| Title |
Comparative analysis of mesophilic YqfB-type amidohydrolases / |
| Authors |
Statkevičiūtė, Roberta ; Sadauskas, Mikas ; Rainytė, Juta ; Kavaliauskaitė, Karolina ; Meškys, Rolandas |
| DOI |
10.3390/biom12101492 |
| Full Text |
|
| Is Part of |
Biomolecules.. Basel : MDPI. 2022, vol. 12, no. 10, art. no. 1492, p. [1-12].. eISSN 2218-273X |
| Keywords [eng] |
ASCH ; N4-acetylcytidine ; amidohydrolase ; prodrug |
| Abstract [eng] |
The widespread superfamily of the human activating signal cointegrator homology (ASCH) domain was identified almost 20 years ago; however, the amount of experimental data regarding the biological function of the domain is scarce. With this study, we aimed to determine the putative cellular functions of four hypothetical ASCH domain-containing amidohydrolase YqfB analogues by investigating their activity towards various N-acylated cytosine derivatives, including potential nucleoside-derived prodrugs, as well as their ability to bind/degrade nucleic acids in vitro. According to determined kinetic parameters, N4-acetylcytidine is assumed to be the primary substrate for amidohydrolases. Despite the similarity to the proteins containing the PUA domain, no nucleic acid binding activity was detected for YqfB-like proteins, suggesting that, in vivo, these enzymes are a part of the pyrimidine salvage pathway. We also demonstrate the possibility of the expression of YqfB-type amidohydrolases in both prokaryotic and eukaryotic hosts. The small protein size and remarkable halotolerance of YqfB-type amidohydrolases are of great interest for further fundamental research and biotechnological applications. |
| Published |
Basel : MDPI |
| Type |
Journal article |
| Language |
English |
| Publication date |
2022 |
| CC license |
|
