P. Engel

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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.

K. S. Yip, K. Britton, T. J. Stillman, 1995, Structure.

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

I. Connerton, K. S. Yip, K. Britton, 1996 .

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

I. Connerton, K. S. Yip, K. Britton, 1996, FEMS microbiology reviews.

Crystallization of an NAD+-dependent glutamate dehydrogenase from Clostridium symbiosum.

D. Rice, D. Hornby, P. Engel, 1985, Journal of molecular biology.

Crystallization of the NAD(P)-dependent glutamate dehydrogenase from the hyperthermophile Pyrococcus furiosus.

K. S. Yip, K. Britton, T. J. Stillman, 1995, Acta crystallographica. Section D, Biological crystallography.

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.

P. Engel, J. Carrigan, S. Coughlan, 2005, FEMS microbiology letters.

Protein thernmstabilRy in extrernophiles

P. Engel, R. Chiaraluce, V. Consalvi, 1998 .

Medium-chain acyl-CoA dehydrogenase (MCAD) mutations identified by MS/MS-based prospective screening of newborns differ from those observed in patients with clinical symptoms: identification and characterization of a new, prevalent mutation that results in mild MCAD deficiency.

I Knudsen, P. Bross, B. Andresen, 2001, American journal of human genetics.

Chapter 3 Enzyme kinetics

P. Engel, 1984 .

A marriage full of surprises; forty-five years living with glutamate dehydrogenase

P. Engel, 2011, Neurochemistry International.

The equilibrium constants of the glutamate dehydrogenase systems.

P. Engel, K. Dalziel, 1967, The Biochemical journal.

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

P. Engel, K. Dalziel, 1968, FEBS letters.

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

P. Engel, A. Parker, 2000, The Biochemical journal.

The production of superoxide anion radicals in the reaction of reduced flavins and flavoproteins with molecular oxygen.

R. Matthews, P. Engel, V. Massey, 1969, Biochemical and biophysical research communications.

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.

L. Bolund, B. Andresen, A. Blakemore, 1991, Clinica chimica acta; international journal of clinical chemistry.

Acylcoenzyme A dehydrogenase deficiency in heart tissue from infants who died unexpectedly with fatty change in the liver

P. Engel, M. Bennett, S. Variend, 1988, British medical journal.

Novel Enzymes for Biotransformation and Resolution of Alpha-Amino Acids

P. Engel, F. Paradisi, 2010 .

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

P. Bross, B. Andresen, P. Engel, 2004, European journal of biochemistry.

An NSAID-like compound, FT-9, preferentially inhibits gamma-secretase cleavage of the amyloid precursor protein compared to its effect on amyloid precursor-like protein 1.

D. Walsh, C. Sala Frigerio, T. Golde, 2009, Biochemistry.

Structure of NADP+‐dependent glutamate dehydrogenase from Escherichia coli – reflections on the basis of coenzyme specificity in the family of glutamate dehydrogenases

P. Engel, A. R. Khan, Michael A Sharkey, 2013, The FEBS journal.

Evolution of substrate diversity in the superfamily of amino acid dehydrogenases. Prospects for rational chiral synthesis.

K. Britton, T. J. Stillman, D. Rice, 1993, Journal of molecular biology.

Phenylalanine dehydrogenase mutants: efficient biocatalysts for synthesis of non-natural phenylalanine derivatives.

P. Engel, A. Maguire, F. Paradisi, 2007, Journal of biotechnology.

Functional properties of two mutants of human glucose 6-phosphate dehydrogenase, R393G and R393H, corresponding to the clinical variants G6PD Wisconsin and Nashville.

P. Engel, Xiao-tao Wang, V. Lam, 2006, Biochimica et biophysica acta.

Alanine dehydrogenase from the psychrophilic bacterium strain PA-43: overexpression, molecular characterization, and sequence analysis

D. Rice, P. Baker, P. Engel, 2003, Extremophiles.

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

P. Engel, S. Aghajanian, 1998, Protein engineering.

Development of a satisfactory and general continuous assay for aminotransferases by coupling with (R)-2-hydroxyglutarate dehydrogenase.

