T. K. Sundaram

Regulation of isocitrate dehydrogenase by phosphorylation in Escherichia coli K-12 and a simple method for determining the amount of inactive phosphoenzyme.

Edlin, J D, Sundaram, T K

In several Escherichia coli K-12 strains grown on a limiting concentration of glucose, isocitrate dehydrogenase (IDH) was inactivated about 90% after cessation of growth upon exhaustion of the...

Malate dehydrogenases from actinomycetes: structural comparison of Thermoactinomyces enzyme with other actinomycete and Bacillus enzymes.

Smith, K, Sundaram, T K, Kernick, M

Malate dehydrogenases from bacteria belonging to the genus Thermoactinomyces are tetrameric, like those from Bacillus spp., and exhibit a high degree of structural homology to Bacillus malate...

Structural basis of the thermostability of monomeric malate synthase from a thermophilic Bacillus.

Chell, R M, Sundaram, T K

Malate synthases from a thermophilic Bacillus and Escherichia coli have been isolated in a high state of purity. Molecular weights of these two proteins determined in the native state and after...

Occurrence of phosphenolpyruvate carboxylase in the extremely thermophilic bacterium Thermus aquaticus.

Bridger, G P, Sundaram, T K

In the extreme thermophile Thermus aquaticus, phosphoenolpyruvate carboxylase catalyzes carbon dioxide fixation on the C3 metabolite phosphoenolpyruvate, producing oxaloacetate. In a moderately...

Isocitrate Lyase from a Thermophilic Bacillus: Effect of Salts on Enzyme Activity

Griffiths, M. W., Sundaram, T. K.

The isocitrate lyase from a thermophilic Bacillus is activated about threefold by a variety of salts. Such strong stimulation of activity is not seen with isocitrate lyase from the mesophiles,...

Chromosomal Location of a Gene Defining Nicotinamide Deamidase in Escherichia coli

Dickinson, Ellen S., Sundaram, T. K.

A gene specifying the enzyme nicotinamide deamidase has been mapped, by the interrupted mating technique, at about 33 min on the chromosome of Escherichia coli K-12.

Regulation of myo-Inositol Catabolism in Aerobacter aerogenes

Sundaram, T. K.

A mutant of Aerobacter aerogenes produces constitutively the series of enzymes that mediates the degradation of myo-inositol and which in the wildtype strain is inducible. When grown on l-histidine,...

Nature of the Complementation Products Formed by a Complementing Mutant of Neurospora crassa

Sundaram, T. K., Fincham, J. R. S.

The mutant am-14 produces no active nicotinamide adenine dinucleotide phosphate-linked glutamate dehydrogenase (GDH) and no protein showing immunological cross-reaction with the enzyme. Nevertheless,...

Physiological Role of Pyruvate Carboxylase in a Thermophilic Bacillus

Sundaram, T. K.

A prototrophic, thermophilic bacillus is in a state of biotin insufficiency when grown in medium consisting of inorganic salts and a carbon source. The effect of this biotin deficiency on the growth...

Energetics of Bacillus stearothermophilus growth: molar growth yield and temperature effects on growth efficiency.

Coultate, T P, Sundaram, T K

The major growth yield of a prototrophic strain of Bacillus stearothermophilus under aerobic conditions on salts medium containing ammonium nitrate as the nitrogen source and glucose or succinate as...

Catalytic-rate improvement of a thermostable malate dehydrogenase by a subtle alteration in cofactor binding.

Alldread, R M, Halsall, D M, Clarke, A R, Sundaram, T K, Atkinson, T, Scawen, M D, ...

The nucleotide-binding fold of many NAD(+)-dependent dehydrogenases contains a conserved acidic amino acid residue which hydrogen-bonds with the 2'- and 3'-hydroxy groups of the adenine-ribose of the...

