Purification and characterization of a novel glycine oxidase from Bacillus subtilis
Purification and characterization of a novel glycine oxidase from Bacillus subtilis
复制标题
DOI：
10.1016/s0014-5793(98)01313-1
复制
发表时间：
1998-11-06
期刊：
影响因子：
3.5
通讯作者：
Imanaka, T
中科院分区：
文献类型：
--
作者：
Nishiya, Y;Imanaka, T
开放阅读框yjbR已作为枯草芽孢杆菌基因组计划的一部分测序，其编码推定的40.9-kDa蛋白。yjbR编码序列与细菌肌氨酸氧化酶的序列略有相似，可能与猪肾D-氨基酸氧化酶的三级结构相容。yjbR基因产物在大肠杆菌中过量生产，从重组菌株中纯化至均一，并进行表征。该蛋白能有效地催化肌氨酸（N-甲基甘氨酸）、N-乙基甘氨酸和甘氨酸的氧化，对D-丙氨酸、D-缬氨酸和D-脯氨酸的氧化活性较低，但对L-氨基酸和其他D-氨基酸没有活性。由于甘氨酸是肌氨酸氧化酶的产物而不是底物，因此这种蛋白质不是一种脱甲基酶，而是一种新的脱氨基氧化酶，通常称为甘氨酸氧化酶。B的几种酶性质。枯草杆菌甘氨酸氧化酶的活性。(C)1998年欧洲生物化学学会联合会。
The open reading frame yjbR which had been sequenced as a part of the Bacillus subtilis genome project encodes a putative 40.9-kDa protein. The yjbR-coding sequence was slightly similar to those of bacterial sarcosine oxidases and possibly compatible with the tertiary structure of the porcine kidney D-amino acid oxidase. The yjbR gene product was overproduced in Escherichia coli, purified to homogeneity from the recombinant strain, and characterized. This protein effectively catalyzed the oxidation of sarcosine (N-methylglycine), N-ethylglycine and glycine, Lower activities on D-alanine, D-valine, and D-proline were detected although no activities were shown on L-amino acids and other D-amino acids. Since glycine is a product and not a substrate for sarcosine oxidase, this protein is not a type of demethylating enzymes but a novel deaminating oxidase, named glycine oxidase as a common name. Several enzymatic properties of the B. subtilis glycine oxidase were also investigated. (C) 1998 Federation of European Biochemical Societies.