MalS, a periplasmic α-amylase in Escherichia coli, has a binding affinity to glycogen with unique substrate specificities.

ABSTRACT: In this study, we investigated MalS, a periplasmic α-enzyme from Escherichia coli K12, known for its unique biochemical properties related to polysaccharide utilization. Evolutionarily, MalS has inherited the glycosyl hydrolase catalytic domain from the glycoside hydrolase family 13, with the protein sequences highly conserved across Enterobacteria, including Salmonella and Shigella. MalS exhibited optimal activity at 65 °C, significantly higher than other E. coli enzymes. Although its reaction pattern resembled that of typical α-amylases, its catalytic efficiency on polysaccharides was notably lower. Intriguingly, MalS demonstrated a strong binding affinity for various glucose polymers, including β-cyclodextrin and glycogen, which significantly enhanced its thermostability. Despite full-l

SUBMITTER: Tran PL 

PROVIDER: S-EPMC11828803 | biostudies-literature | 2025 Feb

REPOSITORIES: biostudies-literature