J. Holbrook

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A specific, highly active malate dehydrogenase by redesign of a lactate dehydrogenase framework.

H. Muirhead, H. Wilks, K. Hart, 1988, Science.

The rates of defined changes in protein structure during the catalytic cycle of lactate dehydrogenase.

K. Hart, A. Clarke, J. Holbrook, 1985, Biochimica et biophysica acta.

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

K. Hart, W. Chia, D. Barstow, 1987, Biochimica et biophysica acta.

Design and synthesis of new enzymes based on the lactate dehydrogenase framework.

H. Muirhead, H. Wilks, C. Dunn, 1991, Philosophical transactions of the Royal Society of London. Series B, Biological sciences.

An investigation of the contribution made by the carboxylate group of an active site histidine-aspartate couple to binding and catalysis in lactate dehydrogenase.

H. Wilks, W. Chia, D. Barstow, 1988, Biochemistry.

Site-directed mutagenesis reveals role of mobile arginine residue in lactate dehydrogenase catalysis

W. Chia, D. Barstow, T. Atkinson, 1986, Nature.

A single mutation in the NAD-specific formate dehydrogenase from Candida methylica allows the enzyme to use NADP

A. Clarke, J. Holbrook, R. Sessions, 2001, Biotechnology Letters.

NADH binding to porcine mitochondrial malate dehydrogenase.

D. M. Parker, S. Evans, J. Holbrook, 1979, The Journal of biological chemistry.

Cloning, sequence and expression of the lactate dehydrogenase gene from the human malaria parasite, Plasmodium vivax

J. Holbrook, R. Sessions, R. L. Brady, 2004, Biotechnology Letters.

4 Lactate Dehydrogenase

Steven J. Steindel, Anders Liljas, Michael G. Rossmann, 1975 .

On the effect on specificity of Thr246----Gly mutation in L-lactate dehydrogenase of Bacillus sterothermophilus.

H. Wilks, K. Hart, J. Holbrook, 1989, Biochemical and biophysical research communications.

1H NMR studies of TYR‐237 of lactate dehydrogenase

D. M. Parker, J. Holbrook, G. Roberts, 1981, FEBS letters.

Reactivity of the essential thiol group of lactate dehydrogenase and substrate binding.

J. Holbrook, R. Stinson, 1970, The Biochemical journal.

The multiple complexes formed by the interaction of platelet factor 4 with heparin.

J. Holbrook, P. E. Bock, D. Pepper, 1980, The Biochemical journal.

A model of Plasmodium falciparum lactate dehydrogenase and its implications for the design of improved antimalarials and the enhanced detection of parasitaemia.

A. Clarke, J. Holbrook, R. Sessions, 1997, Protein engineering.

The interaction of platelet factor 4 with heparins of different chain length.

J. Holbrook, D. Pepper, M. Luscombe, 1984, Biochimica et biophysica acta.

Low-resolution structure of the complex of human blood platelet factor 4 with heparin determined by small-angle neutron scattering.

J. Holbrook, D. Pepper, G. Poland, 1986, Biochimica et biophysica acta.

pH-dependent changes of intrinsic fluorescence of chemically modified liver alcohol dehydrogenases.

D. M. Parker, J. Holbrook, B. Plapp, 1978, The Biochemical journal.

The effect of the chain length of heparin on its interaction with lipoprotein lipase.

A. Clarke, J. Holbrook, M. Luscombe, 1983, Biochimica et biophysica acta.

Protein fluorescence of lactate dehydrogenase.

J. Holbrook, 1972, The Biochemical journal.

Differences in the protein fluorecence of the two iron(III)-binding sites of ovotransferrin.

J. Holbrook, R. W. Evans, 1975, The Biochemical journal.

Malate dehydrogenase of the cytosol. Preparation and reduced nicotinamide-adenine dinucleotide-binding studies.

J. Holbrook, S. Spragg, A. Lodola, 1978, The Biochemical journal.

The transfer of platelet factor 4 from its proteoglycan carrier to natural and synthetic polymers.

J. Holbrook, D. Pepper, M. Luscombe, 1981, Biochimica et biophysica acta.

Multiple complexes of thrombin and heparin.

