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形狀
buffered aqueous glycerol solution
比活性
0.1-1.0 units/mg protein (Lowry)
異物活動
pyruvate dehydrogenase ≤20%
運輸包裝
dry ice
儲存溫度
−20°C
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一般說明
研究领域：Neuroscience
α-酮戊二酸脱氢酶（α-KGDH）是位于线粒体的一种多酶复合体。这种复合酶由多个单位的硫胺素焦磷酸依赖性脱氢酶(E1)、二氢硫辛酰脱氢酶(E3)和二氢硫辛酰转琥珀酰酶(E2)组成。
α-酮戊二酸脱氢酶（α-KGDH）是位于线粒体的一种多酶复合体。这种复合酶由多个单位的硫胺素焦磷酸依赖性脱氢酶(E1)、二氢硫辛酰脱氢酶(E3)和二氢硫辛酰转琥珀酰酶(E2)组成。
應用
α猪心α-酮戊二酸脱氢酶已用于：
- 研究过氧亚硝酸盐处理细胞中谷胱甘肽(GSH)的反硝化作用
- 通过Spectramax M5微孔板分光荧光计检测其在心肌线粒体中的活性
- 作为阳性对照，通过Spectramax GEMINI EM荧光微孔板读板机评估其在小鼠神经元中的活性
生化／生理作用
αα-酮戊二酸脱氢酶(α-KGDH)是生物能量学过程的关键酶，是Krebs循环或三羧酸(TCA)循环代谢流的调控物。它通过还原型烟酰胺腺嘌呤二核苷酸(NADH)的释放，催化α-酮戊二酸氧化脱羧为琥珀酰-CoA。这是TCA循环中的限速反应。该反应为呼吸链提供电子，需要硫胺素焦磷酸作为辅因子。反应速率由NAD（烟酰胺腺嘌呤二核苷酸）还原决定。αα-KGDH的最佳pH值范围为6.6-7.4。该酶会被氧化应激抑制并导致代谢缺乏。但α-KGDH又能产生活性氧(ROS)导致氧化应激。α-KGDH缺陷或浓度不够会导致好几种神经退行性疾病，比如阿尔茨海默病。
α-Ketoglutarate dehydrogenase is most responsive to alterations in the tumor microenvironment and contributes to the adaptive metabolic response in cancer. Inhibiting α-ketoglutarate dehydrogenase counteracts lung metastasis associated with breast cancer.
品質
可能含有痕量的聚乙二醇。
單位定義
在 30 °C、pH 7.4、饱和水平的辅酶 A 存在的条件下，一单位每分钟可将 1.0 μ 摩尔的 β-NAD 转化成 β-NADH。
外觀
以 50％ 甘油溶液的形式提供，含有 9mg 每毫升的牛血清白蛋白、30％ 蔗糖、1.5 mM EDTA、1.5 mM EGTA、1.5 mM 2-巯基乙醇、0.3％ TRITON™ X-100、0.003％ 叠氮化钠和 15 mM 磷酸钾，pH 6.8。
法律資訊
Triton is a trademark of The Dow Chemical Company or an affiliated company of Dow
危險聲明
防範說明
危險分類
Aquatic Chronic 3
儲存類別代碼
10 - Combustible liquids
水污染物質分類（WGK）
WGK 1
閃點（°F）
Not applicable
閃點（°C）
Not applicable
個人防護裝備
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
其他客户在看
Wagner L Araújo et al.
The Plant cell, 24(6), 2328-2351 (2012-07-04)
Transgenic tomato (Solanum lycopersicum) plants expressing a fragment of the gene encoding the E1 subunit of the 2-oxoglutarate dehydrogenase complex in the antisense orientation and exhibiting substantial reductions in the activity of this enzyme exhibit a considerably reduced rate of
Tristan Wagner et al.
Chemistry & biology, 18(8), 1011-1020 (2011-08-27)
The α-ketoglutarate dehydrogenase (KDH) complex is a major regulatory point of aerobic energy metabolism. Mycobacterium tuberculosis was reported to lack KDH activity, and the putative KDH E1o component, α-ketoglutarate decarboxylase (KGD), was instead assigned as a decarboxylase or carboligase. Here
Shuyi Zhang et al.
Science (New York, N.Y.), 334(6062), 1551-1553 (2011-12-17)
It is generally accepted that cyanobacteria have an incomplete tricarboxylic acid (TCA) cycle because they lack 2-oxoglutarate dehydrogenase and thus cannot convert 2-oxoglutarate to succinyl-coenzyme A (CoA). Genes encoding a novel 2-oxoglutarate decarboxylase and succinic semialdehyde dehydrogenase were identified in
Casey L Quinlan et al.
The Journal of biological chemistry, 289(12), 8312-8325 (2014-02-12)
Several flavin-dependent enzymes of the mitochondrial matrix utilize NAD(+) or NADH at about the same operating redox potential as the NADH/NAD(+) pool and comprise the NADH/NAD(+) isopotential enzyme group. Complex I (specifically the flavin, site IF) is often regarded as
Gary E Gibson et al.
Journal of neurochemistry, 134(1), 86-96 (2015-03-17)
Reversible post-translation modifications of proteins are common in all cells and appear to regulate many processes. Nevertheless, the enzyme(s) responsible for the alterations and the significance of the modification are largely unknown. Succinylation of proteins occurs and causes large changes
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