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The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks in maintaining enzyme stability at extreme temperatures

Structure (London), 1995-11, Vol.3 (11), p.1147-1158

1995

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Subunit assembly and active site location in the structure of glutamate dehydrogenase

Proteins, structure, function, and bioinformatics, 1992-01, Vol.12 (1), p.75-86

1992

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Insights into the molecular basis of thermal stability from the structure determination of Pyrococcus furiosus glutamate dehydrogenase

FEMS microbiology reviews, 1996-05, Vol.18 (2-3), p.105-117

1996

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Allosteric behaviour of 1:5 hybrids of mutant subunits of Clostridium symbiosum glutamate dehydrogenase differing in their amino acid specificity

Biochemical journal, 2001-12, Vol.360 (Pt 3), p.651-656

2001

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Evolution of Substrate Diversity in the Superfamily of Amino Acid Dehydrogenases: Prospects for Rational Chiral Synthesis

Journal of molecular biology, 1993-12, Vol.234 (4), p.938-945

1993

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The catalytic role of aspartate in the active site of glutamate dehydrogenase

Biochemical journal, 1994-07, Vol.301 (1), p.13-16

1994

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Protein thermostability in extremophiles

Biochimie, 1998-11, Vol.80 (11), p.933-941

1998

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Use of protein engineering to explore subunit interactions in an allosteric enzyme: construction of inter-subunit hybrids in Clostridium symbiosum glutamate dehydrogenase

Protein engineering, 1998-07, Vol.11 (7), p.569-575

1998

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Preliminary evidence for the existence of specific functional assemblies between enzymes of the beta-oxidation pathway and the respiratory chain

Biochemical journal, 2000-02, Vol.345 Pt 3 (3), p.429-435

2000

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Specificity constants in the context of protein engineering of two-substrate enzymes

Biochemical journal, 1992-06, Vol.284 (2), p.604-605

ENGEL, P. C

1992

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Flavins and Flavoproteins: Proceedings of the Eighth International Symposium, Brighton, England, July 9-13, 1984

2019

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The Y42H mutation in medium‐chain acyl‐CoA dehydrogenase, which is prevalent in babies identified by MS/MS‐based newborn screening, is temperature sensitive

European journal of biochemistry, 2004-10, Vol.271 (20), p.4053-4063

2004

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Octanoylation of the lipoyl domains of the pyruvate dehydrogenase complex in a lipoyl‐deficient strain of Escherichia coli

Molecular microbiology, 1990-06, Vol.4 (6), p.943-950

1990

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Is pyridoxal 5'-phosphate an affinity label for phosphate-binding sites in proteins ? The case of bovine glutamate dehydrogenase

Biochemical journal, 1993-09, Vol.294 (3), p.835-839

1993

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Specificity of coenzyme analogues and fragments in promoting or impeding the refolding of clostridial glutamate dehydrogenase

Protein science, 1999-04, Vol.8 (4), p.866-872

1999

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Specific diagnosis of medium-chain acyl-CoA dehydrogenase (MCAD) deficiency in dried blood spots by a polymerase chain reaction (PCR) assay detecting a point-mutation (G985) in the MCAD gene

Clinica chimica acta, 1991-11, Vol.203 (1), p.23-34

1991

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Dose-area product measurements during barium enema radiograph examinations: A Western Cape study

South African medical journal, 2001-08, Vol.91 (8), p.693-696

2001

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Frequency of the G985 MCAD mutation in the general population

The Lancet (British edition), 1991-02, Vol.337 (8736), p.298-299

1991

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Single Amino Acid Substitution in Bacillus sphaericus Phenylalanine Dehydrogenase Dramatically Increases Its Discrimination between Phenylalanine and Tyrosine Substrates

Biochemistry (Easton), 2002-09, Vol.41 (38), p.11390-11397

2002

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Urea-induced inactivation and denaturation of clostridial glutamate dehydrogenase: the absence of stable dimeric or trimeric intermediates

