Activity test of NagS homologs in vitro and in vivo.

Activity test of NagS homologs in vitro and in vivo.

<p><b>(a)</b> Comparison of amino acid sequences of <i>S. coelicolor</i> NagS and its homologs. These are homologs from <i>Streptacidiphilus jiangxiensis</i> (TrEMBL A0A1H7F721), <i>Clostridium amylolyticum</i> (TrEMBL A0A1M6IM34), <i>Paeni...

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Hlavní autor: Chao Li (145513) (author)
Další autoři: Mia Urem (22683580) (author), Ioli Kotsogianni (9930187) (author), Josephine Lau (20442343) (author), Chao Du (288036) (author), Somayah S. Elsayed (9192571) (author), Nathaniel I. Martin (847378) (author), Iain W. McNae (840777) (author), Patrick Voskamp (2311429) (author), Christoph Mayer (57204) (author), Sébastien Rigali (724082) (author), Navraj Pannu (10163763) (author), Jan Pieter Abrahams (1429531) (author), Lennart Schada von Borzyskowski (22683583) (author), Gilles P. van Wezel (7838948) (author)
Vydáno: 2025
Témata:
Biochemistry
Microbiology
Ecology
Developmental Biology
Inorganic Chemistry
Biological Sciences not elsewhere classified
controls nutrient signaling
also revealed 6
highlighted key residues
glcnac sensing requires
toxicity pathway dependent
6p deacetylase naga
novel glcnac 6
key role
substrate glcnac
novel enzyme
work uncovers
wall leads
unprecedented reaction
substrate mycelium
structural analogue
streptomycetaceae </
streptomyces </
revolves around
promiscuous activity
nature ’
n </
multicellular lifestyle
metabolic checkpoint
medicine makers
lytic dismantling
landmark event
hyphal cell
highly conserved
growth media
function analysis
clinical antibiotics
central metabolism
catalytic inhibitor
antibiotic production
active site
>- acetylglucosamine
6p dehydratase
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