Arginine Coordination in Enzymatic Phosphoryl Transfer: Evaluation of the Effect of Arg166 Mutations in Escherichia coli Alkaline Phosphatase † ‡ (Q27651199)

From Wikidata

Jump to navigation Jump to search

scientific article

Language	Label	Description	Also known as
English	Arginine Coordination in Enzymatic Phosphoryl Transfer: Evaluation of the Effect of Arg166 Mutations in Escherichia coli Alkaline Phosphatase † ‡	scientific article

Statements

scholarly article

0 references

Arginine Coordination in Enzymatic Phosphoryl Transfer: Evaluation of the Effect of Arg166 Mutations in Escherichia coli Alkaline Phosphatase † ‡ (English)

0 references

Escherichia coli

1 reference

based on heuristic

inferred from title

Daniel Herschlag

5

0 references

Jesse G. Zalatan

object named as

Jesse G Zalatan

4

0 references

author name string

Patrick J O'Brien

1

0 references

Jonathan Kyle Lassila

2

0 references

Timothy D Fenn

3

0 references

language of work or name

0 references

publication date

22 July 2008

0 references

0 references

47

0 references

29

0 references

7663-72

0 references

Alkaline phosphatase mono- and diesterase reactions: comparative transition state analysis

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2587100

20 March 2017

A revised mechanism for the alkaline phosphatase reaction involving three metal ions

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2587100

20 March 2017

A model of the transition state in the alkaline phosphatase reaction

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2587100

20 March 2017

Crystal structure of a small G protein in complex with the GTPase-activating protein rhoGAP

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2587100

20 March 2017

Reaction mechanism of alkaline phosphatase based on crystal structures. Two-metal ion catalysis

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2587100

20 March 2017

Likelihood-enhanced fast translation functions

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2587100

20 March 2017

Coot: model-building tools for molecular graphics

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2587100

20 March 2017

Refinement of macromolecular structures by the maximum-likelihood method

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2587100

20 March 2017

PHENIX: building new software for automated crystallographic structure determination

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2587100

20 March 2017

Kinetic isotope effects for alkaline phosphatase reactions: implications for the role of active-site metal ions in catalysis

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2587100

29 September 2017

Enzymatic mechanisms of phosphate and sulfate transfer.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2587100

29 September 2017

Alkaline phosphatase catalysis is ultrasensitive to charge sequestered between the active site zinc ions

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2587100

29 September 2017

The phosphorylation of alkaline phosphatase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2587100

29 September 2017

Functional interrelationships in the alkaline phosphatase superfamily: phosphodiesterase activity of Escherichia coli alkaline phosphatase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2587100

29 September 2017

Impaired transition state complementarity in the hydrolysis of O-arylphosphorothioates by protein-tyrosine phosphatases.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2587100

29 September 2017

Using guanidinium groups for the recognition of RNA and as catalysts for the hydrolysis of RNA.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2587100

29 September 2017

Protein tyrosine phosphatases: mechanism of catalysis and substrate specificity

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2587100

29 September 2017

The Cys(X)5Arg catalytic motif in phosphoester hydrolysis

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2587100

29 September 2017

Kinetic and magnetic resonance studies of active-site mutants of staphylococcal nuclease: factors contributing to catalysis

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2587100

29 September 2017

Use of site-directed mutagenesis to elucidate the role of arginine-166 in the catalytic mechanism of alkaline phosphatase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2587100

29 September 2017

Why nature chose phosphates

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2587100

29 September 2017

Structure and mechanism of alkaline phosphatase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2587100

29 September 2017

Metal dependence of the phosphate (oxygen)-water exchange reaction of Escherichia coli alkaline phosphatase. Kinetics followed by 31P(18O) NMR

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2587100

29 September 2017

Mechanisms of signaling and related enzymes

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2587100

2 June 2018

Phosphoramidic acids. A new class of nonspecific substrates for alkaline phosphatase from Escherichia coli.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2587100

2 June 2018

Alkaline phosphatase. 31P NMR probes of the mechanism

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2587100

2 June 2018

Transition state stabilization by six arginines clustered in the active site of creatine kinase.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2587100

27 November 2018

Structural and kinetic analyses of arginine residues in the active site of the acetate kinase from Methanosarcina thermophila

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2587100

27 November 2018

Do electrostatic interactions with positively charged active site groups tighten the transition state for enzymatic phosphoryl transfer?

