Essential Histidyl Residues in Arginine Oxygenase (Decarboxylating). Comparison with Amino Acid Oxidases
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1971.tb01314.x/fullpdf
Reference31 articles.
1. Arginine décarboxy-oxydase
2. L-Arginine oxygenase decarboxylante IV. Incorporation de 18O dans la γ-guanidinobutyramide
3. Arginine oxygenase decarboxylante
4. Location of hydrogen transfer steps in the mechanism of reduction of L-amino acid oxidase
5. Mechanism of conversion of the purple intermediate into the fully reduced form of D-amino-acid oxidase
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1. Distribution of the Arginine Oxygenase Pathway among Coryneform Bacteria;Agricultural and Biological Chemistry;1989-04
2. Essential Histidyl Residues in Glucose Oxidase. Chemical Modification of Histidyl Residues with Diethylpyrocarbonate†;Agricultural and Biological Chemistry;1984-12
3. 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase from rat liver.;Journal of Biological Chemistry;1983-05
4. Effect of Chemical Modification of a Histidine and a Lysine Residue of Pea Seed Nucleoside Diphosphate Kinase;Upsala Journal of Medical Sciences;1982-01
5. Reactivity of d-Amino Acid Oxidase with 1,2-Cyclohexanedione: Evidence for One Arginine in the Substrate-Binding Site;European Journal of Biochemistry;1981-10
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