Takahashi E, Ito K, Yoshimoto T
Basic Technology Department, Tanabe Seiyaku Co. Ltd., Saitama, Japan.
Biosci Biotechnol Biochem. 1999 Dec;63(12):2244-7. doi: 10.1271/bbb.63.2244.
The L-amino acid degrading enzyme gene from Proteus vulgaris was cloned and the nucleotide sequence of the enzyme gene was clarified. An open reading frame of 1,413 bp starting at an ATG methionine codon was found, which encodes a protein of 471 amino acid residues, the calculated molecular weight of which is 51,518. The amino acid sequence of P. vulgaris was 58.6% identical with the L-amino acid deaminase of P. mirabilis. A significantly conserved sequence was found around the FAD-binding sequence of flavo-proteins. The partially purified wild and recombinant enzymes had the same substrate specificity for L-amino acids to form the respective keto-acids, however not for D-amino acids.
克隆了普通变形杆菌的L-氨基酸降解酶基因，并阐明了该酶基因的核苷酸序列。发现了一个从ATG甲硫氨酸密码子开始的1413 bp的开放阅读框，它编码一个由471个氨基酸残基组成的蛋白质，其计算分子量为51,518。普通变形杆菌的氨基酸序列与奇异变形杆菌的L-氨基酸脱氨酶有58.6%的同一性。在黄素蛋白的FAD结合序列周围发现了一个显著保守的序列。部分纯化的野生型和重组酶对L-氨基酸形成各自的酮酸具有相同的底物特异性，但对D-氨基酸则没有。
