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

S A Aghajanian, S R Martin, P C Engel

Biochem J (1995) 311 (3): 905–910.

https://doi.org/10.1042/bj3110905

Published: 01 November 1995

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

Articles

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

J L E Dean, X G Wang, J K Teller, M L Waugh, K L Britton, P J Baker, T J Stillman, S R Martin, D W Rice, P C Engel

Biochem J (1994) 301 (1): 13–16.

https://doi.org/10.1042/bj3010013

Published: 01 July 1994

View articletitled, The catalytic role of aspartate in the active site of glutamate dehydrogenase

Articles

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

S E H Syed, D P Hornby, P E Brown, J E Fitton, P C Engel

Biochem J (1994) 298 (1): 107–113.

https://doi.org/10.1042/bj2980107

Published: 15 February 1994

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

Articles

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

Z Valinger, P C Engel, D E Metzler

Biochem J (1993) 294 (3): 835–839.

https://doi.org/10.1042/bj2940835

Published: 15 September 1993

View articletitled, Is pyridoxal 5′-phosphate an affinity label for phosphate-binding sites in proteins?: The case of bovine glutamate dehydrogenase

Articles

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

P C Engel

Biochem J (1992) 284 (2): 604–605.

https://doi.org/10.1042/bj2840604

Published: 01 June 1992

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

Articles

A pH-dependent activation-inactivation equilibrium in glutamate dehydrogenase of Clostridium symbiosum

S E H Syed, P C Engel

Biochem J (1990) 271 (2): 351–355.

https://doi.org/10.1042/bj2710351

Published: 15 October 1990

View articletitled, A pH-dependent activation-inactivation equilibrium in glutamate dehydrogenase of Clostridium symbiosum

Articles

The suicide inactivation of ox liver short-chain acyl-CoA dehydrogenase by propionyl-CoA. Formation of an FAD adduct

L Shaw, P C Engel

Biochem J (1985) 230 (3): 723–731.

https://doi.org/10.1042/bj2300723

Published: 15 September 1985

View articletitled, The suicide inactivation of ox liver short-chain acyl-CoA dehydrogenase by propionyl-CoA. Formation of an FAD adduct

Articles

The kinetic mechanism of ox liver glutamate dehydrogenase in the presence of the allosteric effector ADP. The oxidative deamination of L-glutamate

D P Hornby, M J Aitchison, P C Engel

Biochem J (1984) 223 (1): 161–168.

https://doi.org/10.1042/bj2230161

Published: 01 October 1984

View articletitled, The kinetic mechanism of ox liver glutamate dehydrogenase in the presence of the allosteric effector ADP. The oxidative deamination of L-glutamate

Articles

Ox liver glutamate dehydrogenase. The use of chemical modification to study the relationship between catalytic sites for different amino acid substrates and the question of kinetic non-equivalence of the subunits

S E H Syed, P C Engel

Biochem J (1984) 222 (3): 621–626.

https://doi.org/10.1042/bj2220621

Published: 15 September 1984

View articletitled, Ox liver glutamate dehydrogenase. The use of chemical modification to study the relationship between catalytic sites for different amino acid substrates and the question of kinetic non-equivalence of the subunits

Articles

The purification and properties of ox liver short-chain acyl-CoA dehydrogenase

L Shaw, P C Engel

Biochem J (1984) 218 (2): 511–520.

https://doi.org/10.1042/bj2180511

Published: 01 March 1984

View articletitled, The purification and properties of ox liver short-chain acyl-CoA dehydrogenase

Articles

Butyryl-CoA dehydrogenase from Megasphaera elsdenii . Specificity of the catalytic reaction

G Williamson, P C Engel

Biochem J (1984) 218 (2): 521–529.

https://doi.org/10.1042/bj2180521

Published: 01 March 1984

View articletitled, Butyryl-CoA dehydrogenase from Megasphaera elsdenii . Specificity of the catalytic reaction

Articles

The effect on butyryl-CoA dehydrogenase of reagents specific for nucleophilic sulphur

G Williamson, P C Engel

Biochem J (1983) 211 (3): 559–566.

https://doi.org/10.1042/bj2110559

Published: 01 June 1983

View articletitled, The effect on butyryl-CoA dehydrogenase of reagents specific for nucleophilic sulphur

Articles

Modification of mouse testicular lactate dehydrogenase by pyridoxal 5′-phosphate

K G Gould, P C Engel

Biochem J (1980) 191 (2): 365–371.

https://doi.org/10.1042/bj1910365

Published: 01 November 1980

View articletitled, Modification of mouse testicular lactate dehydrogenase by pyridoxal 5′-phosphate

Articles

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

S S Chen, P C Engel, P M Bayley

Biochem J (1977) 163 (2): 297–302.

https://doi.org/10.1042/bj1630297

Published: 01 May 1977

View articletitled, 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

Articles

Reversible modification of pig heart mitochondrial malate dehydrogenase by pyridoxal 5′-phosphate

S S Chen, P C Engel

Biochem J (1975) 151 (2): 297–303.

https://doi.org/10.1042/bj1510297

Published: 01 November 1975

View articletitled, Reversible modification of pig heart mitochondrial malate dehydrogenase by pyridoxal 5′-phosphate

Articles

Dogfish M 4 lactate dehydrogenase: reversible inactivation by pyridoxal 5′-phosphate and complete protection in complexes that mimic the active ternary complex

S S Chen, P C Engel

Biochem J (1975) 151 (2): 447–449.