Synthesis of pyruvate carboxylase from its apoenzyme and (+)-biotin in Bacillus stearothermophilus. Purification and properties of the apoenzyme and the holoenzyme synthetase

Cazzulo, J. J., Sundaram, T. K., Dilks, Susan N., Kornberg, H. L.

1. Methods are described for the assay and purification of pyruvate apocarboxylase and pyruvate holocarboxylase synthetase from biotin-deficient Bacillus stearothermophilus. 2. Pyruvate...

Synthesis of pyruvate carboxylase from its apoenzyme and (+)-biotin in Bacillus stearothermophilus. Mechanism and control of the reaction

Sundaram, T. K., Cazzulo, J. J., Kornberg, H. L.

1. Acetyl-CoA acts as a positive allosteric effector in the formation of active pyruvate carboxylase from its apoenzyme, ATP and (+)-biotin which is catalysed by holoenzyme synthetase; this effect is...

Isolation and characterization of isocitrate lyase from a thermophilic Bacillus sp.

Chell, R M, Sundaram, T K, Wilkinson, A E

Isocitrate lyase was isolated in homogeneous state from a thermophilic Bacillus. The enzyme has a mol.wt. of 180000 and a pI of 4.5 and contains threonine as the N-terminal residue. It resembles in...

Simple efficient methods for the isolation of malate dehydrogenase from thermophilic and mesophilic bacteria.

Wright, I P, Sundaram, T K

Malate dehydrogenase from a number of bacteria drawn from several genera and representing the mesophilic, moderately thermophilic and extremely thermophilic classes was isolated by procedures which...

Tetrameric malate dehydrogenase from a thermophilic Bacillus: cloning, sequence and overexpression of the gene encoding the enzyme and isolation and characterization of the recombinant enzyme.

Wynne, S A, Nicholls, D J, Scawen, M D, Sundaram, T K

The gene encoding the tetrameric malate dehydrogenase (MDH) in a thermophilic Bacillus species (BI) has been cloned in an Escherichia coli plasmid. The nucleotide sequence of the gene, the first to...

Regulation of isocitrate dehydrogenase by phosphorylation in Escherichia coli K-12 and a simple method for determining the amount of inactive phosphoenzyme.

Edlin, J D, Sundaram, T K

In several Escherichia coli K-12 strains grown on a limiting concentration of glucose, isocitrate dehydrogenase (IDH) was inactivated about 90% after cessation of growth upon exhaustion of the...

Malate dehydrogenases from actinomycetes: structural comparison of Thermoactinomyces enzyme with other actinomycete and Bacillus enzymes.

Smith, K, Sundaram, T K, Kernick, M

Malate dehydrogenases from bacteria belonging to the genus Thermoactinomyces are tetrameric, like those from Bacillus spp., and exhibit a high degree of structural homology to Bacillus malate...

Structural basis of the thermostability of monomeric malate synthase from a thermophilic Bacillus.

Chell, R M, Sundaram, T K

Malate synthases from a thermophilic Bacillus and Escherichia coli have been isolated in a high state of purity. Molecular weights of these two proteins determined in the native state and after...

Occurrence of phosphenolpyruvate carboxylase in the extremely thermophilic bacterium Thermus aquaticus.

Bridger, G P, Sundaram, T K

In the extreme thermophile Thermus aquaticus, phosphoenolpyruvate carboxylase catalyzes carbon dioxide fixation on the C3 metabolite phosphoenolpyruvate, producing oxaloacetate. In a moderately...

Isocitrate Lyase from a Thermophilic Bacillus: Effect of Salts on Enzyme Activity

Griffiths, M. W., Sundaram, T. K.

The isocitrate lyase from a thermophilic Bacillus is activated about threefold by a variety of salts. Such strong stimulation of activity is not seen with isocitrate lyase from the mesophiles,...

Chromosomal Location of a Gene Defining Nicotinamide Deamidase in Escherichia coli

Dickinson, Ellen S., Sundaram, T. K.