P. Engel, W. Buckel, Xuejing Yu, 2012, Analytical biochemistry.

Group specific antibodies against the putative AMP‐binding domain signature SGTTGXPKG in peptide synthetases and related enzymes

G. Turner, P. Engel, R. Dieckmann, 1998, Biochemistry and molecular biology international.

Engineered dehydrogenase biocatalysts for non-natural amino acids: efficient isolation of the D-enantiomer from racemic mixtures.

P. Engel, A. Maguire, F. Paradisi, 2008, Organic & biomolecular chemistry.

Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its discrimination between phenylalanine and tyrosine substrates.

K. Britton, D. Rice, Y. Asano, 2002, Biochemistry.

Prospects for robust biocatalysis: engineering of novel specificity in a halophilic amino acid dehydrogenase

P. Engel, N. Munawar, 2012, Extremophiles.

Enantioselective synthesis of non-natural amino acids using phenylalanine dehydrogenases modified by site-directed mutagenesis.

P. Engel, A. Maguire, F. Paradisi, 2004, Organic and biomolecular chemistry.

Overexpression in a non-native halophilic host and biotechnological potential of NAD+-dependent glutamate dehydrogenase from Halobacterium salinarum strain NRC-36014

P. Engel, N. Munawar, 2012, Extremophiles.

Marked decrease in specific activity contributes to disease phenotype in two human glucose 6‐phosphate dehydrogenase mutants, G6PDUnion and G6PDAndalus

P. Engel, Xiao-tao Wang, V. Lam, 2005, Human mutation.

The most common mutation causing medium-chain acyl-CoA dehydrogenase deficiency is strongly associated with a particular haplotype in the region of the gene

L. Bolund, B. Andresen, A. Blakemore, 1991, Human Genetics.

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

I. Connerton, K. S. Yip, K. Britton, 1996 .

Efficient screening for new amino acid dehydrogenase activity: directed evolution of Bacillus sphaericus phenylalanine dehydrogenase towards activity with an unsaturated non-natural amino acid.

P. Engel, Sihong Chen, 2009, Journal of biotechnology.

Biocatalytic stereoinversion of D-para-bromophenylalanine in a one-pot three-enzyme reaction

P. Engel, F. Khorsand, A. J. Whitehead, 2017 .

An engineered mutant, L307V of phenylalanine dehydrogenase from Bacillus sphaericus : high activity and stability in organic-aqueous solvent mixtures and utility for synthesis of non-natural L-amino acids

P. Engel, Sihong Chen, 2007 .

Engineered phenylalanine dehydrogenase in organic solvents: homogeneous and biphasic enzymatic reactions.

P. Engel, F. Paradisi, P. Galletti, 2005, Organic & biomolecular chemistry.

Mutants of Phenylalanine Dehydrogenase: New Biocatalysts in the Asymmetric Synthesis and Racemic Resolution of Non-Natural Amino Acids

P. Engel, A. Maguire, F. Paradisi, 2007 .

Identification of the residue responsible for catalysing regeneration of activity in the inactive glutamate dehydrogenase mutant D165N

P. Engel, K. Geoghegan, F. Paradisi, 2005, FEBS letters.

Contribution of an aspartate residue, D114, in the active site of clostridial glutamate dehydrogenase to the enzyme's unusual pH dependence.

K. Britton, T. J. Stillman, D. Rice, 2001, Biochimica et biophysica acta.

Alteration of the amino acid substrate specificity of clostridial glutamate dehydrogenase by site-directed mutagenesis of an active-site lysine residue.

K. Britton, D. Rice, S. Martin, 1995, Protein engineering.

Homotropic allosteric control in clostridial glutamate dehydrogenase: Different mechanisms for glutamate and NAD+?

P. Engel, M. Hamza, Muaawia Hamza, 2008, FEBS letters.

On the Evidence for Partial Gene Duplication from Amino Acid Sequence of Bovine Glutamate Dehydrogenase (reply)

P. Engel, 1974, Nature.

Glutamate dehydrogenase of Halobacterium salinarum: evidence that the gene sequence currently assigned to the NADP+-dependent enzyme is in fact that of the NAD+-dependent glutamate dehydrogenase.

