73063
丙氨酸脱氢酶，重组
recombinant, expressed in E. coli, ≥15 U/mg
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化学文摘社编号:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-847-9
MDL number:
Specific activity:
≥15 U/mg
Recombinant:
expressed in E. coli
产品名称
丙氨酸脱氢酶，重组, recombinant, expressed in E. coli, ≥15 U/mg
recombinant
expressed in E. coli
form
crystals
powder
specific activity
≥15 U/mg
storage temp.
−20°C
Quality Level
Application
Alanine dehydrogenase (ald) is an oxidoreductase that is involved in taurin/hypotaurine metabolism and CO2 fixation. It is used in various enzyme assays and in kinetic studies .
Biochem/physiol Actions
Alanine dehydrogenase catalyzes the reversible reductive amination of pyruvate using NADH as an oxidation/reduction cofactor .
Other Notes
1 U corresponds to the amount of enzyme which converts 1 μmol L-alanine per minute at pH 10.0 and 30°C (NAD as cofactor).
signalword
Danger
hcodes
Hazard Classifications
Resp. Sens. 1
存储类别
11 - Combustible Solids
wgk
WGK 3
法规信息
常规特殊物品
此项目有
M T Smith et al.
The Journal of biological chemistry, 268(15), 10746-10753 (1993-05-25)
The kinetic mechanism of alanine dehydrogenase from soybean nodule bacteroids was studied by initial velocity experiments with or without product inhibitors, dead-end inhibitors, or alternate substrates. Without inhibitors, double-reciprocal plots of initial velocity experiments showed intersecting lines, indicating a sequential
S Shafe et al.
The West Indian medical journal, 58(2), 164-172 (2009-01-01)
The present study sought to determine whether an association exists between alcohol dependence and select affective and anxiety disorders in patients presenting at substance abuse centres in Trinidad and Tobago (TT). The participants in this study were 143 alcohol dependents
Rafael Pernil et al.
Journal of bacteriology, 192(19), 5165-5172 (2010-08-03)
In the diazotrophic filaments of heterocyst-forming cyanobacteria, an exchange of metabolites takes place between vegetative cells and heterocysts that results in a net transfer of reduced carbon to the heterocysts and of fixed nitrogen to the vegetative cells. Open reading
Crystal structures of the Mycobacterium tuberculosis secretory antigen alanine dehydrogenase (Rv2780) in apo and ternary complex forms captures "open" and "closed" enzyme conformations.
Sarvind Mani Tripathi et al.
Proteins, 72(3), 1089-1095 (2008-05-21)
Wei Ye et al.
Microbiological research, 165(4), 268-275 (2009-09-02)
The major objective of the present study is to change the alanine production of Lactic acid bacteria by expression of Bacillus subtilis (natto) alanine dehydrogenase (AlaDH), the gene that is not present in Lactic acid. B. subtilis AlaDH gene (ald)
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