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Relationship between the induced‐fit loop and the activity of Klebsiella pneumoniae pullulanase
Author(s) -
Saka Naoki,
Malle Dominggus,
Iwamoto Hiroyuki,
Takahashi Nobuyuki,
Mizutani Kimihiko,
Mikami Bunzo
Publication year - 2019
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.374
H-Index - 138
ISSN - 2059-7983
DOI - 10.1107/s2059798319010660
Subject(s) - pullulanase , klebsiella pneumoniae , glycoside hydrolase , mutant , hydrolase , recombinant dna , microbiology and biotechnology , chemistry , biochemistry , stereochemistry , biology , enzyme , escherichia coli , gene
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.