Zn (II)-free dimethylargininase-1 (DDAH-1) is inhibited upon specific Cys-S-nitrosylation

M Knipp, O Braun, PM Gehrig, R Sack… - Journal of Biological …, 2003 - ASBMB
The endogenous nitric oxide synthase inhibitorsl-N ω-methylarginine andl-N ω, N ω-
dimethylarginine are catabolized by the enzyme dimethylargininase. Dimethylargininase-1
from bovine brain contains one tightly bound Zn (II) coordinated by two cysteine sulfur and
two lighter ligands. Activity measurements showed that only the apo-enzyme is active and
that the holo-enzyme is activated by zinc removal. In this work, the effect of NO on
dimethylargininase-1 structure and its activity was investigated using 2-(N, N …
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