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2587100

27 November 2018

Alkaline phosphatase revisited: hydrolysis of alkyl phosphates

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2587100

27 November 2018

The nature of the transition state for enzyme-catalyzed phosphoryl transfer. Hydrolysis of O-aryl phosphorothioates by alkaline phosphatase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2587100

27 November 2018

Conformational isomers of alkaline phosphatase in the mechanism of hydrolysis

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2587100

27 November 2018

Importance of F1-ATPase residue alpha-Arg-376 for catalytic transition state stabilization

1 reference

https://pubmed.ncbi.nlm.nih.gov/18627128

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Mutation of Arg-166 of Alkaline Phosphatase Alters the Thio Effect but Not the Transition State for Phosphoryl Transfer. Implications for the Interpretation of Thio Effects in Reactions of Phosphatases†

1 reference

https://pubmed.ncbi.nlm.nih.gov/18627128

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Aryl phosphate complexation by cationic cyclodextrins. An enthalpic advantage for guanidinium over ammonium and unusual enthalpy-entropy compensation

1 reference

https://pubmed.ncbi.nlm.nih.gov/18627128

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

MECHANISM of action of alkaline phosphatase

1 reference

https://pubmed.ncbi.nlm.nih.gov/18627128

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Alkaline Phosphatase of Escherichia coli: A Zinc Metalloenzyme*

1 reference

https://pubmed.ncbi.nlm.nih.gov/18627128

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Polyethylene imine derivatives ('synzymes') accelerate phosphate transfer in the absence of metal

1 reference

https://pubmed.ncbi.nlm.nih.gov/18627128

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Mechanism of adenylate kinase. Structural and functional demonstration of arginine-138 as a key catalytic residue that cannot be replaced by lysine

1 reference

https://pubmed.ncbi.nlm.nih.gov/18627128

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Processing of X-ray diffraction data collected in oscillation mode

1 reference

https://pubmed.ncbi.nlm.nih.gov/18627128

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Function of arginine-166 in the active site of Escherichia coli alkaline phosphatase

1 reference

https://pubmed.ncbi.nlm.nih.gov/18627128

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Phosphate binding to alkaline phosphatase. Metal ion dependence

1 reference

https://pubmed.ncbi.nlm.nih.gov/18627128

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

The Phosphate Content of Escherichia coli Alkaline Phosphatase and Its Effect on Stopped Flow Kinetic Studies

1 reference

https://pubmed.ncbi.nlm.nih.gov/18627128

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

The free energy of hydrolysis of the phosphoryl-enzyme intermediate in alkaline phosphatase catalyzed reactions

1 reference

https://pubmed.ncbi.nlm.nih.gov/18627128

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Correlation of thermodynamic and kinetic properties of the phosphoryl-enzyme formed with alkaline phosphatase

1 reference

https://pubmed.ncbi.nlm.nih.gov/18627128

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Alkaline phosphatase is an almost perfect enzyme

1 reference

https://pubmed.ncbi.nlm.nih.gov/18627128

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Catalysis of the hydrolysis of phosphorylated pyridines by alkaline phosphatase has little or no dependence on the pKa of the leaving group

1 reference

https://pubmed.ncbi.nlm.nih.gov/18627128

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Mapping the transition state for ATP hydrolysis: implications for enzymatic catalysis

1 reference

https://pubmed.ncbi.nlm.nih.gov/18627128

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1021/BI800545N

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

release_fdcdqbea7jbiffh2qwj4oztoha

0 references

OpenCitations bibliographic resource ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

PMC publication ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

PubMed publication ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

ResearchGate publication ID

0 references

Sitelinks

Wikipedia(0 entries)

Wikibooks(0 entries)

Wikinews(0 entries)

Wikiquote(0 entries)

Wikisource(0 entries)

Wikiversity(0 entries)

Wikivoyage(0 entries)

Wiktionary(0 entries)

Multilingual sites(0 entries)

Retrieved from "https://www.wikidata.org/w/index.php?title=Q27651199&oldid=1401522349"