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）
生物来源
fungus (Trichoderma viride)
质量水平
表单
lyophilized powder
比活
≥20 units/mg protein
分子量
112 kDa
组成
Protein, 5-20%
储存温度
2-8°C
一般描述
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。
应用
赖氨酸氧化酶（来自绿色木霉）已用于制备生物发光芯片。
生化/生理作用
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。
外形
含有磷酸盐缓冲盐和稳定剂
其他说明
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。
储存分类代码
11 - Combustible Solids
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
个人防护装备
Eyeshields, Gloves, type N95 (US)
法规信息
常规特殊物品
此项目有
I P Smirnova et al.
Voprosy meditsinskoi khimii, 46(4), 384-387 (2000-11-15)
The ability of protein isolated from (Trichoderma Rifai) and azydothymidine to inhibit the reproduction of HIV-virus was compared. The obtained experimental data have verified that Trichoderma Rifai protein is a promising human immunodeficiency virus (HIV) inhibitor.
O S Zhukova et al.
Voprosy meditsinskoi khimii, 47(6), 588-592 (2002-04-03)
The conjugates of L-lysine alpha-oxidase and monoclonal antibodies ICO-80 towards CD-5 receptor were produced using glutaraldehyde. The cytotoxic effect of conjugates on Yurkat cells line appeared to be lower in comparison with the native enzyme. Negligible decrease of conjugate biological
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
E V Lukasheva et al.
Biochemistry. Biokhimiia, 67(10), 1152-1158 (2002-12-04)
This review summarizes data on the properties of L-lysine alpha-oxidase, an enzyme that belongs to the group of oxidases of L-amino acids. This enzyme acts virtually only on L-lysine with a rather low Km yielding alpha-keto-epsilon-aminocaproic acid. The decrease in
Jedidah W Danson et al.
Analytical biochemistry, 303(2), 120-130 (2002-04-13)
A new assay for l-lysine alpha-oxidase is described. In this assay, the oxidized product generated from l-lysine is reacted with semicarbazide to form alpha-keto-epsilon-aminocaproate semicarbazone. Formation of the alpha-keto acid semicarbazone is continuously monitored spectrophotometrically at 248 nm (epsilon 10,160
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