Sharma Archana, Kaushik Vineeta, Goel Manisha
Department of Biophysics, University of Delhi South Campus, Benito Juarez Road, New Delhi 110021, India.
ACS Omega. 2022 Nov 2;7(45):40750-40765. doi: 10.1021/acsomega.2c01127. eCollection 2022 Nov 15.
l-Asparaginase catalyzes the hydrolysis of l-asparagine to aspartic acid and ammonia and is used in the medical and food industries. In this investigation, from the proteomes of 176 archaeal organisms (with completely sequenced genomes), 116 homologs of l-asparaginase were obtained from 86 archaeal organisms segregated into Asp1, Asp2, IaaA, Asp2like1, and Asp2like2 families based on the conserved domain. The similarities and differences in the structure of selected representatives from each family are discussed. From the two novel archaeal l-asparaginase families Asp2like1 and Asp2like2, a representative of Asp2like1 family asparaginase (PtAsp2like1) was characterized in detail to find its suitability in therapeutics. PtAsp2like1 was a glutaminase-free asparaginase that showed the optimum activity at 80 °C and pH 10.0. The Km of PtAsp2like1 toward substrate l-asparagine was 11.69 mM. This study demonstrates the improved mapping of asparaginases in the archaeal domain, facilitating future focused research on archaeal asparaginases for therapeutic applications.
L-天冬酰胺酶催化L-天冬酰胺水解成天冬氨酸和氨，应用于医药和食品工业。在本研究中，从176种古生菌（基因组已完全测序）的蛋白质组中，基于保守结构域，从86种古生菌中获得了116个L-天冬酰胺酶同源物，这些同源物被分为Asp1、Asp2、IaaA、Asp2like1和Asp2like2家族。讨论了每个家族中选定代表结构的异同。从两个新的古生菌L-天冬酰胺酶家族Asp2like1和Asp2like2中，详细表征了Asp2like1家族天冬酰胺酶的一个代表（PtAsp2like1），以确定其在治疗方面的适用性。PtAsp2like1是一种无谷氨酰胺酶的天冬酰胺酶，在80℃和pH 10.0时表现出最佳活性。PtAsp2like1对底物L-天冬酰胺的Km为11.69 mM。本研究展示了古生菌域中天冬酰胺酶图谱的改进，有助于未来针对古生菌天冬酰胺酶在治疗应用方面的重点研究。
