title: Structural features, substrate specificity, kinetic properties of insect α-amylase and specificity of plant α-amylase inhibitors.
abstract: BACKGROUND
  α-Amylase is an important digestive enzyme required for the optimal growth and development of insects. Several insect α-amylases had been purified and their physical and chemical properties were characterized. Insect α-amylases of different orders display variability in structure, properties and substrate specificity. Such diverse properties of amylases could be due to different feeding habits and gut environment of insects.
  
  
  CONCLUSIONS
  In this review, structural features and properties of several insect α-amylases were compared. This could be helpful in exploring the diversity in characteristics of α-amylase between the members of the same class (insecta). Properties like pH optima are reflected in enzyme structural features. In plants, α-amylase inhibitors (α-AIs) occur as part of natural defense mechanisms against pests by interfering in their digestion process and thus could also provide access to new pest management strategies. AIs are quite specific in their action; therefore, these could be employed according to their effectiveness against target amylases. Potential of transgenics with α-AIs has also been discussed for insect resistance and controlling infestation.
  
  
  CONCLUSIONS
  The differences in structural features of insect α-amylases provided reasons for their efficient functioning at different pH and the specificity towards various substrates. Various proteinaceous and non-proteinaceous inhibitors discussed could be helpful in controlling pest infestation. In depth detailed studies are required on proteinaceous α-AI-α-amylase interaction at different pH's as well as the insect proteinase action on these inhibitors before selecting the α-AI for making transgenics resistant to particular insect.
authors.affiliation: Department of Biochemistry, Punjab Agricultural University, Ludhiana 141004, India.
authors.forename: Rimaljeet
authors.initials: R
authors.lastname: Kaur
authors.affiliation: Department of Biochemistry, Punjab Agricultural University, Ludhiana 141004, India.
authors.forename: Narinder
authors.initials: N
authors.lastname: Kaur
authors.affiliation: Department of Biochemistry, Punjab Agricultural University, Ludhiana 141004, India. Electronic address: anilkgupta1954@gmail.com.
authors.forename: Anil Kumar
authors.initials: AK
authors.lastname: Gupta
mesh_terms: D000818:Animals; D004791:Enzyme Inhibitors / Q000494:pharmacology; D019476:Insect Proteins / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism; D007313:Insecta; D007527:Isoenzymes / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism; D030821:Plants, Genetically Modified; D013379:Substrate Specificity; D000516:alpha-Amylases / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism
chemical_list: D004791:Enzyme Inhibitors; D019476:Insect Proteins; D007527:Isoenzymes; D000516:alpha-Amylases
keywords: Amylase inhibitors; Insect; Kinetic properties; Substrate specificity; α-Amylase