The role of the conserved Lys68*:Glu265 intersubunit salt bridge in aspartate aminotransferase kinetics: multiple forced covariant amino acid substitutions in natural variants (Q38269508)

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English	The role of the conserved Lys68*:Glu265 intersubunit salt bridge in aspartate aminotransferase kinetics: multiple forced covariant amino acid substitutions in natural variants	scientific article

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scholarly article

1 reference

Europe PubMed Central

PMC publication ID

1 September 2017

The role of the conserved Lys68*:Glu265 intersubunit salt bridge in aspartate aminotransferase kinetics: multiple forced covariant amino acid substitutions in natural variants (English)

1 reference

Europe PubMed Central

PMC publication ID

1 September 2017

author name string

Edgar Deu

1

1 reference

Europe PubMed Central

PMC publication ID

1 September 2017

Keith A Koch

2

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Europe PubMed Central

PMC publication ID

1 September 2017

Jack F Kirsch

3

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Europe PubMed Central

PMC publication ID

1 September 2017

language of work or name

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inferred from title

publication date

1 May 2002

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Europe PubMed Central

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1 September 2017

Protein Science

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Europe PubMed Central

PMC publication ID

1 September 2017

11

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Europe PubMed Central

PMC publication ID

1 September 2017

5

1 reference

Europe PubMed Central

PMC publication ID

1 September 2017

1062-1073

1 reference

Europe PubMed Central

PMC publication ID

1 September 2017

A general method for the quantitative analysis of functional chimeras: applications from site-directed mutagenesis and macromolecular association

1 reference

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Strain is more important than electrostatic interaction in controlling the pKa of the catalytic group in aspartate aminotransferase

1 reference

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6 September 2017

The role of residues outside the active site: structural basis for function of C191 mutants of Escherichia coli aspartate aminotransferase

1 reference

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Energetic analysis of an antigen/antibody interface: alanine scanning mutagenesis and double mutant cycles on the HyHEL-10/lysozyme interaction

1 reference

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6 September 2017

Crystal structure of Saccharomyces cerevisiae cytosolic aspartate aminotransferase

1 reference

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6 September 2017

Double-mutant cycles: a powerful tool for analyzing protein structure and function

1 reference

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6 September 2017

Evolutionary recruitment of biochemically specialized subdivisions of Family I within the protein superfamily of aminotransferases

1 reference

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6 September 2017

Crystal structures of Escherichia coli aspartate aminotransferase in two conformations. Comparison of an unliganded open and two liganded closed forms

1 reference

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Crystal structures of true enzymatic reaction intermediates: aspartate and glutamate ketimines in aspartate aminotransferase

1 reference

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6 September 2017

X-ray crystallographic study of pyridoxal 5'-phosphate-type aspartate aminotransferases from Escherichia coli in open and closed form

1 reference

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6 September 2017

Three-dimensional structure of a pyridoxal-phosphate-dependent enzyme, mitochondrial aspartate aminotransferase

1 reference

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6 September 2017

2.8-A-resolution crystal structure of an active-site mutant of aspartate aminotransferase from Escherichia coli

1 reference

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6 September 2017

Structural and functional role of the amino-terminal region of porcine cytosolic aspartate aminotransferase. Catalytic and structural properties of enzyme derivatives truncated on the amino-terminal side

1 reference

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6 September 2017

Activity and structure of the active-site mutants R386Y and R386F of Escherichia coli aspartate aminotransferase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2373551

6 September 2017

X-ray structure refinement and comparison of three forms of mitochondrial aspartate aminotransferase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2373551

6 September 2017

Effects of site-specific amino acid modification on protein interactions and biological function

1 reference

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Altering the context of an RNA bulge switches the binding specificities of two viral Tat proteins

1 reference

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23 June 2018

Role of arginine-292 in the substrate specificity of aspartate aminotransferase as examined by site-directed mutagenesis.

1 reference

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23 June 2018

Ancestral lysozymes reconstructed, neutrality tested, and thermostability linked to hydrocarbon packing.

1 reference

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23 June 2018

Three-dimensional structures of aspartate aminotransferase from Escherichia coli and its mutant enzyme at 2.5 A resolution.

1 reference

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23 June 2018

The open/closed conformational equilibrium of aspartate aminotransferase. Studies in the crystalline state and with a fluorescent probe in solution

1 reference

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23 June 2018

Kinetics and equilibria for the reactions of coenzymes with wild type and the Y70F mutant of Escherichia coli aspartate aminotransferase

1 reference

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23 June 2018

Tyrosine 70 fine-tunes the catalytic efficiency of aspartate aminotransferase

1 reference

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23 June 2018

Contributions of the substrate-binding arginine residues to maleate-induced closure of the active site of Escherichia coli aspartate aminotransferase

1 reference

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31 August 2018

Interconversion of the ligand arrays in the CD and EF sites of oncomodulin. Influence on Ca2+-binding affinity

1 reference

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31 August 2018

Characterization of the apparent negative co-operativity induced in Escherichia coli aspartate aminotransferase by the replacement of Asp222 with alanine. Evidence for an extremely slow conformational change

1 reference

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31 August 2018

Linear free energy relationships are valid; using plots of log k versus log (k/k') to prove their existence is not.

1 reference

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31 August 2018

A kinetic and equilibrium analysis of the glutamic oxaloacetate transaminase mechanism

1 reference

https://pubmed.ncbi.nlm.nih.gov/11967363

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Mitochondrial aspartate aminotransferase 27/32-410. Partially active enzyme derivative produced by limited proteolytic cleavage of native enzyme

1 reference

https://pubmed.ncbi.nlm.nih.gov/11967363

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Non-additivity in protein-protein interactions

1 reference

https://pubmed.ncbi.nlm.nih.gov/11967363

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Pre-steady-state kinetics of Escherichia coli aspartate aminotransferase catalyzed reactions and thermodynamic aspects of its substrate specificity

1 reference

https://pubmed.ncbi.nlm.nih.gov/11967363

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

The role of His143 in the catalytic mechanism of Escherichia coli aspartate aminotransferase

1 reference

https://pubmed.ncbi.nlm.nih.gov/11967363

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Cysteine-191 in aspartate aminotransferases appears to be conserved due to the lack of a neutral mutation pathway to the functional equivalent, alanine-191

1 reference

https://pubmed.ncbi.nlm.nih.gov/11967363

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1110/PS.0200902

1 reference

Europe PubMed Central

PMC publication ID

1 September 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

1 September 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

1 September 2017

ResearchGate publication ID

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