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

Authors

  • Jyoti Raj Student, Department of Biotechnology, Ghanshyam PG College, Varanasi, Uttar Pradesh, India

Keywords:

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

Abstract

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.

 

References

Aghajari, N., Haser, R., Feller, G. and Gerday, C., 1998. Crystal structures of the psychrophilic α‐amylase from Alteromonas haloplanctis in its native form and complexed with an inhibitor. Protein Science, 7 (3), pp. 564–572.

1998b. Structures of the psychrophilic Alteromonas haloplanctis α-amylase give insights into cold adaptation at a molecular level. Structure 6: 1503–1516.

Aurora, R., and G.D. Rose. 1998. Helix capping. Protein Sci. 7: 21–38.

Bairoch, A., and R. Apweiler. 1999. The SWISS-PROT protein sequence data bank and its supplement TrEMBL in 1999. Nucleic Acids Res. 27: 49–54.

Benson, D.A., I. Karsch-Mizrachi, D.J. Lipman, J. Ostell, B.A. Rapp, and D.L. Wheeler. 2000. GenBank. Nucleic Acids Res. 28: 15–18.

Berman, H.M., Westbrook, J., Feng, Z., Gilliland, G., Bhat, T.N., Weissig, H., Shindyalov, I.N. and Bourne, P.E., 2000. The protein data bank. Nucleic acids research, 28(1), pp.235–242.

Boel, E., Brady, L., Brzozowski, A.M., Derewenda, Z., Dodson, G.G., Jensen, V.J., Petersen, S.B., Swift, H., Thim, L. and Woldike, H.F., 1990. Calcium binding in. alpha.-amylases: an x-ray diffraction study at 2.1-. ANG. resolution of two enzymes from Aspergillus. Biochemistry, 29 (26), pp. 6244–6249.

Bompard-Gilles, C., Rousseau, P., Rougé, P. and Payan, F., 1996. Substrate mimicry in the active center of a mammalian α amylase: structural analysis of an enzyme–inhibitor complex. Structure, 4 (12), pp. 1441–1452.

Brayer, G.D., Luo, Y. and Withers, S.G., 1995. The structure of human pancreatic α‐amylase at 1.8 Å resolution and comparisons with related enzymes. Protein Science, 4 (9), pp. 1730–1742.

Brzozowski, A.M. and Davies, G.J., 1997. Structure of the Aspergillus oryzae α-amylase complexed with the inhibitor acarbose at 2.0 Å resolution. Biochemistry, 36 (36), pp. 10837–10845.

del-Rio, G., Morett, E. and Soberon, X., 1997. Did cyclodextrin glycosyltransferases evolve from α-amylases?. FEBS letters, 416(2), pp.221-224.

Fujimoto, Z., Takase, K., Doui, N., Momma, M., Matsumoto, T. and Mizuno, H., 1998. Crystal structure of a catalytic-site mutant α-amylase from Bacillus subtilis complexed with maltopentaose. Journal of molecular biology, 277 (2), pp. 393–407.

Downloads

Published

2022-03-12

Issue

Vol. 10 No. 3 (2021)

Section

Review Article

License

Declaration and Copyright Transfer Form

(to be completed by authors)

I/ We, the undersigned author(s) of the submitted manuscript, hereby declare, that the above manuscript which is submitted for publication in the STM Journals(s), is not published already in part or whole (except in the form of abstract) in any journal or magazine for private or public circulation, and, is not under consideration of publication elsewhere.

  • I/We will not withdraw the manuscript after 1 week of submission as I have read the Author Guidelines and will adhere to the guidelines.
  • I/We Author(s ) have niether given nor will give this manuscript elsewhere for publishing after submitting in STM Journal(s).
  • I/ We have read the original version of the manuscript and am/ are responsible for the thought contents embodied in it. The work dealt in the manuscript is my/ our own, and my/ our individual contribution to this work is significant enough to qualify for authorship.
  •  I/We also agree to the authorship of the article in the following order:

Author’s name                                    

 

1. ________________

2. ________________

3. ________________

4. ________________

 

We  Author(s) tick this box and would request you to consider it as our signature as we agree to the terms of this Copyright Notice, which will apply to this submission if and when it is published by this journal.