J. Holbrook, M. Luscombe, P. Feldman, 1986, Biochimica et biophysica acta.

The stability and hydrophobicity of cytosolic and mitochondrial malate dehydrogenases and their relation to chaperonin‐assisted folding

T. Atkinson, A. Clarke, J. Holbrook, 1994, FEBS letters.

Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: implications for the mechanism of assisted protein folding.

T. Atkinson, A. Clarke, J. Holbrook, 1993, Biochemistry.

The use of an altered specificity engineered enzyme for asymmetric synthesis: enantioselective reduction of 4-methyl-2-oxopent-3-enoic acid

J. Holbrook, R. Sessions, Thomas V. Lee, 1992 .

Ethidium bromide as a cooperative effector of a DNA structure.

F. Pohl, J. Holbrook, T. Jovin, 1972, Proceedings of the National Academy of Sciences of the United States of America.

Malate dehydrogenase of the cytosol. Ionizations of the enzyme-reduced-coenzyme complex and a comparison with lactate dehydrogenase.

D. M. Parker, J. Holbrook, A. Lodola, 1978, The Biochemical journal.

Ionic properties of an essential histidine residue in pig heart lactate dehydrogenase.

J. Holbrook, V. Ingram, V. Ingram, 1973, The Biochemical journal.

Approaches to the study of enzyme mechanisms lactate dehydrogenase

J. Holbrook, H. Gutfreund, 1973, FEBS letters.

The importance of SH-groups for enzymic activity. 7. The amino acid sequence around the essential SH-group of pig heart lactate dehydrogenase, isoenzyme I.

J. Holbrook, G. Pfleiderer, M. Volz, 1967, European journal of biochemistry.

The site at which 4-iodoacetamidosalicylate reacts with glutamate dehydrogenases.

J. Holbrook, R. Wallis, P. A. Roberts, 1973, The Biochemical journal.

A peptide containing a reactive lysyl group from ox liver glutamate dehydrogenase.

J. Holbrook, R. Jeckel, 1969, The Biochemical journal.

Duck liver 'malic' enzyme. Expression in Escherichia coli and characterization of the wild-type enzyme and site-directed mutants.

B. Roe, R. Wilson, R. Feeney, 1992, The Biochemical journal.

The reaction of a histidine residue in glutamate dehydrogenase with diethyl pyrocarbonate.

J. Holbrook, R. Wallis, 1973, The Biochemical journal.

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

J. Holbrook, R. Stinson, 1973, The Biochemical journal.

Histidine residues and the enzyme activity of pig heart supernatant malate dehydrogenase.

J. Holbrook, N. Illsley, A. Lodola, 1974, The Biochemical journal.

Equilibrium binding of nicotinamide nucleotides to lactate dehydrogenases.

J. Holbrook, R. Stinson, R. A. Stinson, 1973, The Biochemical journal.

Malate dehydrogenase of the cytosol. A kinetic investigation of the reaction mechanism and a comparison with lactate dehydrogenase.

D. M. Parker, J. Holbrook, J. Shore, 1978, The Biochemical journal.

Protein fluorescence of nicotinamide nucleotide-dependent dehydrogenases.

J. Holbrook, M. Gore, R. W. Evans, 1972, The Biochemical journal.

The effect of modifying lysine-126 on the physical, catalytic and regulatory properties of bovine liver glutamate dehydrogenase.

J. Holbrook, R. Wallis, 1973, The Biochemical journal.

Reversible, covalent modification of the essential cysteine residues of pig heart lactate dehydrogenase

J. Holbrook, R. Jeckel, 1967 .

The identification of intermediates in the reaction of pig heart lactate dehydrogenase with its substrates.

J. Holbrook, J. Whitaker, N. Bennett, 1974, The Biochemical journal.

Use of the sulphite adduct of nicotinamide-adenine dinucleotide to study ionizations and the kinetics of lactate dehydrogenase and malate dehydrogenase.

D. M. Parker, J. Holbrook, A. Lodola, 1978, The Biochemical journal.

The importance of SH-groups for enzymic activity. V. The coenzyme-binding capacity of pig heart lactate dehydrogenase, isozyme I, after inhibition by various maleinimides.