A. Moir, P. Engel, M. Bonete, 2002, FEMS microbiology letters.

The contribution of tryptophan residues to conformational changes in clostridial glutamate dehydrogenase − W64 and W449 as mediators of the cooperative response to glutamate

S. Martin, P. Engel, Stephen R. Martin, 2007, The FEBS journal.

Modular coenzyme specificity: A domain‐swopped chimera of glutamate dehydrogenase

P. Engel, Michael A. Sharkey, 2009, Proteins.

The glutamate dehydrogenase gene of Clostridium symbiosum. Cloning by polymerase chain reaction, sequence analysis and over-expression in Escherichia coli.

M. McPherson, P. Engel, J. Guest, 1992, European journal of biochemistry.

Functional studies of a glutamate dehydrogenase with known three-dimensional structure: steady-state kinetics of the forward and reverse reactions catalysed by the NAD(+)-dependent glutamate dehydrogenase of Clostridium symbiosum.

D. M. Parker, P. Engel, S. Syed, 1991, Biochimica et biophysica acta.

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

P. Engel, S. Syed, 1990, The Biochemical journal.

Conversion of a glutamate dehydrogenase into methionine/norleucine dehydrogenase by site-directed mutagenesis.

K. Britton, T. J. Stillman, D. Rice, 2001, European journal of biochemistry.

Initial formation of a non-covalent enzyme-reagent complex during the inactivation of clostridial glutamate dehydrogenase by Ellman's reagent: determination of the enzyme's dissociation constant for the binary complex with NAD+ from protection studies.

L. A. Basso, P. Engel, 1994, Biochimica et biophysica acta.

Identification of the reactive cysteine in clostridial glutamate dehydrogenase by site-directed mutagenesis and proof that this residue is not strictly essential.

P. Engel, X. Wang, 1994, Protein engineering.

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

D. Hornby, P. Engel, S. Syed, 1994, The Biochemical journal.

The essentail active‐site lysines of clostridial glutamate dehydrogenase

K. Lilley, P. Engel, 1992 .

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

D. Hornby, P. Engel, S. Hatanaka, 1983, The International journal of biochemistry.

Glutamate Dehydrogenases: The Why and How of Coenzyme Specificity

P. Engel, 2013, Neurochemical Research.

Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase activity with guidance from homology-based modelling.

K. Britton, D. Rice, Y. Asano, 2003, European journal of biochemistry.

Transport of C4-dicarboxylates by anaerobically grown Escherichia coli. Energetics and mechanism of exchange, uptake and efflux.

P. Engel, G. Unden, R Krämer, 1994, European journal of biochemistry.

CoA-persulphide: a possible in vivo inhibitor of mammalian short-chain acyl-CoA dehydrogenase.

P. Engel, L. Shaw, 1987, Biochimica et biophysica acta.

Activity staining of halophilic enzymes: substitution of salt with a zwitterion in non-denaturing electrophoresis.

P. Engel, Q. Cadenas, 1994, Biochemistry and molecular biology international.

Novel nicotinamide adenine dinucleotide analogues as selective inhibitors of NAD+-dependent enzymes

P. Engel, F. Paradisi, M. Migaud, 2004 .

Enzyme Kinetics: The Steady-State Approach

Paul C. Engel, P. Engel, 1977 .

Causes and elimination of erratic blanks in enzymatic metabolite assays involving the use of NAD+ in alkaline hydrazine buffers: improved conditions for the assay of L-glutamate, L-lactate, and other metabolites.

P. Engel, Janet B. Jones, 1978, Analytical biochemistry.

Enantioselective synthesis of non-natural amino acids using phenylalanine dehydrogenases modified by site-directed mutagenesis.

P. Engel, A. Maguire, F. Paradisi, 2004, Organic & biomolecular chemistry.

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

P. Engel, W. Ferdinand, 1973, The Biochemical journal.

On the Crystal Chemistry of Some Thallium Sulphides and Sulphosalts

P. Engel, A. Nagl, W. Nowacki, 1982 .

Kinetic studies on the binding of 1,N6-etheno-NAD+ to glutamate dehydrogenase from Clostridium symbiosum.

L. A. Basso, P. Engel, A. Walmsley, 1997, Biochimica et biophysica acta.

The reactions of pyridoxal 5'-phosphate with the M4 and H4 isoenzymes of pig lactate dehydrogenase.

