Negative co-operativity in glutamate dehydrogenase. Involvement of the 2-position in glutamate in the induction of conformational changes (Q42848798)

8 November 2017

Negative co-operativity in glutamate dehydrogenase. Involvement of the 2-position in glutamate in the induction of conformational changes (English)

1 reference

8 November 2017

E T Bell

1 reference

8 November 2017

C LiMuti

series ordinal

1 reference

8 November 2017

C L Renz

series ordinal

1 reference

8 November 2017

J E Bell

series ordinal

1 reference

8 November 2017

language of work or name

English

0 references

publication date

1 January 1985

1 reference

8 November 2017

1 reference

8 November 2017

225

1 reference

8 November 2017

1 reference

8 November 2017

209-217

1 reference

Antagonistic homotropic interactions as a possible explanation of coenzyme activation of glutamate dehydrogenase

8 November 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1144571

Effects of adenosine 5'-diphosphate on bovine glutamate dehydrogenase: diethyl pyrocarbonate modification

27 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1144571

Dual nucleotide specificity of bovine glutamate dehydrogenase. The role of negative co-operativity

27 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1144571

A steady-state random-order mechanism for the oxidative deamination of norvaline by glutamate dehydrogenase

27 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1144571

The binding of oxidized coenzymes by glutamate dehydrogenase and the effects of glutarate and purine nucleotides

27 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1144571

Molecular interactions of six aromatic competitive inhibitors with bovine liver glutamate dehydrogenase.

27 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1144571

Kinetic studies of glutamate dehydrogenase with glutamate and norvaline as substrates. Coenzyme activation and negative homotropic interactions in allosteric enzymes

27 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1144571

Protection of glutamate dehydrogenase by nicotinamide-adenine dinucleotide against reversible inactivation by pyridoxal 5'-phosphate as a sensitive indicator of conformational change induced by substrates and substrate analogues

27 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1144571

The significance of abrupt transitions in Lineweaver-Burk plots with particular reference to glutamate dehydrogenase. Negative and positive co-operativity in catalytic rate constants

27 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1144571

The allosteric mechanism of bovine liver glutamate dehydrogenase. Evidence from circular-dichroism studies for a conformational change in the ternary complex enzyme-(oxidized nicotinamide-adenine dinucleotide)-glutarate

27 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1144571

A product-inhibition study of bovine liver glutamate dehydrogenase

27 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1144571

Kinetic mechanism of glutamate dehydrogenase.

27 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1144571

Active centre equivalent weight of glutamate dehydrogenase from dry weight determinations and spectrophotometric titrations of abortive complexes

16 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1144571

Glutamic dehydrogenase. III. The order of substrate addition in the enzymatic reaction

16 August 2018

1 reference

12 December 2020

Molecular interactions of competitive inhibitors with bovine liver glutamate dehydrogenase

1 reference

12 December 2020

Mechanism of hysteresis in bovine glutamate dehydrogenase: role of subunit interactions

1 reference

12 December 2020

THE THIONICOTINAMIDE ANALOGS OF DPN AND TPN. I. PREPARATION AND ANALYSIS

1 reference

12 December 2020

Beef liver glutamate dehydrogenase: a study of the oxidation of various alternative amino acid substrates retaining the correct spacing of the two carboxylate groups

1 reference

12 December 2020

L-glutamic acid dehydrogenase; structural requirements for substrate competition; effect of thyroxine

1 reference

12 December 2020

A conformational transition of the oligomer of glutamate dehydrogenase induced by half-saturation with NAD + or NADP +

1 reference

12 December 2020

Identifiers

DOI

10.1042/BJ2250209

1 reference

8 November 2017

1 reference

8 November 2017

PubMed publication ID

2858197

1 reference