Aldehyde dehydrogenase is a class of enzymes with a variety of aldehydes as substrates. Aldehyde dehydrogenase has been classified according to enzymatic properties, subcellular localization and tissue specificity. In recent years, many studies have found certain aldehydes. In addition to its catalytic action, dehydrogenase has many other important physiological functions. A study by the US National Academy of Sciences shows that the amount of alcohol and the presence or absence of alcohol addiction are not developed by the exercise of the day after tomorrow, but by the "drinking gene", which can affect people's response to alcohol. So decide if this person is an alcoholic.
Aldehyde dehydrogenase is a kind of enzyme with a variety of aldehydes as substrates. In addition to its catalytic effect, aldehyde dehydrogenase has many other important physiological functions. Scientists at the University of Madrid in Spain pointed out that if genetic factors are excluded, drinking during pregnancy is the main reason for the unsound intelligence of the fetus. In fact, drinking alcohol has a lot of harm to the human body, not only for fetal intelligence, but also for the liver, kidney, stomach, prostate, nervous system and cardiovascular of the human body. Especially those who drink on the face, they are more damaging to him, and they can't get on the face, they can still inherit. If the parents are homozygous for the aldehyde dehydrogenase genotype, they will pass on the gene for good drinking to their children.
The spinach betaine aldehyde dehydrogenase gene (SoBADH) was isolated to construct a binary plant expression vector pBSB driven by CaMV35S, and the Agrobacterium strain LBA4404 carried the vector to transform cotton to obtain transgenic cotton plants. 65 strains of transgenic plants were screened by Southern blotting and Southern blotting analysis showed that 45 strains were successful transformants. The foreign genes have been integrated into the cotton genome and inserted in a single copy. Analysis of the expression of the SoBADH gene in some strains showed higher mRNA and protein expression. The betaine dehydrogenase activity in these lines was determined to be significantly increased to a level of 0.66 to 1.70 nmol/min/mg. At the same time, these transgenic lines grew stronger than the control under salt stress, and the fresh weight of plant height and aerial part was significantly higher than that of non-transgenic control. Under low temperature stress, these transgenic lines showed significant antifreeze performance, and the results showed that spinach beet Alkali aldehyde dehydrogenase can be overexpressed in heterologous plant cotton and has high enzymatic activity. Transgenic cotton can be used as a germplasm material for stress-resistant breeding.
A purified aldehyde dehydrogenase having the following physicochemical properties:
1. The molecular weight is 100000±10000 Da (consisting of 2 homologous subunits) or the molecular weight is 150,000±15000 Da (composed of 3 homologous subunits), wherein each subunit has a molecular weight of 55000±2000 Da;
2. Substrate specificity: active against aldehyde compounds;
3. Cofactor: pyrroloquinoline quinone (PQQ);
4. Optimum pH from about 6.5 to about 8.0 (for the production of vitamin C from L-sorbosone) or an optimum pH of about 9.0 (for the production of 2-keto-L-gulonic acid from L-sorbosone));
5. Inhibitors: Co↑ [2+], Cu↑ [2+], Fe↑ [3+], Ni↑ [2+], Zn↑ [2+] and monoiodoacetate.
In the process of inheritance, parents will randomly pass one of the two genes to their children. Therefore, if parents are homozygous, their children are naturally homozygous. From this perspective, good drinking and poor drinking can be inherited. Of course, drinking is also related to body weight, body weight, body fluids, and the dilution effect on alcohol is also strong, so you can drink a little more. In addition, the proportion of genotypes of homozygotes in Westerners is higher, and the aldehyde dehydrogenases they produce have subtle differences and are more active. Therefore, Westerners are better off than the Orientals.
In life, there are many people who drink good, some people fight for the body, and some people naturally rely on enzymes. Needless to say, it is self-inflicted, but even if the enzyme is too much, it is harmful to health. After drinking, ethanol is first converted to acetaldehyde by the action of alcohol dehydrogenase. However, when the blood ethanol concentration is too high, another metabolic pathway is initiated, which is oxidatively decomposed into acetaldehyde by metabolism by the microsomal alcohol oxidase system (MEOS) in the endoplasmic reticulum.
However, ethanol is metabolized by the MEOS pathway, which not only does not produce energy, but also increases the consumption of oxygen, causing energy failure in the liver, damage to liver cells, and even death. At the same time, too much ethanol can cause damage to other organs of the human body, such as stomach bleeding, prostatitis, pancreatitis and even brain cell damage. Moreover, the genetic metabolite acetaldehyde is not only toxic to the liver, but also toxic to the human body. Therefore, even if you have more aldehyde dehydrogenase, its metabolism into acetic acid is faster, and acetaldehyde always has a short residence time in the body. For a long time, this damage can not be ignored.
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