P. Engel, K. Gould, 1982, Archives of biochemistry and biophysics.

Re‐engineering the discrimination between the oxidized coenzymes NAD+ and NADP+ in clostridial glutamate dehydrogenase and a thorough reappraisal of the coenzyme specificity of the wild‐type enzyme

P. Engel, D. Scanlon, Marina Capone, 2011, The FEBS journal.

The crystal structure of synthetic Tl2MnAs2S5

P. Engel, W. Nowacki, A. Edenharter, 1982 .

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

P. Engel, K. Dalziel, 1969, The Biochemical journal.

A re-examination of the reaction between ox liver glutamate dehydrogenase and 1-fluoro-2,4-dinitrobenzene.

P. Engel, K. Gould, 1979, Archives of biochemistry and biophysics.

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

P. Engel, K. Dalziel, 1970, The Biochemical journal.

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

P. Engel, S. S. Chen, 1975, The Biochemical journal.

Equilibrium protection studies of the interaction of bovine glutamate dehydrogenase with purine nucleotide effectors

P. Engel, Soo-Se Chen, 1975, FEBS letters.

Recombinant human glucose-6-phosphate dehydrogenase. Evidence for a rapid-equilibrium random-order mechanism.

P. Engel, S. Au, Xiao-tao Wang, 2002, European journal of biochemistry.

Beef liver glutamate dehydrogenase: effects of partial proteolysis with chymotrypsin.

P. Engel, M. Aitchison, 1983, The International journal of biochemistry.

Kinetics and Mechanism of Glutamate Dehydrogenase

P. Engel, K. Dalziel, 1970 .

The mechanism of substrate and coenzyme binding to clostridial glutamate dehydrogenase during oxidative deamination.

L. A. Basso, P. Engel, A. Walmsley, 1993, European journal of biochemistry.

Kinetic studies of Ox-liver glutamate dehydrogenase oxidative deamination of two glutamate analogues, L-threo-γ-methylglutamate and L-α-amino-γ-nitraminobutyrate, in the presence of the allosteric effector ADP

D. Hornby, P. Engel, S. Hatanaka, 1985 .

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.

P. Engel, S. S. Chen, 1977, The Biochemical journal.

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

K. Britton, T. J. Stillman, D. Rice, 1992, Proteins.

The structural basis of proteolytic activation of bovine glutamate dehydrogenase

P. Engel, J. Carrigan, 2008, Protein science : a publication of the Protein Society.

The effects of digestion by bovine pancreas alpha-chymotrypsin on native bovine glutamate dehydrogenase.

P. Engel, M. Aitchison, 1980, Biochemical Society transactions.

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.

P. Engel, S. Chen, 1974, The Biochemical journal.

Positive cooperativity with Hill coefficients of up to 6 in the glutamate concentration dependence of steady-state reaction rates measured with clostridial glutamate dehydrogenase and the mutant A163G at high pH.

P. Engel, X. Wang, 1995, Biochemistry.

Steady-state kinetics and transient studies of substrate and coenzyme analogue binding to clostridial glutamate dehydrogenase (GDH) during oxidative deamination.

L. A. Basso, P. Engel, A. Walmsley, 1994, Biochemical Society transactions.

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

K. Britton, T. J. Stillman, D. Rice, 1994, The Biochemical journal.

The glutamate dehydrogenase gene of Clotridium symbiosum

M. McPherson, P. Engel, J. Guest, 1992 .

Characterization of Peptostreptococcus asaccharolyticus glutamate dehydrogenase purified by dye-ligand chromatography.

D. Hornby, P. Engel, 1984, Journal of general microbiology.

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

P. Engel, S. S. Chen, 1975, The Biochemical journal.

The equilibrium position of the reaction of bovine liver glutamate dehydrogenase with pyridoxal5'-phosphate. A demonstration that covalent modification with this reagent completely abolishes catalytic activity.

P. Engel, S. S. Chen, 1975, The Biochemical journal.

Modification of mouse testicular lactate dehydrogenase by pyridoxal 5'-phosphate.

