食氨基假单胞菌仲胺单加氧酶催化反应的稳态动力学研究。
A steady-state kinetic study of the reaction catalysed by the secondary-amine mono-oxygenase of Pseudomonas aminovorans.
作者信息
Brook D F, Large P J
出版信息
Biochem J. 1976 Jul 1;157(1):197-205. doi: 10.1042/bj1570197.
Abstract
- Secondary-amine mono-oxygenase (proposed EC group 1.14.99.-) was partially purified from trimethylamine-grown Pseudomonas aminovorans by (NH4)2SO4 fractionation, gel filtration, hydrophobic chromatography on 5-aminopentylamino-Sepharose, and affinity chromatography on Sepharose-bound NADH. 2. Some problems in the affinity-chromatography step are discussed. 3. A steady-state kinetic analysis varying substrate, oxygen and electron-donor concentrations was performed, which, over the concentration range studied, gave a series of families of approximately parallel double-reciprocal plots. From secondary and tertiary plots, Michaelis constants of 0.160 mM, 0.086 mM and 0.121 mM were obtained for dimethylamine, NADPH and oxygen respectively. 4. Product-inhibition studies supported the postulated Hexa Uni Ping Pong (triple-transfer) reaction mechanism.
摘要
- 利用硫酸铵分级分离、凝胶过滤、在5-氨基戊基氨基琼脂糖上进行疏水色谱以及在琼脂糖结合的NADH上进行亲和色谱，从以三甲胺为生长底物的食氨基假单胞菌中部分纯化了仲胺单加氧酶（暂定EC分类1.14.99.-）。2. 讨论了亲和色谱步骤中的一些问题。3. 进行了一项稳态动力学分析，改变底物、氧气和电子供体的浓度，在所研究的浓度范围内，得到了一系列近似平行的双倒数图族。从二级和三级图中，分别得到二甲胺、NADPH和氧气的米氏常数为0.160 mM、0.086 mM和0.121 mM。4. 产物抑制研究支持了假定的六底物单产物乒乓（三转移）反应机制。
相似文献
1
A steady-state kinetic study of the reaction catalysed by the secondary-amine mono-oxygenase of Pseudomonas aminovorans.食氨基假单胞菌仲胺单加氧酶催化反应的稳态动力学研究。
Biochem J. 1976 Jul 1;157(1):197-205. doi: 10.1042/bj1570197.
2
Microbial oxidation of amines. Partial purification of a trimethylamine mono-oxygenase from Pseudomonas aminovorans and its role in growth on trimethylamine.胺的微生物氧化。从食胺假单胞菌中部分纯化三甲胺单加氧酶及其在三甲胺生长中的作用。
Biochem J. 1974 May;140(2):253-63. doi: 10.1042/bj1400253.
3
Inhibition by carbon monoxide of the secondary-amine mono-oxygenase of Pseudomonas aminovorans and the photochemical action spectrum for its reversal.一氧化碳对食氨假单胞菌仲胺单加氧酶的抑制作用及其逆转的光化学作用光谱。
Eur J Biochem. 1975 Jul 15;55(3):601-9. doi: 10.1111/j.1432-1033.1975.tb02197.x.
4
Oxidation of N-alkyl- and NN-dialkylhydroxylamines by partially purified preparations of trimethylamine mono-oxygenase from Pseudomonas aminovorans.氨基营养型假单胞菌中三甲胺单加氧酶部分纯化制剂对N-烷基羟胺和N,N-二烷基羟胺的氧化作用。
FEBS Lett. 1975 Jul 15;55(1):286-90. doi: 10.1016/0014-5793(75)81013-1.
5
Solubilization, partial purification and properties of N-methylglutamate dehydrogenase from Pseudomonas aminovorans.食氨基假单胞菌N-甲基谷氨酸脱氢酶的增溶、部分纯化及性质
Biochem J. 1977 Feb 1;161(2):357-70. doi: 10.1042/bj1610357.
6
Subcellular localization and properties of partially purified dimethylamine and trimethylamine mono-oxygenase activities in Candida utilis.产朊假丝酵母中部分纯化的二甲胺和三甲胺单加氧酶活性的亚细胞定位及性质
J Gen Microbiol. 1984 Oct;130(10):2577-88. doi: 10.1099/00221287-130-10-2577.
7
Primary amines as uncouplers of electron transport from hydroxylation in the secondary-amine mono-oxygenase system of Pseudomonas aminovorans.伯胺作为食氨基假单胞菌仲胺单加氧酶系统中羟基化作用电子传递的解偶联剂。
Biochem Biophys Res Commun. 1972 Nov 1;49(3):740-7. doi: 10.1016/0006-291x(72)90473-1.