J. Holbrook, 1966, Biochemische Zeitschrift.

The amino acid sequence around the reactive cysteine residue in human plasma Factor XIII (Short Communication)

J. Holbrook, R. Cooke, I. B. Kingston, 1973 .

Kinetic analysis of experiments involving the single turnover of an enzyme.

J. Holbrook, J. Südi, H. Gutfreund, 1976, Biochemical Journal.

NAD(+)-dependent D-2-hydroxyisocaproate dehydrogenase of Lactobacillus delbrueckii subsp. bulgaricus. Gene cloning and enzyme characterization.

J. Holbrook, D. Garmyn, P. Hols, 1994, European journal of biochemistry.

D175 discriminates between NADH and NADPH in the coenzyme binding site of Lactobacillus delbrueckii subsp. bulgaricus D-lactate dehydrogenase.

J. Holbrook, J. Delcour, N. Bernard, 1995, Biochemical and biophysical research communications.

Designs for a broad substrate specificity keto acid dehydrogenase.

H. Wilks, W. Chia, T. Atkinson, 1990, Biochemistry.

Amino acid sequence of the L-lactate dehydrogenase of Bacillus caldotenax deduced from the nucleotide sequence of the cloned gene.

D. Barstow, T. Atkinson, A. Clarke, 1987, European journal of biochemistry.

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

W. Chia, D. Barstow, T. Atkinson, 1986, Gene.

Substitution of the amino acid at position 102 with polar and aromatic residues influences substrate specificity of lactate dehydrogenase

T. Atkinson, A. Clarke, J. Holbrook, 1994, Journal of protein chemistry.

Opportunities and limits in creating new enzymes. Experiences with the NAD-dependent lactate dehydrogenase frameworks of humans and bacteria.

H. Wilks, A. Clarke, J. Holbrook, 1992, Annals of the New York Academy of Sciences.

Opportunities and Limits in Creating New Enzymes

J. Holbrook, D. Emery, A. Clarke, 1992 .

Engineering surface loops of proteins--a preferred strategy for obtaining new enzyme function.

A. Clarke, J. Holbrook, R. Sessions, 1994, Trends in biotechnology.

Cancer-associated lactate dehydrogenase is a tyrosylphosphorylated form of human LDH-A, skeletal muscle isoenzyme.

J. Holbrook, M. J. Evans, G. Clinton, 1988, Cancer investigation.

Isolation, sequence and overexpression of the gene encoding NAD-dependent formate dehydrogenase from the methylotrophic yeast Candida methylica.

J. Holbrook, S. Allen, 1995, Gene.

From analysis to synthesis: new ligand binding sites on the lactate dehydrogenase framework. Part II.

T. Atkinson, A. Clarke, J. Holbrook, 1989, Trends in biochemical sciences.

A single amino acid substitution deregulates a bacterial lactate dehydrogenase and stabilizes its tetrameric structure.

W. Chia, D. Barstow, T. Atkinson, 1987, Biochimica et biophysica acta.

The use of site-directed mutagenesis and time-resolved fluorescence spectroscopy to assign the fluorescence contributions of individual tryptophan residues in Bacillus stearothermophilus lactate dehydrogenase.

K. Hart, W. Chia, D. Barstow, 1987, Biochimica et biophysica acta.

The molecular pathway by which fructose 1,6-bisphosphate induces the assembly of a bacterial lactate dehydrogenase

T. Atkinson, A. Clarke, J. Holbrook, 1986 .

The assembly mechanism of the lactate dehydrogenase tetramer from Bacillus stearothermophilus. The equilibrium relationships between quaternary structure and the binding of fructose 1,6-biphosphate, NADH and oxamate

J. W. Campbell, T. Atkinson, A. Clarke, 1985 .

Changes in the state of subunit association of lactate dehydrogenase from Bacillus stearothermophilus.

A. Clarke, J. Holbrook, A. D. Waldman, 1985, Biochimica et biophysica acta.

A prediction of the three-dimensional structure of maize NADP+-dependent malate dehydrogenase which explains aspects of light-dependent regulation unique to plant enzymes

Richard B. Sessions, Richard M. Jackson, J. John Holbrook, 1992, J. Comput. Aided Mol. Des..

