catalysis

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902638-2

Examination of the transition state of the low-molecular mass small tyrosine phosphatase 1. Comparisons with other protein phosphatases

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902638-2

Alkaline phosphatase is an almost perfect enzyme

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902638-2

Structure, mechanism, and specificity of protein-tyrosine phosphatases

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902638-2

inferred from DOI database lookup

7 January 2021

based on heuristic

Identifiers

DOI

10.1016/S0014-5793(01)02638-2

1 reference

1 August 2017

1 reference

PubMed ID

11470264