P. Engel, K. Gould, 1980, The Biochemical journal.

Dogfish M4 lactate dehydrogenase: reversible inactivation by pyridoxal 5'-phosphate and complete protection in complexes that mimic the active ternary complex.

P. Engel, S. S. Chen, 1975, The Biochemical journal.

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

P. Engel, S. S. Chen, 1975, The Biochemical journal.

Modification of pig M4 lactate dehydrogenase by pyridoxal 5'-phosphate. Demonstration of an essential lysine residue.

P. Engel, S. S. Chen, 1975, The Biochemical journal.

Crystal structure of NAD+-dependent Peptoniphilus asaccharolyticus glutamate dehydrogenase reveals determinants of cofactor specificity.

John B Carrigan, Santosh Panjikar, S. Panjikar, 2012, Journal of structural biology.

Glutaric aciduria type II: Biochemical investigation and treatment of a child diagnosed prenatally

P. Engel, M. Bennett, R. Pollitt, 1984, Journal of Inherited Metabolic Disease.

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

P. Engel, M. Bennett, S. Variend, 1985, British medical journal.

Medium chain acyl CoA dehydrogenase deficiency

B. Andresen, P. Engel, N. Gregersen, 2000 .

Characterization of a disease-causing Lys329 to Glu mutation in 16 patients with medium-chain Acyl-CoA dehydrogenase deficiency

L. Bolund, P. Bross, B. Andresen, 1991, Journal of Inherited Metabolic Disease.

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

P. Engel, L. Shaw, 1984, The Biochemical journal.

Novel methylenecyclopropyl‐based acyl‐CoA dehydrogenase inhibitor

P. Engel, N. Broadway, Neil M. Broadway, 1998, FEBS letters.

[43] Butyryl-CoA dehydrogenase from Megasphaera elsdenii: EC 1.3.99.2 butyryl-CoA:(acceptor) oxidoreductase

P. Engel, 1981 .

Sequence homologies among pyridine nucleotide‐linked dehydrogenases: Possible partial gene duplications in glyceraldehyde‐3‐phosphate dehydrogenase

P. Engel, 1973, FEBS letters.

Cooperativity between trimers of the hexameric glutamate dehydrogenase from Clostridium symbiosum.

L. A. Basso, P. Engel, A. Walmsley, 1998, Biochimica et biophysica acta.

Enzyme-Activated Irreversible Inhibitors : Edited by N. Seiler, M. J. Jung and J. Koch-Weser Elsevier/North-Holland; Amsterdam, New York, 1978 viii + 360 pages, $53.75, Dfl 110.00

P. Engel, P. C. Engel, 1980 .

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

P. Engel, L. Shaw, 1985, The Biochemical journal.

What is the role of the second “structural” NADP+‐binding site in human glucose 6‐phosphate dehydrogenase?

P. Engel, Xiao-tao Wang, V. Lam, 2008, Protein science : a publication of the Protein Society.

Overexpression in a non-native halophilic host and biotechnological potential of NAD+-dependent glutamate dehydrogenase from Halobacterium salinarum strain NRC-36014

P. Engel, N. Munawar, 2012, Extremophiles.

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

P. Engel, K. Geoghegan, B. M. Hayden, 2005, Gene.

Purification and detailed study of two clinically different human glucose 6-phosphate dehydrogenase variants, G6PD(Plymouth) and G6PD(Mahidol): Evidence for defective protein folding as the basis of disease.

P. Engel, S. Au, D. M. Au, 2008, Molecular genetics and metabolism.

Protein thermostability in extremophiles.

P. Engel, R. Chiaraluce, V. Consalvi, 1998, Biochimie.

The essential active-site lysines of clostridial glutamate dehydrogenase. A study with pyridoxal-5'-phosphate.

K. Lilley, P. Engel, 1992, European journal of biochemistry.

Clinical mutants of human glucose 6-phosphate dehydrogenase: impairment of NADP(+) binding affects both folding and stability.

P. Engel, Xiao-tao Wang, 2009, Biochimica et biophysica acta.

An optimised system for refolding of human glucose 6-phosphate dehydrogenase

P. Engel, Xiao-tao Wang, 2009, BMC biotechnology.

The purification and properties of butyryl-coenzyme A dehydrogenase from Peptostreptococcus elsdenii.