https://doi.org/10.1042/bj1510447

Published: 01 November 1975

View articletitled, Dogfish M 4 lactate dehydrogenase: reversible inactivation by pyridoxal 5′-phosphate and complete protection in complexes that mimic the active ternary complex

Articles

A product-inhibition study of bovine liver glutamate dehydrogenase

P C Engel, S S Chen

Biochem J (1975) 151 (2): 305–318.

https://doi.org/10.1042/bj1510305

Published: 01 November 1975

View articletitled, A product-inhibition study of bovine liver glutamate dehydrogenase

Articles

Ox liver glutamate dehydrogenase. The role of lysine-126 reappraised in the light of studies of inhibition and inactivation by pyridoxal 5'-phosphate

S S Chen, P C Engel

Biochem J (1975) 149 (3): 619–626.

https://doi.org/10.1042/bj1490619

Published: 01 September 1975

View articletitled, Ox liver glutamate dehydrogenase. The role of lysine-126 reappraised in the light of studies of inhibition and inactivation by pyridoxal 5'-phosphate

Articles

Horse liver alcohol dehydrogenase. A study of the essential lysine residue

S S Chen, P C Engel

Biochem J (1975) 149 (3): 627–635.

https://doi.org/10.1042/bj1490627

Published: 01 September 1975

View articletitled, Horse liver alcohol dehydrogenase. A study of the essential lysine residue

Articles

Modification of pig M 4 lactate dehydrogenase by pyridoxal 5'-phosphate. Demonstration of an essential lysine residue

S S Chen, P C Engel

Biochem J (1975) 149 (1): 107–113.

https://doi.org/10.1042/bj1490107

Published: 01 July 1975

View articletitled, Modification of pig M 4 lactate dehydrogenase by pyridoxal 5'-phosphate. Demonstration of an essential lysine residue

Articles

The equilibrium position of the reaction of bovine liver glutamate dehydrogenase with pyridoxal 5′-phosphate. A demonstration that covalent modification with this reagent completely abolishes catalytic activity

S S Chen, P C Engel

Biochem J (1975) 147 (2): 351–358.

https://doi.org/10.1042/bj1470351

Published: 01 May 1975

View articletitled, The equilibrium position of the reaction of bovine liver glutamate dehydrogenase with pyridoxal 5′-phosphate. A demonstration that covalent modification with this reagent completely abolishes catalytic activity

Articles

The interpretation of abrupt transitions in Lineweaver-Burk plots

P C Engel

Biochem J (1972) 130 (1): 42P–43P.

https://doi.org/10.1042/bj1300042P

Published: 01 November 1972

View articletitled, The interpretation of abrupt transitions in Lineweaver-Burk plots

Articles

Kinetic studies of glutamate dehydrogenase. The reductive amination of 2-oxoglutarate

P. C. Engel, K. Dalziel

Biochem J (1970) 118 (3): 409–419.

https://doi.org/10.1042/bj1180409

Published: 01 July 1970

View articletitled, Kinetic studies of glutamate dehydrogenase. The reductive amination of 2-oxoglutarate

Articles

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

P. C. Engel, K. Dalziel

Biochem J (1969) 115 (4): 621–631.

https://doi.org/10.1042/bj1150621

Published: 01 December 1969

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

Articles

The equilibrium constants of the glutamate dehydrogenase systems

P. C. Engel, K. Dalziel

Biochem J (1967) 105 (2): 691–695.

https://doi.org/10.1042/bj1050691

Published: 01 November 1967

View articletitled, The equilibrium constants of the glutamate dehydrogenase systems

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

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

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

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

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

A pH-dependent activation-inactivation equilibrium in glutamate dehydrogenase of Clostridium symbiosum

The suicide inactivation of ox liver short-chain acyl-CoA dehydrogenase by propionyl-CoA. Formation of an FAD adduct

The kinetic mechanism of ox liver glutamate dehydrogenase in the presence of the allosteric effector ADP. The oxidative deamination of L-glutamate

Ox liver glutamate dehydrogenase. The use of chemical modification to study the relationship between catalytic sites for different amino acid substrates and the question of kinetic non-equivalence of the subunits

The purification and properties of ox liver short-chain acyl-CoA dehydrogenase

Butyryl-CoA dehydrogenase from Megasphaera elsdenii . Specificity of the catalytic reaction

The effect on butyryl-CoA dehydrogenase of reagents specific for nucleophilic sulphur

Modification of mouse testicular lactate dehydrogenase by pyridoxal 5′-phosphate

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

Reversible modification of pig heart mitochondrial malate dehydrogenase by pyridoxal 5′-phosphate

Dogfish M 4 lactate dehydrogenase: reversible inactivation by pyridoxal 5′-phosphate and complete protection in complexes that mimic the active ternary complex

A product-inhibition study of bovine liver glutamate dehydrogenase

Ox liver glutamate dehydrogenase. The role of lysine-126 reappraised in the light of studies of inhibition and inactivation by pyridoxal 5'-phosphate

Horse liver alcohol dehydrogenase. A study of the essential lysine residue

Modification of pig M 4 lactate dehydrogenase by pyridoxal 5'-phosphate. Demonstration of an essential lysine residue

The equilibrium position of the reaction of bovine liver glutamate dehydrogenase with pyridoxal 5′-phosphate. A demonstration that covalent modification with this reagent completely abolishes catalytic activity

The interpretation of abrupt transitions in Lineweaver-Burk plots

Kinetic studies of glutamate dehydrogenase. The reductive amination of 2-oxoglutarate

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

The equilibrium constants of the glutamate dehydrogenase systems

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