Redefining pseudokinases: A look at the untapped enzymatic potential of pseudokinases.
IUBMB Life
; 75(4): 370-376, 2023 04.
Article
in English
| MEDLINE | ID: covidwho-2173018
ABSTRACT
Catalytically inactive kinases, known as pseudokinases, are conserved in all three domains of life. Due to the lack of catalytic residues, pseudokinases are considered to act as allosteric regulators and scaffolding proteins with no enzymatic function. However, since these "dead" kinases are conserved along with their active counterparts, a role for pseudokinases may have been overlooked. In this review, we will discuss the recently characterized pseudokinases Selenoprotein O, Legionella effector SidJ, and the SARS-CoV2 protein nsp12 which catalyze AMPylation, glutamylation, and RNAylation, respectively. These studies provide structural and mechanistic insight into the versatility and diversity of the kinase fold.
Keywords
Full text:
Available
Collection:
International databases
Database:
MEDLINE
Main subject:
RNA, Viral
/
COVID-19
Limits:
Humans
Language:
English
Journal:
IUBMB Life
Journal subject:
Molecular Biology
/
Biochemistry
Year:
2023
Document Type:
Article
Affiliation country:
Iub.2698
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