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Molecular cloning and sequence analysis of cDNA encoding human kidney D‐amino acid oxidase
Author(s) -
Momoi Kyoko,
Fukui Kiyoshi,
Watanabe Fusao,
Miyake Yoshihiro
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80252-7
Subject(s) - complementary dna , microbiology and biotechnology , amino acid , cdna library , biochemistry , d amino acid oxidase , peptide sequence , biology , molecular cloning , methionine , northern blot , enzyme , oxidase test , gene
cDNA clones encoding D‐amino acid oxidase were isolated from a human kidney cDNA library by hybridization with cDNA for the pig enzyme. The cDNA insert of 2.0 kilobase pairs long provided coding information for a protein consisting of 347 amino acids. The molecular mass of the enzyme was calculated to be 39 410 Da. The amino acid sequence similarity between the pig and human enzymes is 84.4%, and among the active site residues proposed from chemical modification studies, methionine‐110 of the pig enzyme was replaced by threonine. Northern blot analysis confirmed the expression of an mRNA of 2.0 kilobases encoding the D‐amino acid oxidase in human kidney.