47753
甲酸脱氢酶 来源于博伊丁假丝酵母
liquid (clear), clear brown, 40.0-60.0 U/mL
别名:
FDH, 甲酸盐:NAD+ 氧化还原酶
生物来源
fungus (Candida boidinii)
表单
liquid (clear)
分子量
Mr ~76000
浓度
40.0-60.0 U/mL
颜色
clear brown
密度
1.1 g/mL at 20 °C
储存温度
−20°C
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生化/生理作用
甲酸脱氢酶参与植物的应激反应并催化 NAD+ 还原为 NADH。
其他说明
在 pH 7.6 和 25 °C 下，1U 相当于每分钟氧化 1 μmol 甲酸钠（货号 71539）所需的酶量
由 NAD 再生 NADH 的优选酶
警示用语：
Danger
危险声明
预防措施声明
危险分类
Resp. Sens. 1
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
K. Drauz et al.
Enzyme Catalysis in Organic Synthesis, 597-597 (1995)
C Vinals et al.
Biochemical and biophysical research communications, 192(1), 182-188 (1993-04-15)
We propose a multiple alignment of the sequence of formate dehydrogenase with the D-specific 2-hydroxy acid dehydrogenases family. Structurally conserved regions are predicted for those sequences corresponding to important regions of the catalytic and the coenzyme binding domains defined from
Samrat Dutta et al.
The journal of physical chemistry. B, 116(1), 542-548 (2011-12-01)
Functionally relevant femtosecond to picosecond dynamics in enzyme active sites can be difficult to measure because of a lack of spectroscopic probes that can be located in the active site without altering the behavior of the enzyme. We have developed
Yoshihiro Ojima et al.
Biotechnology letters, 34(5), 889-893 (2012-01-05)
Pyruvate was produced from glucose by Escherichia coli BW25113 that contained formate dehydrogenase (FDH) from Mycobacterium vaccae. In aerobic shake-flask culture (K (L) a = 4.9 min(-1)), the recombinant strain produced 6.7 g pyruvate l(-1) after 24 h with 4 g sodium formate l(-1) and a yield of
Sofia Marques da Silva et al.
Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 17(5), 831-838 (2012-04-25)
Desulfovibrio spp. are sulfate-reducing organisms characterized by having multiple periplasmic hydrogenases and formate dehydrogenases (FDHs). In contrast to enzymes in most bacteria, these enzymes do not reduce directly the quinone pool, but transfer electrons to soluble cytochromes c. Several studies
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