M42 aminopeptidase catalytic site: the structural and functional role of a strictly conserved aspartate residue-Reference-Cited by-同舟云学术

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M42 aminopeptidase catalytic site: the structural and functional role of a strictly conserved aspartate residue

Published:2020-08-13 Issue:12 Volume:88 Page:1639-1647
ISSN:0887-3585
Container-title:Proteins: Structure, Function, and Bioinformatics
language:en
Short-container-title:Proteins

Author:

Dutoit Raphaël¹²^ORCID,Brandt Nathalie²,Van Gompel Tom³,Van Elder Dany¹,Van Dyck Jeroen³,Sobott Frank³⁴,Droogmans Louis¹

Affiliation:

1. Laboratory of Microbiology, Department of Molecular Biology Université Libre de Bruxelles Brussels Belgium

2. Labiris Institut de Recherche Brussels Belgium

3. Biomolecular & Analytical Mass Spectrometry, Department of Chemistry Universiteit van Antwerpen Antwerpen Belgium

4. Astbury Centre for Structural and Molecular Biology University of Leeds Leeds UK

Publisher

Wiley

Subject

Molecular Biology,Biochemistry,Structural Biology

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/prot.25982

Reference43 articles.

1. Crystal Structure of TET Protease Reveals Complementary Protein Degradation Pathways in Prokaryotes

2. TET peptidases: A family of tetrahedral complexes conserved in prokaryotes

3. Crystal Structure of a Dodecameric Tetrahedral-shaped Aminopeptidase

4. An Archaeal Peptidase Assembles into Two Different Quaternary Structures

5. The structural and biochemical characterizations of a novel TET peptidase complex from Pyrococcus horikoshii reveal an integrated peptide degradation system in hyperthermophilic Archaea

Cited by 3 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Substrate Characterization for Hydrolysis of Multiple Types of Aromatic Esters by Promiscuous Aminopeptidases;Journal of Agricultural and Food Chemistry;2024-07-18

2. Functional control of a 0.5 MDa TET aminopeptidase by a flexible loop revealed by MAS NMR;Nature Communications;2022-04-08

3. Functional control of a 0.5 MDa TET aminopeptidase by a flexible loop revealed by MAS NMR;2021-06-30

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