Relationship between the induced-fit loop and the activity of Klebsiella pneumoniae pullulanase

Klebsiella pneumoniae pullulanase (KPP) belongs to glycoside hydrolase family 13 subfamily 13 (GH13_13) and is the only enzyme that is reported to perform an induced-fit motion of the active-site loop (residues 706 – 710). Comparison of pullulanase structures indicated that only KPP has Leu680 present behind the loop, in contrast to the glycine found in other GH13_13 members. Analysis of the structure and activity of recombinant pullulanase from K. pneumoniae ATCC 9621 (rKPP) and its mutant (rKPP-G680L) indicated that the side chain of residue 680 is important for the induced-fit motion of the loop 706 – 710 and alters the binding affinity of the substrate.

Source: Acta Crystallographica Section D - August 21, 2019 Category: Biochemistry Authors: Saka, N. Malle, D. Iwamoto, H. Takahashi, N. Mizutani, K. Mikami, B. Tags: crystal structure pullulanase Klebsiella pneumoniae induced fit mutagenesis research papers Source Type: research