About: Crystal structures of a bacterial dipeptidyl peptidase IV reveal a novel substrate recognition mechanism distinct from that of mammalian orthologues

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About: Crystal structures of a bacterial dipeptidyl peptidase IV reveal a novel substrate recognition mechanism distinct from that of mammalian orthologues Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Crystal structures of a bacterial dipeptidyl peptidase IV reveal a novel substrate recognition mechanism distinct from that of mammalian orthologues
Creator	Nakamura, Akihiro Suzuki, Yoshiyuki Fujimoto, Mayu Honma, Nobuyuki Iizuka, Ippei Morisawa, Saori Nonaka, Takamasa Ogasawara, Wataru Roppongi, Saori Sakamoto, Yasumitsu Shida, Yosuke Tanaka, Nobutada Tateoka, Chika
Source	Medline; PMC
abstract	Dipeptidyl peptidase IV (DPP IV, DPP4, or DAP IV) preferentially cleaves substrate peptides with Pro or Ala at the P1 position. The substrate recognition mechanism has been fully elucidated for mammalian DPP IV by crystal structure analyses but not for bacterial orthologues. Here, we report the crystal structures of a bacterial DPP IV (PmDAP IV) in its free form and in complexes with two kinds of dipeptides as well as with a non-peptidyl inhibitor at 1.90 to 2.47 Å resolution. Acyl-enzyme intermediates were observed for the dipeptide complexes of PmDAP IV, whereas tetrahedral intermediates were reported for the oligopeptide complexes of mammalian DPP IVs. This variation reflects the different structural environments of the active site Arg residues, which are involved in the recognition of a substrate carbonyl group, of mammalian and bacterial enzymes. A phylogenetic analysis revealed that PmDAP IV is a closer relative of dipeptidyl peptidases 8 and 9 (DPP8 and DPP9, DPP IV-family enzymes) than DPP IV. These results provide new insights into the substrate recognition mechanism of bacterial DAP IVs and may assist in the development of selective inhibitors for DAP IVs from pathogenic asaccharolytic bacteria, which utilise proteins or peptides as an energy source.
has issue date	2018-02-09(xsd:dateTime)
bibo:doi	10.1038/s41598-018-21056-y
bibo:pmid	29426867
has license	cc-by
sha1sum (hex)	2106f8105f3cb30bf479fdcb6d78e4891a204080
schema:url	https://doi.org/10.1038/s41598-018-21056-y
resource representing a document's title	Crystal structures of a bacterial dipeptidyl peptidase IV reveal a novel substrate recognition mechanism distinct from that of mammalian orthologues
has PubMed Central identifier	PMC5807507
has PubMed identifier	29426867
schema:publication	Sci Rep
resource representing a document's body	covid:2106f8105f3cb30bf479fdcb6d78e4891a204080#body_text
is schema:about of	named entity 'MECHANISM' named entity 'closer' named entity 'involved' named entity 'substrate' named entity 'reveal' named entity 'mechanism' named entity 'SUBSTRATE RECOGNITION' named entity 'ACTIVE SITE' named entity 'ENZYME' named entity 'DIFFERENT' named entity 'DPP9' named entity 'REFLECTS' named entity 'NEW' named entity 'ENERGY SOURCE' named entity 'DEVELOPMENT' named entity 'HERE' named entity 'FULLY' named entity 'IVS' named entity 'TETRAHEDRAL' named entity 'THESE' named entity 'PHYLOGENETIC ANALYSIS' named entity 'ALA' named entity 'BUT' named entity 'RELATIVE' named entity 'COMPLEXES' named entity 'STRUCTURAL' named entity 'POSITION' named entity 'DPP IV' named entity 'STRUCTURES' named entity 'SUBSTRATE' named entity 'REPORT' named entity 'INHIBITOR' named entity 'DIPEPTIDES' named entity 'SELECTIVE' named entity 'INTERMEDIATES' named entity 'NON-' named entity 'MECHANISM' named entity 'BACTERIA' named entity 'REVEALED' named entity 'RECOGNITION' named entity 'DPP' named entity 'RESOLUTION' named entity 'ASSIST' named entity 'PEPTIDES' named entity 'RESULTS' named entity 'CRYSTAL STRUCTURE' named entity 'DAP' named entity 'OLIGOPEPTIDE' named entity 'FORM' named entity 'REPORTED' named entity 'FAMILY' named entity 'MAMMALIAN' named entity 'PROVIDE' named entity 'PROTEINS' named entity 'PEPTIDYL' named entity 'CRYSTAL' named entity 'BACTERIAL' named entity 'MAMMALIAN' named entity 'DIPEPTIDYL PEPTIDASE IV' named entity 'NOVEL' named entity 'REVEAL' named entity 'OBSERVED' named entity 'INVOLVED' named entity 'CRYSTAL' named entity 'PRO' named entity 'INSIGHTS' named entity 'DIPEPTIDE' named entity 'VARIATION' named entity 'BACTERIAL'

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