Batool Tahira, Makky Essam A, Jalal Muna, Yusoff Mashitah M
Faculty of Industrial Sciences & Technology, University Malaysia Pahang, 26300 Gambang, Kuantan, Pahang, Malaysia.
Department of Pathological analysis, Al-Haweeja Technical Institute, Foundation of Technical Education, Kirkuk, Iraq.
Appl Biochem Biotechnol. 2016 Mar;178(5):900-23. doi: 10.1007/s12010-015-1917-3. Epub 2015 Nov 7.
L-asparaginase (LA) catalyzes the degradation of asparagine, an essential amino acid for leukemic cells, into ammonia and aspartate. Owing to its ability to inhibit protein biosynthesis in lymphoblasts, LA is used to treat acute lymphoblastic leukemia (ALL). Different isozymes of this enzyme have been isolated from a wide range of organisms, including plants and terrestrial and marine microorganisms. Pieces of information about the three-dimensional structure of L-asparaginase from Escherichia coli and Erwinia sp. have identified residues that are essential for catalytic activity. This review catalogues the major sources of L-asparaginase, the methods of its production through the solid state (SSF) and submerged (SmF) fermentation, purification, and characterization as well as its biological roles. In the same breath, this article explores both the past and present applications of this important enzyme and discusses its future prospects.
L-天冬酰胺酶(LA)催化将白血病细胞必需的氨基酸天冬酰胺降解为氨和天冬氨酸。由于其抑制淋巴母细胞中蛋白质生物合成的能力,LA被用于治疗急性淋巴细胞白血病(ALL)。这种酶的不同同工酶已从多种生物体中分离出来,包括植物以及陆地和海洋微生物。有关来自大肠杆菌和欧文氏菌属的L-天冬酰胺酶三维结构的信息已确定了对催化活性至关重要的残基。本综述编目了L-天冬酰胺酶的主要来源、通过固态发酵(SSF)和深层发酵(SmF)生产该酶的方法、纯化、表征及其生物学作用。同时,本文探讨了这种重要酶的过去和现在的应用,并讨论了其未来前景。