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 Physioljournal_title
Plant physiologyauthors
Martín-Falquina A,Legaz MEdoi
10.1104/pp.76.4.1065subject
Has Abstractpub_date
1984-12-01 00:00:00pages
1065-9issue
4eissn
0032-0889issn
1532-2548journal_volume
76pub_type
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