Characterization of choline dehydrogenase from Pseudomonas aeruginosa A-16.
Characterization of choline dehydrogenase from Pseudomonas aeruginosa A-16.
复制标题
铜绿假单胞菌 A-16 胆碱脱氢酶的表征。
DOI：
10.1271/bbb1961.40.2077
复制
发表时间：
1976
期刊：
影响因子：
--
通讯作者：
K. Ogata
中科院分区：
文献类型：
--
作者：
T. Nagasawa;N. Mori;Y. Tani;K. Ogata
甲胆碱脱氢酶，这是存在于颗粒部分的铜绿假单胞菌A-16的无细胞提取物，氧化胆碱甜菜碱醛没有任何可分离的辅酶，而酶，这是用Triton X-100处理，氧化胆碱只有补充吩嗪硫酸甲酯。差谱图显示微粒中存在细胞色素样成分。胆碱和吩嗪硫酸甲酯的Km值分别为1.7 × 10−3 m和1.4 × 10−4 m。对氯汞苯甲酸盐和碘乙酸等SH试剂对脱氢酶有抑制作用。各种底物测试，只有胆碱引起的酶还原吩嗪硫酸甲酯。用该酶测定了胆碱的含量。
A choline dehydrogenase, which was present in the particulate fraction of the cell-free extract of Pseudomonas aeruginosa A-16, oxidized choline to betaine aldehyde without any dissociable coenzymes, while the enzyme, which was treated with Triton X-100, oxidized choline only with a supplement of phenazine methosulfate. The difference spectrum showed the presence of cytochrome-like components in the particulate. Km values for choline and phenazine methosulfate were 1.7 × 10−3 m and 1.4 × 10−4 m, respectively. The dehydrogenase was inhibited by SH-reagents such as p-chloromercuribenzoate and iodoacetic acid. Of a variety of substrates tested, only choline caused the enzymatic reduction of phenazine methosulfate. The estimation of choline was tried using the enzyme.