Structural and mutational analyses of dipeptidyl peptidase 11 from Porphyromonas gingivalis reveal the molecular basis for strict substrate specificity. (Q30152912)

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English	Structural and mutational analyses of dipeptidyl peptidase 11 from Porphyromonas gingivalis reveal the molecular basis for strict substrate specificity.	scientific article

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scholarly article

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16 February 2020

Structural and mutational analyses of dipeptidyl peptidase 11 from Porphyromonas gingivalis reveal the molecular basis for strict substrate specificity (English)

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16 February 2020

Porphyromonas gingivalis

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Yasumitsu Sakamoto

1

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Yoshiyuki Suzuki

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Ippei Iizuka

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Chika Tateoka

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Saori Roppongi

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Mayu Fujimoto

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Koji Inaka

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Hiroaki Tanaka

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Mitsugu Yamada

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Kazunori Ohta

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Hiroaki Gouda

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Takamasa Nonaka

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Wataru Ogasawara

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Nobutada Tanaka

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9 June 2015

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16 February 2020

Scientific Reports

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16 February 2020

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11151

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16 February 2020

describes a project that uses

Japan Aerospace Exploration Agency Protein Crystallization Growth

object has role

International Space Station experiment

1 reference

https://www.nasa.gov/mission_pages/station/research/experiments/explorer/Investigation.html?#id=151

Crystallization and preliminary X-ray crystallographic studies of dipeptidyl peptidase 11 from Porphyromonas gingivalis.

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S46 Peptidases are the First Exopeptidases to be Members of Clan PA

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Crystallization and preliminary X-ray crystallographic studies of dipeptidyl aminopeptidase BII from Pseudoxanthomonas mexicana WO24.

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Identification of the catalytic triad of family S46 exopeptidases, closely related to clan PA endopeptidases

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Identification and characterization of prokaryotic dipeptidyl-peptidase 5 from Porphyromonas gingivalis

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JAXA protein crystallization in space: ongoing improvements for growing high-quality crystals

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Phenylalanine 664 of dipeptidyl peptidase (DPP) 7 and Phenylalanine 671 of DPP11 mediate preference for P2-position hydrophobic residues of a substrate

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Discrimination based on Gly and Arg/Ser at position 673 between dipeptidyl-peptidase (DPP) 7 and DPP11, widely distributed DPPs in pathogenic and environmental gram-negative bacteria

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Porphyromonas gingivalis: an invasive and evasive opportunistic oral pathogen

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Asp- and Glu-specific novel dipeptidyl peptidase 11 of Porphyromonas gingivalis ensures utilization of proteinaceous energy sources

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Structure of crystalline alpha-chymotrypsin. IV. The structure of indoleacryloyl-alpha-chyotrypsin and its relevance to the hydrolytic mechanism of the enzyme

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based on heuristic

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based on heuristic

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Diprotins A and B, inhibitors of dipeptidyl aminopeptidase IV, produced by bacteria

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10.1038/SREP11151

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16 February 2020

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16 February 2020

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16 February 2020

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10.1038/srep11151

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