Effect of site-specific mutagenesis of tyrosine-55, methionine-110 and histidine-217 in porcine kidney D-amino acid oxidase on its catalytic function
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(88)80494-0/fullpdf
Reference18 articles.
1. The primary structure of D-amino acid oxidase from pig kidney. II. Isolation and sequence of overlap peptides and the complete sequence.
2. Chemical modification of D-amino acid oxidase. Amino acid sequence of the tryptic peptides containing tyrosine and lysine residues modified by fluorodinitrobenzene.
3. Methylation of the active center histidine 217 in D-amino acid oxidase by methyl-p-nitrobenzenesulfonate.
4. Identification of methionine-110 as the residue covalently modified in the electrophilic inactivation of D-amino-acid oxidase by O-(2,4-dinitrophenyl)hydroxylamine
5. Molecular cloning and sequence analysis of cDNAs encoding porcine kidney D-amino acid oxidase
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1. Modulating D-amino acid oxidase (DAAO) substrate specificity through facilitated solvent access;PLOS ONE;2018-06-15
2. A single Phe54Tyr substitution improves the catalytic activity and thermostability of Trigonopsis variabilis d-amino acid oxidase;New Biotechnology;2010-02
3. Potential pathophysiological role of d-amino acid oxidase in schizophrenia: immunohistochemical and in situ hybridization study of the expression in human and rat brain;Journal of Neural Transmission;2009-08-15
4. Potential Role for Astroglial d-Amino Acid Oxidase in Extracellular d-Serine Metabolism and Cytotoxicity;The Journal of Biochemistry;2006-02-01
5. Substitution of the critical methionine residues in Trigonopsis variabilis ?-amino acid oxidase with leucine enhances its resistance to hydrogen peroxide;FEMS Microbiology Letters;2000-05-05
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