2020
DOI: 10.1002/pro.3847
|View full text |Cite
|
Sign up to set email alerts
|

Single‐particle analysis of urea amidolyase reveals its molecular mechanism

Abstract: Urea amidolyase (UA), a bifunctional enzyme that is widely distributed in bacteria, fungi, algae, and plants, plays a pivotal role in the recycling of nitrogen in the biosphere. Its substrate urea is ultimately converted to ammonium, via successive catalysis at the C-terminal urea carboxylase (UC) domain and followed by the N-terminal allophanate hydrolyse (AH) domain. Although our previous studies have shown that Kluyveromyces lactis UA (KlUA) functions efficiently as a homodimer, the architecture of the full… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1

Citation Types

0
1
0

Year Published

2022
2022
2022
2022

Publication Types

Select...
1

Relationship

1
0

Authors

Journals

citations
Cited by 1 publication
(1 citation statement)
references
References 40 publications
0
1
0
Order By: Relevance
“…The structure of human, mouse, and rat CRP were examined with electron microscopy 32 , 39 , 61 , 62 . Briefly, samples were negatively stained with 1% uranyl acetate for 40 s and imaged with a FEI Talos F200C electron microscope at a magnification of ×120,000.…”
Section: Methodsmentioning
confidence: 99%
“…The structure of human, mouse, and rat CRP were examined with electron microscopy 32 , 39 , 61 , 62 . Briefly, samples were negatively stained with 1% uranyl acetate for 40 s and imaged with a FEI Talos F200C electron microscope at a magnification of ×120,000.…”
Section: Methodsmentioning
confidence: 99%