A cupin domain is involved in α-amylase inhibitory activity.

Proteinaceous α-amylase inhibitors have specialized activities that make some strong inhibition of α-amylases. New α-amylase inhibitors continue to be discovered so far. A proteinaceous α-amylase inhibitor CL-AI was isolated and identified from chickpea seeds.

Isolation, Identification and Characterization of a New Type of Lectin with α-Amylase Inhibitory Activity in Chickpea (Cicer arietinum L.).

Background: Plant lectins are a group of highly diverse proteins that possess at least one non-catalytic domain that binds reversibly to a specific mono- or oligosaccharide. So far, only seven members in the lectin-arcelin-αAI1 supergene family in legume lectins have been reported to have inhibitory activity of α-amylases.

Objective & Methods: A proteinaceous α-amylase inhibitor was isolated and purified using Ammonium sulfate precipitation (ASP), Ion exchange chromatography (IEC) and Reversed phase liquid chromatography (RPLC) from the mature seeds of chickpea.

CarNAC4, a NAC-type chickpea transcription factor conferring enhanced drought and salt stress tolerances in Arabidopsis.

CarNAC4 is a typical stress-responsive NAC transcription factor and enhances drought and salt stress tolerances in transgenic Arabidopsis. Chickpea (Cicer arietinum L.) is relatively vulnerable to abiotic stress conditions, but the tolerance mechanisms for such stresses in chickpea are largely unknown.