P. Engel, V. Massey, 1971, The Biochemical journal.

Characterization of alanine and malate dehydrogenases from a marine psychrophile strain PA-43

P. Engel, J. Irwin, V. Marteinsson, 2001, Extremophiles.

A convenient and rapid method for the complete removal of CoA from butyryl-CoA dehydrogenase.

P. Engel, G. Williamson, 1982, Biochimica et biophysica acta.

A resonance Raman study on the nature of charge‐transfer interactions in butyryl CoA dehydrogenase

P. Engel, G. Williamson, Y. Nishina, 1982, FEBS letters.

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

P. Engel, K. Geoghegan, B. Chrunyk, 2003, The Journal of Biological Chemistry.

Use of Fed‐Batch Cultivation for Achieving High Cell Densities for the Pilot‐Scale Production of a Recombinant Protein (Phenylalanine Dehydrogenase) in Escherichia coli

B. Glennon, M. Barrett, P. Kieran, 2006 .

The partial amino acid sequence of the NAD(+)-dependent glutamate dehydrogenase of Clostridium symbiosum: implications for the evolution and structural basis of coenzyme specificity.

K. Britton, T. J. Stillman, D. Rice, 1991, Biochimica et biophysica acta.

Purification and characterisation of a serine peptidase from the marine psychrophile strain PA-43.

P. Engel, J. Irwin, A. Lanzetti, 2001, FEMS microbiology letters.

Purification and properties of psychrophilic dehydrogenases.

P. Engel, J. Irwin, G. Alfredsson, 1998, Biochemical Society transactions.

Correlation of intron-exon organisation with the three-dimensional structure in glutamate dehydrogenase.

K. Britton, T. J. Stillman, D. Rice, 1995, Biochimica et biophysica acta.

A product-inhibition study of bovine liver glutamate dehydrogenase.

P. Engel, S. S. Chen, 1975, The Biochemical journal.

Insights into the Molecular Basis of Salt Tolerance from the Study of Glutamate Dehydrogenase from Halobacterium salinarum *

K. S. Yip, K. Britton, T. J. Stillman, 1998, The Journal of Biological Chemistry.

Insights into thermal stability from a comparison of the glutamate dehydrogenases from Pyrococcus furiosus and Thermococcus litoralis.

K. S. Yip, K. Britton, T. J. Stillman, 1995, European journal of biochemistry.

Forced evolution of Escherichia coli cells with the ability to effectively utilize non-natural amino acids l-tert-leucine, l-norleucine and γ-methyl-l-leucine

P. Engel, S. Lynch, Pingping Zhang, 2010 .

Butyryl Coenzyme A Dehydrogenase: Studies on the Specificity of the Formation of Acyl Coenzyme A Complexes with Long-Wavelength Absorption

P. Engel, 1972, Zeitschrift fur Naturforschung. Teil B. Anorganische Chemie, organische Chemie, Biochemie, Biophysik, Biologie.

Protein stability in extremophilic archaea.

P. Engel, R. Chiaraluce, V. Consalvi, 2000, Frontiers in bioscience : a journal and virtual library.

Prospects for robust biocatalysis: engineering of novel specificity in a halophilic amino acid dehydrogenase

P. Engel, N. Munawar, 2012, Extremophiles.

5,5'-Dithiobis-(2-nitrobenzoic acid) as a probe for a non-essential cysteine residue at the medium chain acyl-coenzyme A dehydrogenase binding site of the human 'electron transferring flavoprotein' (ETF).

P. Engel, A. Parker, 1999, Journal of enzyme inhibition.

Reversal of the extreme coenzyme selectivity of Clostridium symbiosum glutamate dehydrogenase

P. Engel, A. Gori, Michael A. Sharkey, 2012, The FEBS journal.

Two novel variants of human medium chain acyl‐CoA dehydrogenase (MCAD)

B. Andresen, P. Engel, L. O’Reilly, 2005, The FEBS journal.

Anaerobic fumarate transport in Escherichia coli by an fnr-dependent dicarboxylate uptake system which is different from the aerobic dicarboxylate uptake system

P. Engel, G. Unden, R Krämer, 1992, Journal of bacteriology.

The crystal structure of synthetic TISb3S5

P. Engel, W. Nowacki, Μ. Gostojic, 1982 .

Making biochemistry count: life among the amino acid dehydrogenases.