8
Microbial oxidation of amines. Partial purification of a mixed-function secondary-amine oxidase system from Pseudomonas aminovorans that contains an enzymically active cytochrome-P-420-type haemoprotein.胺的微生物氧化。从食氨基假单胞菌中部分纯化一种混合功能仲胺氧化酶系统，该系统含有一种具有酶活性的细胞色素-P-420型血红蛋白。
Biochem J. 1971 Nov;125(2):449-59. doi: 10.1042/bj1250449.
9
Spectroscopic characterization of secondary amine mono-oxygenase. Comparison to cytochrome P-450 and myoglobin.仲胺单加氧酶的光谱表征。与细胞色素P-450和肌红蛋白的比较。
J Biol Chem. 1989 Dec 5;264(34):20467-73.
10
Purification and kinetic properties of glutathione reductase from bovine liver.牛肝谷胱甘肽还原酶的纯化及动力学性质
Mol Cell Biochem. 2007 Sep;303(1-2):45-51. doi: 10.1007/s11010-007-9454-1. Epub 2007 Apr 5.
引用本文的文献
1
Microbial oxidation of amines. Distribution, purification and properties of two primary-amine oxidases from the yeast Candida boidinii grown on amines as sole nitrogen source.胺的微生物氧化。以胺作为唯一氮源生长的博伊丁假丝酵母中两种伯胺氧化酶的分布、纯化及性质
Biochem J. 1981 Oct 1;199(1):187-201. doi: 10.1042/bj1990187.
2
The dye-linked alcohol dehydrogenase of Rhodopseudomonas acidophila. Comparison with dye-linked methanol dehydrogenases.嗜酸红假单胞菌的染料连接醇脱氢酶。与染料连接甲醇脱氢酶的比较。
Biochem J. 1978 Mar 1;169(3):677-86. doi: 10.1042/bj1690677.
本文引用的文献
1
Protein measurement with the Folin phenol reagent.使用福林酚试剂进行蛋白质测定。
J Biol Chem. 1951 Nov;193(1):265-75.
2
The kinetics of enzyme-catalyzed reactions with two or more substrates or products. I. Nomenclature and rate equations.具有两种或更多种底物或产物的酶催化反应动力学。I. 命名法和速率方程。
Biochim Biophys Acta. 1963 Jan 8;67:104-37. doi: 10.1016/0006-3002(63)91800-6.
3
The interpretation of kinetic data for enzyme-catalysed reactions involving three substrates.涉及三种底物的酶催化反应动力学数据的解读
Biochem J. 1969 Sep;114(3):547-56. doi: 10.1042/bj1140547.
4
Kinetic studies of the enzymatic dopamine beta-hydroxylation reaction.
Biochemistry. 1968 Aug;7(8):2724-30. doi: 10.1021/bi00848a005.
5
Protein purification by affinity chromatography. Derivatizations of agarose and polyacrylamide beads.通过亲和色谱法进行蛋白质纯化。琼脂糖和聚丙烯酰胺珠粒的衍生化。
J Biol Chem. 1970 Jun;245(12):3059-65.
6
The reaction pathway of membrane-bound rat liver mitochondrial monoamine oxidase.膜结合大鼠肝脏线粒体单胺氧化酶的反应途径。
Biochem J. 1973 Dec;135(4):735-50. doi: 10.1042/bj1350735.
7
Distribution of the enzymes oxidizing secondary and tertiary amines in Pseudomonas aminovorans grown on various substrates.
J Gen Microbiol. 1972 Nov;73(1):205-8. doi: 10.1099/00221287-73-1-205.
8
Microbial oxidation of amines. Partial purification of a mixed-function secondary-amine oxidase system from Pseudomonas aminovorans that contains an enzymically active cytochrome-P-420-type haemoprotein.胺的微生物氧化。从食氨基假单胞菌中部分纯化一种混合功能仲胺氧化酶系统，该系统含有一种具有酶活性的细胞色素-P-420型血红蛋白。
Biochem J. 1971 Nov;125(2):449-59. doi: 10.1042/bj1250449.
9
Affinity chromatography of nicotinamide-adenine dinucleotide-linked dehydrogenases on immobilized derivatives of the dinucleotide.烟酰胺腺嘌呤二核苷酸连接的脱氢酶在二核苷酸固定化衍生物上的亲和层析
Biochem J. 1973 Dec;135(4):595-607. doi: 10.1042/bj1350595.
10
The mechanism of action of the flavoprotein melilotate hydroxylase.
J Biol Chem. 1973 Apr 25;248(8):2953-62.
Zotero 插件