Identification of methionine-110 as the residue covalently modified in the electrophilic inactivation of D-amino-acid oxidase by O-(2,4-dinitrophenyl)hydroxylamine-Reference-Cited by-同舟云学术

Identification of methionine-110 as the residue covalently modified in the electrophilic inactivation of D-amino-acid oxidase by O-(2,4-dinitrophenyl)hydroxylamine

Published:1987-03 Issue:6 Volume:26 Page:1717-1722
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

D'Silva Claudius,Williams Charles H.,Massey Vincent

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi00380a034

Reference29 articles.

1. Reactions of Horseradish Peroxidase with Azide. Evidence for a Methionine Residue at the Active Site*

2. Studies of the Biological and Immunological Properties of Parathyroid Hormone, Labeled Selectively on the Methionine Residues by [3H]Methyl Exchange to High Specific Activity*

3. Effect of Modification of a Methionyl Residue on the Kinetic and Molecular Properties of Isocitrate Dehydrogenase

4. Improved purification, amino acid analysis and molecular weight of homogeneous d-amino acid oxidase from pig kidney

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