Amino acid sequence homology in alcohol dehydrogenase
نویسندگان
چکیده
منابع مشابه
Amino acid sequence homology between pig heart lipoamide dehydrogenase and human erythrocyte glutathione reductase.
Extensive amino acid sequence homology has been found between nine tryptic peptides of pig heart lipoamide dehydrogenase (NADH:lipoamide oxidoreductase, EC 1.6.4.3] and the sequence of human erythrocyte glutathione reductase [NAD(P)H:glutathione oxidoreductase, EC 1.6.4.2]. The average homology is 40%. Six lipoamide dehydrogenase peptides are homologous with segments of the two parts of the FAD...
متن کاملFrequency and Markov chain analysis of the amino-acid sequence of human alcohol dehydrogenase alpha-chain.
The amino-acid sequences of human alcohol dehydrogenase alpha-chain (ADH1) were analysed according to two-, three- and four-amino-acid sequences. The measured frequencies and probabilities were compared with the predicted frequencies and probabilities. Of 373 two-amino-acid sequences in the ADH1, 92 (24.665%) and 32 (8.579%) sequences can be explained by the predicted frequencies and probabilit...
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Lactate dehydrogenase isolated from vertebrate tissues catalyzes the reversible oxidation of L-lactic acid to pyruvic acid. The catalysis requires nicotinamide adenine dinucleotide (NAD’) as a coenzyme and is specific for the A-hydrogen of the nicotinamide ring (1) (Fig. 1). Although the enzyme is tetrameric, no cooperative effects have been observed between subunits (2). Each identical subunit...
متن کاملAmino acid sequence around lipoic acid residues in the pyruvate dehydrogenase multienzyme complex of Escherichia coli.
Amino-acid sequences around two lipoic acid residues in the lipoate acetyltransferase component of the pyruvate dehydrogenase complex of Escherichia coli were investigated. A single amino acid sequence of 13 residues was found. A repeated amino acid sequence in the lipoate acetyltransferase chain might explain this result.
متن کاملThe complete amino acid sequence of three alcohol dehydrogenase alleloenzymes (AdhN-11, AdhS and AdhUF) from the fruitfly Drosophila melanogaster.
The sequence of three alcohol dehydrogenase alleloenzymes from the fruitfly Drosophila melanogaster has been determined by the sequencing of peptides produced by trypsin, chymotrypsin, thermolysin, pepsin and Staphylococcus aureus-V8-proteinase digestion. The amino acid sequence shows no obvious homology with the published sequences of the horse liver and yeast enzymes, and secondary structure ...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1973
ISSN: 0014-5793
DOI: 10.1016/0014-5793(73)80144-9