Structural highlights
Function
W9BQ28_KLEPN
Publication Abstract from PubMed
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.
Relationship between the induced-fit loop and the activity of Klebsiella pneumoniae pullulanase.,Saka N, Malle D, Iwamoto H, Takahashi N, Mizutani K, Mikami B Acta Crystallogr D Struct Biol. 2019 Sep 1;75(Pt 9):792-803. doi: , 10.1107/S2059798319010660. Epub 2019 Aug 22. PMID:31478902[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Saka N, Malle D, Iwamoto H, Takahashi N, Mizutani K, Mikami B. Relationship between the induced-fit loop and the activity of Klebsiella pneumoniae pullulanase. Acta Crystallogr D Struct Biol. 2019 Sep 1;75(Pt 9):792-803. PMID:31478902 doi:10.1107/S2059798319010660
