Apis mellifera RidA, a novel member of the canonical YigF/YER057c/UK114 imine deiminase superfamily of enzymes pre-empting metabolic damage-Reference-Cited by-同舟云学术

Apis mellifera RidA, a novel member of the canonical YigF/YER057c/UK114 imine deiminase superfamily of enzymes pre-empting metabolic damage

Published:2022-08 Issue: Volume:616 Page:70-75
ISSN:0006-291X
Container-title:Biochemical and Biophysical Research Communications
language:en
Short-container-title:Biochemical and Biophysical Research Communications

Author:

Visentin Cristina,Rizzi Giulia^ORCID,Degani Genny^ORCID,Digiovanni Stefania^ORCID,Robecchi Giovanni^ORCID,Barbiroli Alberto^ORCID,Popolo Laura^ORCID,Vanoni Maria Antonietta^ORCID,Ricagno Stefano

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry,Biophysics

Reference29 articles.

1. Genomic and experimental evidence for multiple metabolic functions in the RidA/YjgF/YER057c/UK114 (Rid) protein family;Niehaus;BMC Genom.,2015

2. Members of the Rid protein family have broad imine deaminase activity and can accelerate the Pseudomonas aeruginosa D-arginine dehydrogenase (DauA) reaction in vitro;Hodge-Hanson;PLoS One,2017

3. RidA proteins protect against metabolic damage by reactive intermediates;Irons;Microbiol. Mol. Biol. Rev. MMBR.,2020

4. RidA proteins prevent metabolic damage inflicted by PLP-dependent dehydratases in all domains of life;Lambrecht;mBio,2013

5. From microbiology to cancer biology: the Rid protein family prevents cellular damage caused by endogenously generated reactive nitrogen species;Downs;Mol. Microbiol.,2015

Cited by 1 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. Site‐directed mutagenesis reveals the interplay between stability, structure, and enzymatic activity in RidA from Capra hircus;Protein Science;2024-05-27