Biochemical and functional characterization of an atypical plant l-arginase from Cilantro (Coriandrum sativam L.)

Siddappa, Shiva and Venkatesha, B. and Rai, V. Ravishankar and Marathe, G. K. (2018) Biochemical and functional characterization of an atypical plant l-arginase from Cilantro (Coriandrum sativam L.). International Journal of Biological Macromolecules, 118 (P A). 844 - 856. ISSN 1879-0003

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Arginase is one of the key enzymes responsible for maintaining the essential levels of nitrogen among plants, but biochemical and functional characterization of arginase among plants is limited. While screening for stable plant arginase, we found cilantro possessing an abundant and stable arginase. We purified arginase to apparent homogeneity (3300-fold purification) with a specific activity of 81,728 nmoles of urea formed/mg of protein/min and its eight-tryptic fragments had amino acid sequences identical to Arabidopsis thaliana arginase. Cilantro arginase exhibited absolute requirement for Mn2+ (0.5 mM–1 mM). Unlike other known plant arginases, cilantro arginase did not hydrolyse d-arginine and other arginine analogues. While for sulfhydryl reagents the enzyme was sensitive, l-NOHA, an arginase inhibitor showed only moderate inhibition - a property distinct from tomato arginase. We also found arginine derived amino acids and polyamines can regulate cilantro arginase in vitro. In addition, we also noticed an increase in cilantro arginase activity to both biotic and abiotic stress. We conclude that, cilantro may be used as a model plant to study plant arginases and to delineate arginase role, beyond its classical role in nitrogen recycling and polyamine biosynthesis.

Item Type: Article
Uncontrolled Keywords: Cilantro arginase, Polyamines, Biotic and abiotic stress, Nitrogen recycling
Subjects: C Chemical Science > Biochemistry
Divisions: Department of > Biochemistry
Depositing User: Manjula P Library Assistant
Date Deposited: 05 Jul 2019 11:13
Last Modified: 30 Jun 2020 10:40

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