L6150
赖氨酸氧化酶 来源于绿色木霉
lyophilized powder, ≥20 units/mg protein
别名:
L -赖氨酸：氧氧化还原酶（脱氨）
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关于此项目
化学文摘社编号:
UNSPSC Code:
12352204
NACRES:
NA.54
MDL number:
Specific activity:
≥20 units/mg protein
Biological source:
fungus (Trichoderma viride)
biological source
fungus (Trichoderma viride)
form
lyophilized powder
specific activity
≥20 units/mg protein
mol wt
112 kDa
composition
Protein, 5-20%
storage temp.
2-8°C
Quality Level
General description
赖氨酸氧化酶（来自绿色木霉）是一种分子量为112kDa的同型二聚体黄素酶。在65°C下稳定，对L-赖氨酸具有高度选择性。它由FAD结合、底物结合和螺旋结构域组成，具有明显的活性部位通道。
Application
赖氨酸氧化酶（来自绿色木霉）已用于制备生物发光芯片。
Biochem/physiol Actions
赖氨酸氧化酶（来自绿色木霉）通过催化L-赖氨酸的氧化脱氨形成α-酮基-ε-氨基己酸。它在白血病细胞中表现抗癌能力,也是鳞状细胞、成纤维细胞、卵巢和胃癌的肿瘤抑制剂。赖氨酸氧化酶在结缔组织结构完整性和胚胎发育中起重要作用。
Physical form
含有磷酸盐缓冲盐和稳定剂
Other Notes
一个单元在 37°C，pH 8.0 的条件下催化 L-赖氨酸每分钟生成 1 μmol 的 6-氨基-2-氧代己酸。
存储类别
11 - Combustible Solids
wgk
WGK 3
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
Raluca-Ioana Stefan-van Staden et al.
Biosensors & bioelectronics, 35(1), 439-442 (2012-03-16)
An amperometric biosensor was proposed for the enantioanalysis of L-lysine. The biosensor is based on the impregnation of L-lysine oxidase in diamond paste. The potential used for the determination of l-lysine was 650 mV. The biosensor exhibited a linear concentration
Design of luminescent biochips based on enzyme, antibody, or DNA composite layers
Marquette CA, et al.
Analytical and Bioanalytical Chemistry, 377(5), 922-928 (2003)
I P Smirnova et al.
Voprosy meditsinskoi khimii, 44(4), 384-387 (1998-12-10)
L-lysin-a-oxidase (LO), a fungal enzyme catalysing oxidative deamination of L-lysin, was used for the inhibition of the reproduction of herpes simplex virus type 1 (HSV-1). Antiviral activity of LO was tested in vitro. The expression of viral antigens and CPE
Studies on Anti-Cancer Activity of Lysyl Oxidase from Trichoderma Viride MTCC 167
Kalra S, et al.
International Journal of Applied Sciences and Biotechnology, 4(1), 57-63 (2016)
Seiji Okazaki et al.
Journal of biochemistry, 154(3), 233-236 (2013-08-03)
We have determined the x-ray crystal structure of L-lysine ε-oxidase from Marinomonas mediterranea in its native and L-lysine-complex forms at 1.94- and 1.99-Å resolution, respectively. In the native enzyme, electron densities clearly indicate the presence of cysteine tryptophylquinone (CTQ) previously
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