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Structure and function of l lactate dehydrogenases ec 1.1.1.27 from thermophilic and mesophilic bacteria 3. the primary structure of thermophilic lactate dehydrogenase from bacillus stearothermophilus hydroxylamine o iodoso benzoic acid and tryptic fragments the complete amino acid sequence


Structure and function of l lactate dehydrogenases ec 1.1.1.27 from thermophilic and mesophilic bacteria 3. the primary structure of thermophilic lactate dehydrogenase from bacillus stearothermophilus hydroxylamine o iodoso benzoic acid and tryptic fragments the complete amino acid sequence



Hoppe Seyler's Zeitschrift fuer Physiologische Chemie 364(7): 893-910



Based on the partial sequence of the cyanogen bromide fragments, the amino-acid sequence of thermophilic lactate dehydrogenase from B. stearothermophilus was completed by the preparation and sequencing (sequenator, carboxypeptidase A and Y) of further overlapping fragments. Suitable peptide fragments were obtained by lactate dehydrogenase cleavage with hydroxylamine, o-iodosobenzoic acid and trypsin. The polypeptide chain of thermophilic lactate dehydrogenase from B. stearothermophilus consists of 317 amino-acid residues. While sequence homology with mesophilic lactate dehydrogenase of higher organisms reaches 35%, it is substantially higher with this mesophilic enzyme of bacillae (> 60%, B. megaterium, B. subtilis). The secondary structure elements and amino-acid residues of the active site of thermophilic lactate dehydrogenase deducted from primary structure data were compared with those from the mesophilic enzyme; the same was done for the internal sequence homology at the nucleotide-binding units. A comparative structure analysis (matrix system) based on the primary structure data of thermophilic enzyme should provide insight into the characteristic structure differences between thermophilic and mesophilic lactate dehydrogenase.

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Structure and function of L-lactate dehydrogenases from thermophilic and mesophilic bacteria. III) the primary structure of thermophilic lactate dehydrogenase from Bacillus stearothermophilus. Hydroxylamine-, o-iodosobenzoic acid- and tryptic-fragments. the complete amino-acid sequence. Hoppe-Seyler's Zeitschrift für Physiologische Chemie 364(7): 893-909, 1983

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