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
历史批次信息供参考:
分析证书(COA)
Lot/Batch Number
Vadim S Pokrovsky et al.
Anti-cancer drugs, 24(8), 846-851 (2013-06-20)
L-Lysine α-oxidase (LO) from a novel Trichoderma strain: Trichoderma cf. aureoviride Rifai shows favorable biochemical and kinetic properties (Km for L-lysine of 17.9 µmol/l, optimum pH 8.0, high stability) and significant antiproliferative activity both in vitro and in vivo. The
Recombinant expression, molecular characterization and crystal structure of antitumor enzyme, l-lysine alpha-oxidase from Trichoderma viride
Amano M, et al.
The Journal of Biological Chemistry, 157(6), 549-559 (2015)
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
Patricia Lucas-Elío et al.
Journal of bacteriology, 188(7), 2493-2501 (2006-03-21)
Marinocine is a broad-spectrum antibacterial protein synthesized by the melanogenic marine bacterium Marinomonas mediterranea. This work describes the basis for the antibacterial activity of marinocine and the identification of the gene coding for this protein. The antibacterial activity is inhibited
E E Ferapontova et al.
Biochemistry. Biokhimiia, 66(8), 832-839 (2001-09-22)
Adsorption and bioelectrocatalytic activity of native horseradish peroxidase (HRP) and its recombinant forms on polycrystalline gold electrodes were studied. Recombinant forms of HRP were produced by a genetic engineering approach using an E. coli expression system. According to direct mass
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