P. Engel, 2011, Biochemical Society transactions.

The –SH Protection Method for Determining Accurate Kd Values for Enzyme-Coenzyme Complexes of NAD+-Dependent Glutamate Dehydrogenase and Engineered Mutants: Evidence for Nonproductive NADPH Complexes

P. Engel, J. Griffin, 2010, Enzyme research.

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

P. Engel, A. Goyal, X. Wang, 2001, The Biochemical journal.

Construction, separation and properties of hybrid hexamers of glutamate dehydrogenase in which five of the six subunits are contributed by the catalytically inert D165S.

P. Engel, B. M. Hayden, 2001, European journal of biochemistry.

Construction of a dimeric form of glutamate dehydrogenase from Clostridium symbiosum by site-directed mutagenesis.

K. Britton, T. J. Stillman, D. Rice, 1996, Biochimica et biophysica acta.

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

P. Engel, D. Metzler, Z. Valinger, 1993, Biochemical Journal.

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

P. Engel, G. Williamson, 1984, The Biochemical journal.

On the molecular pathology of neurodegeneration in IMPDH1-based retinitis pigmentosa.

I. Alberts, A. Kennan, A. Aherne, 2004, Human molecular genetics.

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

D. Hornby, P. Engel, M. Aitchison, 1984, The Biochemical journal.

The effects of deletion mutagenesis on the pyruvate dehydrogenase complex of Escherichia coli

J. S. Miles, P. Engel, P. Srere, 1987 .

An Examination by Site-Directed Mutagenesis of Putative Key Residues in the Determination of Coenzyme Specificity in Clostridial NAD+-Dependent Glutamate Dehydrogenase

P. Engel, J. Griffin, 2011, Enzyme research.

Plasmodium falciparum glutamate dehydrogenase a is dispensable and not a drug target during erythrocytic development

Kellen L. Olszewski, S. Müller, M. Llinás, 2011, Malaria Journal.

Enhancing long-term thermal stability in mesophilic glutamate dehydrogenase from Clostridium symbiosum by eliminating cysteine residues

P. Engel, Muaawia Hamza, 2007 .

Probing the determinants of coenzyme specificity in Peptostreptococcus asaccharolyticus glutamate dehydrogenase by site‐directed mutagenesis

P. Engel, J. Carrigan, 2007, The FEBS journal.

Evidence that the greening ligand in native butyryl-CoA dehydrogenase is a CoA persulfide.

P. Engel, G. Williamson, C. Thorpe, 1982, The Journal of biological chemistry.

Green butyryl-coenzyme A dehydrogenase. An enzyme-acyl-coenzyme A complex.

P. Engel, V. Massey, 1971, The Biochemical journal.

The interpretation of abrupt transitions in Lineweaver-Burk plots.

P. Engel, 1972, The Biochemical journal.

Alteration of the quaternary structure of glutamate dehydrogenase from Clostridium symbiosum by a single mutation distant from the subunit interfaces

D. Rice, S. Harding, P. Engel, 1997, European Biophysics Journal.

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

A. Moir, P. Engel, J. Guest, 1990, Molecular microbiology.

77 Mutations of Human Medium-Chain Acyl-CoA Dehydrogenase

P. Bross, B. Andresen, P. Engel, 1998 .

Intersubunit communication in hybrid hexamers of K89L/A163G/S380A and C320S mutants of glutamate dehydrogenase from Clostridium symbiosum.

P. Engel, A. Goyal, S. Aghajanian, 1997, Biochemistry.

A circular dichroism study of the pH‐dependent activation/inactivation equilibrium in the glutamate dehydrogenase of Clostridium symbiosum

S. Martin, P. Engel, S. Syed, 1990 .

Molecular recruitment as a basis for negative dominant inheritance? propagation of misfolding in oligomers of IMPDH1, the mutated enzyme in the RP10 form of retinitis pigmentosa.