A gene specifying the enzyme nicotinamide deamidase has been mapped, by the interrupted mating technique, at about 33 min on the chromosome of Escherichia coli K-12.

Regulation of myo-Inositol Catabolism in Aerobacter aerogenes

Sundaram, T. K.

A mutant of Aerobacter aerogenes produces constitutively the series of enzymes that mediates the degradation of myo-inositol and which in the wildtype strain is inducible. When grown on l-histidine,...

Nature of the Complementation Products Formed by a Complementing Mutant of Neurospora crassa

Sundaram, T. K., Fincham, J. R. S.

The mutant am-14 produces no active nicotinamide adenine dinucleotide phosphate-linked glutamate dehydrogenase (GDH) and no protein showing immunological cross-reaction with the enzyme. Nevertheless,...

Physiological Role of Pyruvate Carboxylase in a Thermophilic Bacillus

Sundaram, T. K.

A prototrophic, thermophilic bacillus is in a state of biotin insufficiency when grown in medium consisting of inorganic salts and a carbon source. The effect of this biotin deficiency on the growth...

Energetics of Bacillus stearothermophilus growth: molar growth yield and temperature effects on growth efficiency.

Coultate, T P, Sundaram, T K

The major growth yield of a prototrophic strain of Bacillus stearothermophilus under aerobic conditions on salts medium containing ammonium nitrate as the nitrogen source and glucose or succinate as...

Catalytic-rate improvement of a thermostable malate dehydrogenase by a subtle alteration in cofactor binding.

Alldread, R M, Halsall, D M, Clarke, A R, Sundaram, T K, Atkinson, T, Scawen, M D, ...

The nucleotide-binding fold of many NAD(+)-dependent dehydrogenases contains a conserved acidic amino acid residue which hydrogen-bonds with the 2'- and 3'-hydroxy groups of the adenine-ribose of the...

Synthesis of pyruvate carboxylase from its apoenzyme and (+)-biotin in Bacillus stearothermophilus. Purification and properties of the apoenzyme and the holoenzyme synthetase

Cazzulo, J. J., Sundaram, T. K., Dilks, Susan N., Kornberg, H. L.

1. Methods are described for the assay and purification of pyruvate apocarboxylase and pyruvate holocarboxylase synthetase from biotin-deficient Bacillus stearothermophilus. 2. Pyruvate...

Synthesis of pyruvate carboxylase from its apoenzyme and (+)-biotin in Bacillus stearothermophilus. Mechanism and control of the reaction

Sundaram, T. K., Cazzulo, J. J., Kornberg, H. L.

1. Acetyl-CoA acts as a positive allosteric effector in the formation of active pyruvate carboxylase from its apoenzyme, ATP and (+)-biotin which is catalysed by holoenzyme synthetase; this effect is...

Isolation and characterization of isocitrate lyase from a thermophilic Bacillus sp.

Chell, R M, Sundaram, T K, Wilkinson, A E

Isocitrate lyase was isolated in homogeneous state from a thermophilic Bacillus. The enzyme has a mol.wt. of 180000 and a pI of 4.5 and contains threonine as the N-terminal residue. It resembles in...

Simple efficient methods for the isolation of malate dehydrogenase from thermophilic and mesophilic bacteria.

Wright, I P, Sundaram, T K

Malate dehydrogenase from a number of bacteria drawn from several genera and representing the mesophilic, moderately thermophilic and extremely thermophilic classes was isolated by procedures which...

Tetrameric malate dehydrogenase from a thermophilic Bacillus: cloning, sequence and overexpression of the gene encoding the enzyme and isolation and characterization of the recombinant enzyme.

Wynne, S A, Nicholls, D J, Scawen, M D, Sundaram, T K

The gene encoding the tetrameric malate dehydrogenase (MDH) in a thermophilic Bacillus species (BI) has been cloned in an Escherichia coli plasmid. The nucleotide sequence of the gene, the first to...