Zn(II)-free Dimethylargininase-1 (DDAH-1) Is Inhibited upon Specific Cys-S-Nitrosylation

The endogenous nitric oxide synthase inhibitors l - N Ï -methylarginine and l - N Ï , N Ï -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. Activi...

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Veröffentlicht in:	The Journal of biological chemistry 2003-01, Vol.278 (5), p.3410-3416
Hauptverfasser:	Knipp, Markus, Braun, Oliver, Gehrig, Peter M, Sack, Ragna, Vasák, Milan
Format:	Artikel
Sprache:	eng
Schlagworte:	Amidohydrolases - antagonists & inhibitors Amidohydrolases - chemistry Amidohydrolases - genetics Amidohydrolases - ultrastructure Amino Acid Sequence Animals Binding Sites Brain - enzymology Cattle Cysteine - metabolism Hot Temperature Integrins - physiology Kinetics Ligands Mammals Models, Molecular Molecular Sequence Data Nitric Oxide - metabolism Nitric Oxide - pharmacology Nitrosation Peptide Fragments - chemistry Protein Structure, Secondary Pseudomonas aeruginosa - enzymology Recombinant Proteins - chemistry Recombinant Proteins - metabolism Recombinant Proteins - ultrastructure Sequence Alignment Sequence Homology, Amino Acid Thermodynamics Zinc - metabolism Zinc - pharmacology
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