Removal of substrate inhibition in a lactate dehydrogenase from human muscle by a single residue change

A. Clarke, J. Holbrook, R. Sessions, 1996, FEBS letters.

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

H. Muirhead, J. Holbrook, D. Wigley, 1992, Journal of molecular biology.

Binding of a chaperonin to the folding intermediates of lactate dehydrogenase.

J. Holbrook, I. Badcoe, S. Wood, 1991, Biochemistry.

Expression of the copy DNA for human A4 and B4 L-lactate dehydrogenases in Escherichia coli.

W. Chia, D. Barstow, T. Atkinson, 1990, Biochimica et biophysica acta.

The energetics and cooperativity of protein folding: a simple experimental analysis based upon the solvation of internal residues.

T. Atkinson, A. Clarke, J. Holbrook, 1993, Biochemistry.

The importance of arginine 102 for the substrate specificity of Escherichia coli malate dehydrogenase.

T. Atkinson, A. Clarke, J. Holbrook, 1992, Biochemical and biophysical research communications.

Source of catalysis in the lactate dehydrogenase system. Ground-state interactions in the enzyme-substrate complex.

A. Clarke, J. Holbrook, R. Callender, 1994, Biochemistry.

Crystallization of a ternary complex of lactate dehydrogenase from Bacillus stearothermophilus.

H. Muirhead, J. Holbrook, D. Wigley, 1988, Journal of molecular biology.

Guided evolution of enzymes with new substrate specificities.

J. Holbrook, R. Sessions, K. Moreton, 1996, Journal of molecular biology.

Role of solvent reorganization energies in the catalytic activity of enzymes

Arieh Warshel, Richard M. Jackson, Arpita Yadav, 1991 .

Evaluation and Testing of Noble Metals Surrogates

B. D. Macisaac, J. Holbrook, S. Sundaram, 2002 .

The influence of chaperonins on protein folding. A mechanism for increasing the yield of the native form.

A. Clarke, J. Holbrook, S. Burston, 1992, Annals of the New York Academy of Sciences.

The mechanism of activation of lipoprotein lipase by apolipoprotein C-II. The formation of a protein-protein complex in free solution and at a triacylglycerol/water interface.

A. Clarke, J. Holbrook, 1985, Biochimica et Biophysica Acta.

Protein-protein interactions in blood clotting. The use of polarization of fluorescence to measure the dissociation of plasma factor XIIIa.

J. Holbrook, B. Lewis, J. Shore, 1978, The Biochemical journal.

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

T. Atkinson, A. Clarke, J. Holbrook, 1993, European journal of biochemistry.

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.

K. Hart, W. Chia, D. Barstow, 1988, Biochemical and biophysical research communications.

The greater strength of arginine: carboxylate over lysine carboxylate ion pairs implications for the design of novel enzymes and drugs.

K. Hart, J. Holbrook, D. Wigley, 1987, Biochemical and biophysical research communications.

The importance of arginine 171 in substrate binding by Bacillus stearothermophilus lactate dehydrogenase.

K. Hart, W. Chia, D. Barstow, 1987, Biochemical and biophysical research communications.

The oxaloacetate reductase activity of vertebrate lactate dehydrogenase.

D. M. Parker, J. Holbrook, 1981, The International journal of biochemistry.

The engineering of a more thermally stable lactate dehydrogenase by reduction of the area of a water-accessible hydrophobic surface.

H. Muirhead, C. Dunn, W. Chia, 1987, Biochimica et biophysica acta.

Correlation of the enzyme activities of Bacillus stearothermophilus lactate dehydrogenase on three substrates with the results of molecular dynamics/energy minimization conformational searching

J. Holbrook, T. Dafforn, R. Sessions, 1997, Proteins.

Bioinformatics and type II G-protein-coupled receptors.

J. Holbrook, S. Jupe, S. Foord, 2001, Biochemical Society transactions.

A general method of domain closure is applied to phosphoglycerate kinase and the result compared with the crystal structure of a closed conformation of the enzyme

B. Bernstein, H. Muirhead, N. Chandra, 1998, Proteins.

A general method for relieving substrate inhibition in lactate dehydrogenases.

