Functional and Structural Analysis of a Novel Acyltransferase from Pathogenic Phytophthora melonis.

ABSTRACT: This investigation characterizes an acyltransferase enzyme responsible for the pathogenicity of Phytophthora melonis. The protein was characterized in vitro for its physicochemical properties. The biochemical characterization, including thermal and pH stability, revealed the 35 °C temperature and 7.0 pH as the optimum conditions for the enzyme. Applying the Tween-80 solution enhanced the activity up to 124.9%. Comprehensive structural annotation revealed two domains, A (ranging from residues 260 to 620) and B (ranging from 141 to 219). Domain A had transglutaminase (T-Gase) elicitor properties, while B possessed antifreeze features. Rigorous sequence characterization of the acyltransferase tagged it as a low-temperature-resistant protein. Further, the tax

SUBMITTER: Ahmad A 

PROVIDER: S-EPMC7841795 | biostudies-literature | 2021 Jan

REPOSITORIES: biostudies-literature