Identification and Characterization of a Pepsin- and Chymotrypsin-Resistant Peptide in the α Subunit of the 11S Globulin Legumin from Common Bean ( L.).

The 11S globulin legumin typically accounts for approximately 3% of the total protein in common beans (). It was previously reported that a legumin peptide of approximately 20 kDa is resistant to pepsin digestion. Sequence prediction suggested that the pepsin-resistant peptide is located at the C-terminal end of the α-subunit, within a glutamic acid-rich domain, overlapping with a chymotrypsin-resistant peptide.

Global analysis of common bean multidrug and toxic compound extrusion transporters (PvMATEs): PvMATE8 and pinto bean seed coat darkening.

In common bean ( L.), postharvest seed coat darkening is an undesirable trait that affects crop value. The increased accumulation of proanthocyanidins (PAs) in the seed coat results in darker seeds in many market classes of colored beans after harvest.

Diurnal accumulation of K-dependent L-asparaginase in leaf of common bean (Phaseolus vulgaris L.).

L-Asparaginase (EC 3.5.1.

Evidence that class I glutamine amidotransferase, GAT1_2.1, acts as a glutaminase in roots of Arabidopsis thaliana.

The glutamine amidotransferase gene GAT1_2.1 is a marker of N status in Arabidopsis root, linked to a shoot branching phenotype. The protein has an N-terminal glutamine amidotransferase domain and a C-terminal extension with no recognizable protein domain.

Common Bean ( L.) Accumulates Most -Methylcysteine as Its γ-Glutamyl Dipeptide.

The common bean () constitutes an excellent source of vegetable dietary protein. However, there are sub-optimal levels of the essential amino acids, methionine and cysteine. On the other hand, accumulates large amounts of the γ-glutamyl dipeptide of -methylcysteine, and lower levels of free -methylcysteine and -methylhomoglutathione.