Volume 10, Issue 10, October - 2023

Conservation of amino acid/s of enzymes of the glycolysis pathway

Author(s):Chandresh Soni 1, Khanjan Chudasama2

Abstract: Glycolysis is one of the carbohydrate metabolism in which glucose is broken down to obtain NADH, ATP and pyruvate and this process is observed from bacteria to humans. The comparison of glycolytic enzymes of Homo sapiens and Escherichia coli K-12 MG1655 is done by using various Bioinformatics tools and databases such as BLAST (Basic Local Alignment Sequence Tool) of NCBI (National Centre of Biotechnology Information), Uniport and KEGG (Kyoto Encyclopaedia of Gene and Genome ) . The glycolysis pathway and basic information of enzyme is retired from KEGG, the conserved sequence of amino acid is obtained from BLAST results, the significance of conserved amino acid or particular sequence of it is gained from database of uniport. The four major conclusions are that the evolution of enzymes has shown that single amino acids or specific sequences of amino acids can be conserved at different sequence numbers. This is observed in Phosphoglucomutase, Glyceraldehyde 3-phosphate dehydrogenase, Enolase, and pyruvate kinase. From bacteria to humans, a single amino acid change in enzymes like 6-phosphofructokinase, Phosphoglycerate kinase, and 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase is observed. BLAST results can predict many binding sites, as the sequence of amino acids responsible for it, in both organisms is the same. However, in 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase, not only is a single amino acid or sequence conserved but also the sequence number remains the exactly same.

Keywords: glycolysis, conservation of amino acid sequence, BLAST, a single amino acid mutation, prediction of binding site, 2,3-bisphosphoglycerate-dependent, Escherichia coli K-12 MG1655, Homo sapiens

DOI: 10.61165/sk.publisher.v10i10.1

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