| Type: | Family | Name: | Molecular chaperone Hsp31 and glyoxalase 3 |
| Description: | This group represents a chaperone Hsp31. E coli. Hsp31 functions as a holding molecular chaperone (holdase) which stabilises unfolding intermediates and rapidly releases them in an active form once stress has abated. It plays an important role in protecting cells from severe heat shock and starvation, as well as in acid resistance of stationary-phase cells. It uses temperature-induced exposure of structured hydrophobic domains to capture and stabilises early unfolding and denatured protein intermediates under severe thermal stress. It catalyzes the conversion of methylglyoxal (MG) to D-lactate in a single glutathione (GSH)-independent step. It can also use phenylglyoxal as substrate. Its glyoxalase activity protects cells against dicarbonyl stress. It displays an aminopeptidase activity that is specific against peptide substrates with alanine or basic amino acids (lysine, arginine) at N terminus [, , , , , , , ]. | Short Name: | HchA |
