(Q38307687)

English

Contribution of a buried aspartate residue towards the catalytic efficiency and structural stability of Bacillus stearothermophilus lactate dehydrogenase

scientific article published on June 1994

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scholarly article

1 reference

Europe PubMed Central

PMC publication ID

2 September 2017

Contribution of a buried aspartate residue towards the catalytic efficiency and structural stability of Bacillus stearothermophilus lactate dehydrogenase (English)

1 reference

Europe PubMed Central

PMC publication ID

2 September 2017

Bacillus stearothermophilus

object named as

Bacillus stearothermophilus

1 reference

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author name string

Nobbs TJ

1

1 reference

Europe PubMed Central

PMC publication ID

2 September 2017

Cortés A

2

1 reference

Europe PubMed Central

PMC publication ID

2 September 2017

Gelpi JL

3

1 reference

Europe PubMed Central

PMC publication ID

2 September 2017

Holbrook JJ

4

1 reference

Europe PubMed Central

PMC publication ID

2 September 2017

Atkinson T

5

1 reference

Europe PubMed Central

PMC publication ID

2 September 2017

Scawen MD

6

1 reference

Europe PubMed Central

PMC publication ID

2 September 2017

Nicholls DJ

7

1 reference

Europe PubMed Central

PMC publication ID

2 September 2017

language of work or name

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publication date

1 June 1994

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Europe PubMed Central

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2 September 2017

Biochemical Journal

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Europe PubMed Central

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2 September 2017

300 ( Pt 2)

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Europe PubMed Central

PMC publication ID

2 September 2017

491-499

1 reference

Europe PubMed Central

PMC publication ID

2 September 2017

Amino acid sequence homology among the 2-hydroxy acid dehydrogenases: mitochondrial and cytoplasmic malate dehydrogenases form a homologous system with lactate dehydrogenase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1138189

6 September 2017

Hydrogen bonding and biological specificity analysed by protein engineering

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1138189

6 September 2017

The use of genetically engineered tryptophan to identify the movement of a domain of B. stearothermophilus lactate dehydrogenase with the process which limits the steady-state turnover of the enzyme

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1138189

6 September 2017

Structure determination and refinement of Bacillus stearothermophilus lactate dehydrogenase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1138189

6 September 2017

Structure of a ternary complex of an allosteric lactate dehydrogenase from Bacillus stearothermophilus at 2.5 A resolution

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1138189

6 September 2017

The use of ternary complexes to study ionizations and isomerizations during catalysis by lactate dehydrogenase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1138189

23 June 2018

Structure and energetics of ligand binding to proteins: Escherichia coli dihydrofolate reductase-trimethoprim, a drug-receptor system.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1138189

23 June 2018

Cloning, expression and complete nucleotide sequence of the Bacillus stearothermophilus L-lactate dehydrogenase gene

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1138189

23 June 2018

Detection and characterization of intermediates in the folding of large proteins by the use of genetically inserted tryptophan probes.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1138189

23 June 2018

Redesigning enzyme structure by site-directed mutagenesis: tyrosyl tRNA synthetase and ATP binding

1 reference

https://pubmed.ncbi.nlm.nih.gov/8002955

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Site-directed mutagenesis as a probe of enzyme structure and catalysis: tyrosyl-tRNA synthetase cysteine-35 to glycine-35 mutation

1 reference

https://pubmed.ncbi.nlm.nih.gov/8002955

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Solute perturbation of protein fluorescence. Quenching of the tryptophyl fluorescence of model compounds and of lysozyme by iodide ion

1 reference

https://pubmed.ncbi.nlm.nih.gov/8002955

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Dissecting the contributions of a specific side-chain interaction to folding and catalysis of Bacillus stearothermophilus lactate dehydrogenase

1 reference

https://pubmed.ncbi.nlm.nih.gov/8002955

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

A strong carboxylate-arginine interaction is important in substrate orientation and recognition in lactate dehydrogenase

1 reference

https://pubmed.ncbi.nlm.nih.gov/8002955

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1042/BJ3000491

1 reference

Europe PubMed Central

PMC publication ID

2 September 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

2 September 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

2 September 2017

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