J. Holbrook, R. Sessions, J. Takei, 1999, Protein engineering.

A single amino acid substitution in lactate dehydrogenase improves the catalytic efficiency with an alternative coenzyme.

R. Feeney, A. Clarke, J. Holbrook, 1990, Biochemical and biophysical research communications.

The structure of lactate dehydrogenase from Plasmodium falciparum reveals a new target for anti-malarial design

C. Dunn, J. Holbrook, M. Banfield, 1996, Nature Structural Biology.

Alteration of enzyme specificity and catalysis by protein engineering.

H. Wilks, J. Holbrook, J.John Holbrook, 1991, Current opinion in biotechnology.

A study of the interaction between bovine cardiac-muscle cyclic AMP-dependent protein kinase and cyclic AMP using fluorescence-polarization spectroscopy.

J. Holbrook, M. Seville, P. England, 1984, The Biochemical journal.

The preparation of cyclic nucleotide-depleted regulatory subunits from type II adenosine 3':5'-monophosphate-dependent protein kinase by a nondenaturing method.

J. Holbrook, M. Seville, 1984, Analytical biochemistry.

Preparation of regulatory subunits from bovine heart cAMP-dependent protein kinase by a nondenaturing method.

J. Holbrook, M. Seville, 1988, Methods in enzymology.

Electrostatic interaction energies in lactate dehydrogenase catalysis

R. Jackson, J. Holbrook, J. Gelpi, 1993 .

13C-NMR and transient kinetic studies on lactate dehydrogenase [Cys(13CN)165]. Direct measurement of a rate-limiting rearrangement in protein structure.

J. Holbrook, A. D. Waldman, G. Roberts, 1986, Biochimica et biophysica acta.

Production of an activated form of Bacillus stearothermophilus L-2-hydroxyacid dehydrogenase by directed evolution.

J. Holbrook, S. Allen, 2000, Protein engineering.

Slow structural changes shown by the 3-nitrotyrosine-237 residue in pig heart [Tyr(3NO2)237] lactate dehydrogenase.

D. M. Parker, J. Holbrook, D. Jeckel, 1982, The Biochemical journal.

Studies on the changes in protein fluorescence and enzymic activity of aspartate aminotransferase on binding of pyridoxal 5'-phosphate.

J. Holbrook, R. W. Evans, 1974, Biochemical Journal.

The reactivities of the lysine, cysteine and tyrosine residues of pig heart lactate dehydrogenase in the presence of sulphite

J. Holbrook, G. Pfleiderer, L. Zaki, 1968, FEBS letters.

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

W. Chia, T. Atkinson, A. Clarke, 1991, Biochemistry.

[SYNTHESIS AND PROPERTIES OF PYRID-4-ONE-3-CARBOXAMIDE ADENINE DINUCLEOTIDE].

J. Holbrook, G. Pfleiderer, T. Wieland, 1963, Biochemische Zeitschrift.

Lactate Dehydrogenase (LDH)

J. Holbrook, 2002 .

Mapping motion in large proteins by single tryptophan probes inserted by site-directed mutagenesis: lactate dehydrogenase.

H. Wilks, K. Hart, W. Chia, 1987, Biochemical Society transactions.

Site-directed mutagenesis of Bacillus stearothermophilus lactate dehydrogenase

K. Hart, W. Chia, D. Barstow, 1987 .

The catalysis by heparin of the reaction between thrombin and antithrombin.

J. Holbrook, M. Luscombe, P. Feldman, 1986, Biochimica et Biophysica Acta.

D-2-hydroxy-4-methylvalerate dehydrogenase from Lactobacillus delbrueckii subsp. bulgaricus. II. Mutagenic analysis of catalytically important residues.

J. Holbrook, D. Garmyn, P. Hols, 1997, European journal of biochemistry.

Construction of a stable dimer of Bacillus stearothermophilus lactate dehydrogenase.

R. Jackson, H. Wilks, J. Holbrook, 1992, Biochemistry.

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

J. Holbrook, T. J. Nobbs, MichaelD. Scawen, 1994, The Biochemical journal.