@article {46619,
	title = {Molecular determinant for specificity: differential interaction of alpha-amylases with their proteinaceous inhibitors},
	journal = {Biochimica Et Biophysica Acta-General Subjects},
	volume = {1864},
	year = {2020},
	month = {DEC},
	pages = {129703},
	type = {Review},
	abstract = {<p>Background: alpha-Amylase inhibitors (alpha-AIs) belong to the discrete classes, and exhibited differential specificities against alpha-amylases from various sources. Several alpha-amylases and their complexes with inhibitors at the molecular level have been studied in detail. Interestingly, some alpha-AIs depict specific and selective interactions amid different insect alpha-amylases. Scope of review: There are studies to understand evolutionary variability and functional differentiation of insect alpha-amylases and their cognate inhibitors. We have examined sequence, structural, and interaction diversity between various alpha-amylases and alpha-AIs. Based on these analyses, we are providing a potential basis for the functional differentiation among certain insect a-amylases concerning mammalian counterparts and their interactions with different proteinaceous alpha-AIs. Major conclusions: Insect alpha-amylases have conserved domain architecture with differences in length, number of disulfide bonds, and secondary structure. Furthermore, few of them exhibit variable characteristics like chloride dependent activity, the presence of N-terminal glutamine residue to protect against proteolytic degradation, and loop variations near the enzyme active site. Conformation of alpha-AI protein could be an essential factor for their specificity and binding affinities towards target alpha-amylase(s). Furthermore, variation into the enzyme binding pocket residues might contribute to differential interactions with inhibitors. General significance: Molecular insights in the interactions between insect alpha-amylases and plant alpha-AI will provide the details of mechanisms assisting the inhibitor specificity. Furthermore, this information will help to design potent and effective alpha-AIs against specific alpha-amylase.</p>
},
	keywords = {Active site, alpha-amylase, alpha-amylase inhibitor, Insect, molecular interactions},
	issn = {0304-4165},
	doi = {10.1016/j.bbagen.2020.129703},
	author = {Rane, Ashwini S. and Joshi, Rakesh S. and Giri, Ashok P.}
}