Biochemical journal, 1995-11, Vol.311 ( Pt 3) (3), p.905-910

1995

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Defects of metabolism of fatty acids in the sudden infant death syndrome

BMJ, 1985-06, Vol.290 (6484), p.1771-1773

1985

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The discovery of four distinct glutamate dehydrogenase genes in a strain of Halobacterium salinarum

Gene, 2005-04, Vol.349, p.237-244

2005

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Properties of the thermostable glutamate dehydrogenase of the mesophilic anaerobe Peptostreptoccus asaccharolyticus purified by a novel method after over-expression in an Escherichia coli host

FEMS microbiology letters, 2005-03, Vol.244 (1), p.53-59

2005

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Site and significance of chemically modifiable cysteine residues in glutamate dehydrogenase of Clostridium symbiosum and the use of protection studies to measure coenzyme binding

Biochemical journal, 1994-02, Vol.298 ( Pt 1) (1), p.107-113

1994

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A Thermally Sensitive Loop in Clostridial Glutamate Dehydrogenase Detected by Limited Proteolysis

The Journal of biological chemistry, 2003-01, Vol.278 (2), p.1067-1074

2003

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The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks in maintaining enzyme stability at extreme temperatures

Subunit assembly and active site location in the structure of glutamate dehydrogenase

Insights into the molecular basis of thermal stability from the structure determination of Pyrococcus furiosus glutamate dehydrogenase

Allosteric behaviour of 1:5 hybrids of mutant subunits of Clostridium symbiosum glutamate dehydrogenase differing in their amino acid specificity

Evolution of Substrate Diversity in the Superfamily of Amino Acid Dehydrogenases: Prospects for Rational Chiral Synthesis

The catalytic role of aspartate in the active site of glutamate dehydrogenase

Protein thermostability in extremophiles

Use of protein engineering to explore subunit interactions in an allosteric enzyme: construction of inter-subunit hybrids in Clostridium symbiosum glutamate dehydrogenase

Preliminary evidence for the existence of specific functional assemblies between enzymes of the beta-oxidation pathway and the respiratory chain

Specificity constants in the context of protein engineering of two-substrate enzymes

Flavins and Flavoproteins: Proceedings of the Eighth International Symposium, Brighton, England, July 9-13, 1984

The Y42H mutation in medium‐chain acyl‐CoA dehydrogenase, which is prevalent in babies identified by MS/MS‐based newborn screening, is temperature sensitive

Octanoylation of the lipoyl domains of the pyruvate dehydrogenase complex in a lipoyl‐deficient strain of Escherichia coli

Is pyridoxal 5'-phosphate an affinity label for phosphate-binding sites in proteins ? The case of bovine glutamate dehydrogenase

Specificity of coenzyme analogues and fragments in promoting or impeding the refolding of clostridial glutamate dehydrogenase

Specific diagnosis of medium-chain acyl-CoA dehydrogenase (MCAD) deficiency in dried blood spots by a polymerase chain reaction (PCR) assay detecting a point-mutation (G985) in the MCAD gene

Dose-area product measurements during barium enema radiograph examinations: A Western Cape study

Frequency of the G985 MCAD mutation in the general population

Single Amino Acid Substitution in Bacillus sphaericus Phenylalanine Dehydrogenase Dramatically Increases Its Discrimination between Phenylalanine and Tyrosine Substrates

Urea-induced inactivation and denaturation of clostridial glutamate dehydrogenase: the absence of stable dimeric or trimeric intermediates

Defects of metabolism of fatty acids in the sudden infant death syndrome

The discovery of four distinct glutamate dehydrogenase genes in a strain of Halobacterium salinarum

Properties of the thermostable glutamate dehydrogenase of the mesophilic anaerobe Peptostreptoccus asaccharolyticus purified by a novel method after over-expression in an Escherichia coli host

Site and significance of chemically modifiable cysteine residues in glutamate dehydrogenase of Clostridium symbiosum and the use of protection studies to measure coenzyme binding

A Thermally Sensitive Loop in Clostridial Glutamate Dehydrogenase Detected by Limited Proteolysis

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