Purification and Properties of the Constitutive Arginase of Evernia prunastri.

Abstract:

:Constitutive arginase (molecular weight 330,000) 920-fold purified from Evernia prunastri thallus, is activated by putrescine, l-ornithine, and agmatine with K(a) values of 2.7, 1.1, and 5.8 millimolar, respectively. Constitutive arginase is also activated by endogenous l-arginine, reaching its maximum activity at 16 hours of incubation on Tris-HCl (pH 9.15) with a subsequent decrease. Urea behaves as a mixed inhibitor of the enzyme with a K(i) value of 2.6 millimolar. Atranorin and evernic acid behave as in vitro activators of the enzyme; usnic acid does not have any significant effect as activator.

journal_name

Plant Physiol

journal_title

Plant physiology

authors

Martín-Falquina A,Legaz ME

doi

10.1104/pp.76.4.1065

subject

Has Abstract

pub_date

1984-12-01 00:00:00

pages

1065-9

issue

4

eissn

0032-0889

issn

1532-2548

journal_volume

76

pub_type

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