A. Aherne, P. Engel, B. Mion, 2011, Biochimica et biophysica acta.

Reversible interconversion of the functional state of the gene regulator FNR from Escherichia coli in vivo by O2 and iron availability

P. Engel, G. Unden, M. Trageser, 1991, Archives of Microbiology.

Kinetic characterisation of recombinant Corynebacterium glutamicum NAD+-dependent LDH over-expressed in E. coli and its rescue of an lldD− phenotype in C. glutamicum: the issue of reversibility re-examined

P. Engel, A. Guyonvarch, Michael A. Sharkey, 2011, Archives of Microbiology.

Glutamate Dehydrogenases: The Why and How of Coenzyme Specificity

P. Engel, 2013, Neurochemical Research.

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

S. Martin, P. Engel, S. Aghajanian, 1995, Biochemical Journal.

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

P. Engel, S. Aghajanian, T. P. Walsh, 2008, Protein science : a publication of the Protein Society.

A monomeric mutant of Clostridium symbiosum glutamate dehydrogenase: Comparison with a structured monomeric intermediate obtained during refolding

T. J. Stillman, D. Rice, P. Engel, 1998, Protein science : a publication of the Protein Society.

Apparent negative co-operativity and substrate inhibition in overexpressed glutamate dehydrogenase from Escherichia coli.

P. Engel, Michael A. Sharkey, 2008, FEMS microbiology letters.

Re-activation of GDH(s) from Halobacterium salinarum, cloned and overexpressed in Escherichia coli

P. Engel, N. Munawar, 2007 .

Crystallization and preliminary structural analyses of glutamate dehydrogenase from Peptoniphilus asaccharolyticus.

P. Engel, J. Carrigan, Amir R. Khan, 2010, Acta crystallographica. Section F, Structural biology and crystallization communications.

Crystal structure of a chimaeric bacterial glutamate dehydrogenase.

P. Engel, Amir R. Khan, T. Oliveira, 2016, Acta crystallographica. Section F, Structural biology communications.

Insights into the mechanism of domain closure and substrate specificity of glutamate dehydrogenase from Clostridium symbiosum.

K. Britton, T. J. Stillman, D. Rice, 1999, Journal of molecular biology.

Spontaneous chemical reversion of an active site mutation: deamidation of an asparagine residue replacing the catalytic aspartic acid of glutamate dehydrogenase.

P. Engel, J. Dean, K. Geoghegan, 2005, Biochemistry.

The specificity and kinetic mechanism of branched‐chain amino acid aminotransferase from Escherichia coli studied with a new improved coupled assay procedure and the enzyme's potential for biocatalysis

P. Engel, Xuejing Yu, Xingguo Wang, 2014, The FEBS journal.

Purification and characterisation of a serine peptidase from the marine psychrophile strain PA-43.

P. Engel, J. Irwin, A. Lanzetti, 2001, FEMS microbiology letters.

Evolution of Enzyme Regulator Sites: Evidence for Partial Gene Duplication from Amino-acid Sequence of Bovine Glutamate Dehydrogenase

P. Engel, 1973, Nature.

Alteration in relative activities of phenylalanine dehydrogenase towards different substrates by site‐directed mutagenesis

D. Rice, P. Baker, Y. Asano, 1995, FEBS letters.

Problems in the application of gel filtration to the desalting of organic compounds: retardation of aromatic and heteroaromatic anions by commonly used salts.

P. Engel, 1977, Analytical biochemistry.

Medium chain acyl-CoA dehydrogenase deficiency in the United Kingdom.

A. Blakemore, P. Engel, S. Kolvraa, 1992, Progress in clinical and biological research.

Identification of three essential lysine residues probably involved in substrate binding of the NAD+ - dependent glutamate dehydrogenase of Clostridium symbiosum

K. Lilley, P. Engel, 1988 .

Clinical mutants of human glucose 6-phosphate dehydrogenase: impairment of NADP(+) binding affects both folding and stability.

P. Engel, Xiao-tao Wang, 2009, Biochimica et biophysica acta.

Biochemical characterisation of mutations of human medium-chain acyl-CoA dehydrogenase.

P. Bross, B. Andresen, P. Engel, 1999, Advances in experimental medicine and biology.

Determinants of substrate specificity in the superfamily of amino acid dehydrogenases.

D W Rice, T. J. Stillman, D. Rice, 1997, Biochemistry.