form
lyophilized powder
specific activity
25-50 units/mg solid
mol wt
44 kDa
storage temp.
−20°C
Quality Level
General description
单体肌氨酸氧化酶(MSOX)是一种黄素酶,可催化肌氨酸(N-甲基甘氨酸)发生氧化去甲基化,产生甘氨酸、甲醛和过氧化氢。单体肌氨酸氧化酶可以氧化其他次级氨基酸,例如N-甲基-L-丙氨酸、N-乙基甘氨酸和L-脯氨酸。
肌氨酸氧化酶是 44kDa 蛋白质,其共价结合 1 mol 黄素腺嘌呤二核苷酸(FAD)。它属于具有结合 FAD 的氨基酸氧化酶家族。
Application
来自芽孢杆菌的肌氨酸氧化酶已被用作阳性对照,用于通过 UV 共价结合黄素腺嘌呤二核苷酸(FAD)检测蛋白质。它还被用于通过与铂电极上的其他酶共固定来制备肌酸酐生物传感器。
肌氨酸氧化酶已用于研究固定化构建的安培生物传感器时作为多酶级联反应的一个组份。肌氨酸氧化酶也被用于研究黄素蛋白对胺的氧化作用。
Physical form
没有添加稳定剂
Other Notes
在 pH8.3,37℃ 下,一个单位的酶每分钟从肌氨酸形成 1.0 μmole 甲醛。
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
存储类别
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
法规信息
常规特殊物品
此项目有
Paul F Fitzpatrick
Archives of biochemistry and biophysics, 493(1), 13-25 (2009-08-05)
Many flavoproteins catalyze the oxidation of primary and secondary amines, with the transfer of a hydride equivalent from a carbon-nitrogen bond to the flavin cofactor. Most of these amine oxidases can be classified into two structural families, the D-amino acid
Rastislav Monošík et al.
Analytical biochemistry, 421(1), 256-261 (2011-11-10)
Amperometric biosensors based on gold planar or nanocomposite electrode containing multiwalled carbon nanotubes for determination of glycerol were developed. The biosensors were constructed by immobilization of a novel multienzyme cascade consisting of glycerol kinase/creatine kinase/creatinase/sarcosine oxidase/peroxidase between a chitosan "sandwich."
Optimization of the production of Chondrus crispus hexose oxidase in Pichia pastoris
Wolff AM, et al.
Protein Expression and Purification, 22(2), 189-199 (2001)
Handbook of Flavoproteins: Oxidases, Dehydrogenases and Related Systems, 196-196 (2012)
Mutsumi Saito et al.
Journal of biochemistry, 141(6), 799-815 (2007-03-31)
Heterotetrameric sarcosine oxidase from Corynebacterium sp.U-96(SO-U96) contains non-covalent and covalent flavins. Lys-358 and Lys-171 in the beta subunit is present at non-covalent flavin adenine dinucleotide (FAD)- and covalent flavin monodinucleotide (FMN)-binding sites, respectively. The Lys-358 mutant, K358R showed 0.07% activity
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