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To Find the Nucleotide and Protein Sequence of AMYLASE in Homo Sapiens in FASTA Format

Jyoti Raj


Comprehensive analysis of current enzymes with α-amylase activity (AAMY) belonging to family 13 of glycoside hydrolases (arrangements of 144 archaea, bacteria, and eukaryotes from different species of GH13; 87). Offers. This study aims to deepen our knowledge of the evolutionary molecular relationships between the sequences of the A and B domains, with a particular focus on the correlation between what is observed in structure and the evolution of proteins. A-domain multi-alignment distinguishes between 2 clusters for sequences from archaea, 8 for sequences from bacterial organisms, and 3 for sequences from eukaryotes. Bacterial clusters do not follow a rigorous taxonomic pathway. In fact, they are pretty scattered. Comparing the A domains of sequences belonging to different kingdoms, we find that different pairs of clusters are significantly similar. Using either sequence similarity to the crystallized structure or secondary structure prediction methods, the eight putative β-strands that make up the β-sheet of the TIM barrel of all AAMY A domains are identified and packed in them. I checked. We also found "hidden homology" in the TIM barrel, an invariant Gly located upstream of the sequence from the conserved Asp of β-strand 3. This Gly precedes the α-helix and is actively involved in capping its N-terminus in the capping box. In all cases, the Shelman motif covers the C-terminus of this helix.



α-amylase, Eukaryotes, Crystallized, Hidden homology, Enzymes

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