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Merck
CN

O4878

Sigma-Aldrich

草酰乙酸脱羧酶 来源于假单胞菌

lyophilized powder, ≥100 units/mg solid

别名:

OAD

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About This Item

CAS号:
MDL编号:
UNSPSC代码:
12352204
NACRES:
NA.54

形式

lyophilized powder

质量水平

比活

≥100 units/mg solid

储存温度

−20°C

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相关类别

一般描述

草酰乙酸脱羧酶 (OAD) 在厌氧菌中起 Na 泵的作用。是一种由 α、β 和 γ 三个亚基组成的膜蛋白,α 亚基含有羧化酶活性。

应用

来自假单胞菌 属的草酰乙酸脱羧酶已被用于消化低分子量(LMW)人乳馏分(5kF馏分)并可用作测定嗜热纤维梭状芽孢杆菌(C. thermocellum)草酰乙酸脱羧酶活性的阳性对照。
草酰乙酸脱羧酶已用于一项研究,以评估 Na (+)-谷氨酸盐转运蛋白 GltS 的转换率和折返环的可及性。 在一项研究中也被用来研究木葡糖酸醋杆菌对不同碳源的发酵和代谢特性。

生化/生理作用

草酰乙酸脱羧酶催化草酰乙酸盐的脱羧反应,其活性不需要锰和镁。它与多种革兰氏阴性菌有关。

单位定义

在 25℃、pH 8.0 的条件下,每分钟有 1 个单位的草酰乙酸转化为丙酮酸和 CO2

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

分析证书(COA)

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Monica Balsera et al.
The Journal of biological chemistry, 286(11), 9457-9467 (2011-01-07)
The oxaloacetate decarboxylase primary Na(+) pump (OAD) is an essential membrane protein complex that functions in the citrate fermentation pathway of some pathogenic bacteria under anaerobic conditions. OAD contains three different subunits: Oad-α, a biotinylated extrinsic protein that catalyzes the
Pablo D Sender et al.
FEBS letters, 570(1-3), 217-222 (2004-07-15)
The citM gene from Lactococcus lactis CRL264 was demonstrated to encode for an oxaloacetate decarboxylase. The enzyme exhibits high levels of similarity to malic enzymes (MEs) from other organisms. CitM was expressed in Escherichia coli, purified and its oxaloacetate decarboxylase
Pius Dahinden et al.
The FEBS journal, 272(3), 846-855 (2005-01-27)
The oxaloacetate decarboxylase Na+ pumps OAD-1 and OAD-2 of Vibrio cholerae are composed of a peripheral alpha-subunit associated with two integral membrane-bound subunits (beta and gamma). The alpha-subunit contains the carboxyltransferase domain in its N-terminal portion and the biotin-binding domain
Oxalacetic carboxylase of Micrococcus lysodeikticus.
Herbert, D.
Methods in Enzymology, 1, 753-757 (1955)
Tomas Krupnik et al.
Molecular membrane biology, 28(7-8), 462-472 (2011-10-15)
GltS of Escherichia coli is a secondary transporter that catalyzes Na+-glutamate symport. The structural model of GltS shows two homologous domains with inverted membrane topology that are connected by a central loop that resides in the cytoplasm. Each domain contains

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