Homologous partial sequences in dehydrogenases

Mátrai, György and Darvas, Ferenc and Keleti, Tamás (1983) Homologous partial sequences in dehydrogenases. ACTA BIOCHIMICA ET BIOPHYSICA HUNGARICA, 18 (3-4). pp. 169-183. ISSN 0237-6261

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Abstract

Such details of the primary structure were sought that are common in all dehydrogenases of known amino acid sequence. Twenty-six sequences of eight kinds of dehydrogenase (D-glyceraldehyde-3-phosphate dehydrogenase, alcohol dehydrogenase, lactate dehydrogenase, glutamate dehydrogenase, glycerol-3-phosphate dehydrogenase, ribitol dehydrogenase, L-hydroxyacyl-CoA dehydrogenase and homoserine dehydrogenase) have been compared by the aid of the artificial intelligence language Prolog, the amino acids being classified into groups according to their chemical properties, and alpha-helix or beta-sheet-forming abilities. We found tetrapeptides that occurred in all dehydrogenases examined. By using these tetrapeptides as markers a population of 84 partial sequences has been described. The partial sequences constituting this population are peptides comprising 35 residues. It has been shown statistically that these peptides form a homogeneous sample as regards the frequency of occurrence of amino acid groups. This statistically homogeneous partial sequences can be regarded as homologous and it is assumed that their presence is characteristic of dehydrogenases.

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