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
历史批次信息供参考:
分析证书(COA)
Lot/Batch Number
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
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
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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