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Above undated message substituted from Template:Dashboard.wikiedu.org assignment by PrimeBOT ( talk) 13:46, 16 January 2022 (UTC)
I think the link to acetate is wrong, but I don't know what the right link should be. -- Walt Pohl 03:39, 17 Nov 2004 (UTC)
Er, now that I have your attention...a recent edit begs a question: how can it be possible that a sexual dichotomy exists in digestive enzyme production? I could imagine sexual dimorphism, but this article seems to assert that all women have a different gene coding for this enzyme than all men...or that some digestive enzyme genes are turned off in women, but active in men, which seems only slightly less plausible. I want to know whose theory this is.-- Joel 23:32, 11 July 2005 (UTC)
"It is believed that alcohol dehydrogenase in women is less effective than that in men, which can cause women to be more affected by alcohol than men." This suggests that women have a different type of alcohol dehydrogenase. I think it would be more appropriate to state that the activity of alcohol dehydrogenase is lower.
-I agree; I believe the expression level is lower, but I don't have time to find a source, sorry! Also, shouldn't the statement about ethnic variation be re-written? It doesn't make a lot of sense as is. Are asians lower or higher in ADH? What about Jews? -- Eirinn 13:25, 25 October 2005 (UTC)
-its not so black and white - certain populations show polymorphisms of 2 ADH genes, so if an individual is from that population they are more likely to contain those alleles. This means they have more genes producing ADH, which leads to the problem with not being able to take alcohol as well. Asian populations tend to show higher frequencies of those genes compared to Western populations. Not sure about Jews offhand.
-Alcohol has three main different mechanisms for breakdown; P450's, ADH and peroxide, so any one pathway could be deficient in women. The ADH pathway may be perfect. Paul, 14-12-06
I got in an argument with a friend of the family once - me claiming the metabolism of alcohol provides the body no useful energy, her claiming it does. Does anyone know who is right? - GSchjetne 08:52, 2 April 2006 (UTC)
Your freind is right, alcohol is a metabolic precursor to Acteyl CoA (takes a few steps to get there). This is the molecule that enters the Krebs cycle, which generates NADH for use in oxidative phosphorylation in the electron transport chain.
A chemical mechanism (preferably including residues and cofactors) would be nice Paul, 14-12-06
No mention has been made of elevated gene expression, in response to continuous exposure to the substrate and why this means the person has to consume progressively larger quantities to achieve the desired level of intoxication. This leads to 'stockpiling' of the enzyme and liver damage from the increased amounts of the reaction products. I don't have any sources to quote, at present. EatYerGreens 13:27, 21 February 2007 (UTC)
There are two problems with methanol: 1) "Alcohol dehydrogenase is also involved in the toxicity of other types of alcohol: for instance, it oxidizes methanol to produce formaldehyde, " well in fact the formaldehyde is the toxic compound and not the methanol itself. So in this case this enzyme is not reducing the methanol toxicity, but instead it is aggravating the problems. 2) Alcohol dehydrogenase is marginarly catalisyng the methanol oxidation, its prefered substrate being ethanol. In fact only some isoenzymes are able to oxidise the methanol and even those at much lower speed compared with ethanol. The enzyme that preferes methanol to ethanol is the alcohol oxidase (1.1.3.13). Sorry I do not have references to modify the main page. BdB-18 18:36, 21 May 2007 (UTC)BdB-18
It seems a little inappropriate to say that ADH does not work well on primary alcohols, as its primary function is with the primary alcohol methanol, and one of its most toxicologically important substrates (ethylene glycol) is also primary. —Preceding unsigned comment added by Mah159 ( talk • contribs) 04:10, 1 March 2008 (UTC)
"For example, populations from Europe have been found to express an allele for the alcohol dehydrogenase gene that makes it much more active than those found in populations from Asia or the Americas."
This statements are incorrect, a faster metabolizing form of ADH means a decreased risk of alcoholism (because of the production of toxic aldehydes). Many Asians have a faster metabolizing form of ADH, (but a ineffective version of the aldehydes dehydrogenase)
"If the variants of these genes encode slower metabolizing forms of ADH2 and ADH3, there is increased risk of alcoholism. The studies have found that mutations of ADH2 and ADH3 are related to alcoholism in Asian populations"
This statement is confusing, it seems to say alcoholism is a bigger problem in Asian populations, which is contrary to the facts.
Clacker ( talk) 21:03, 21 July 2008 (UTC)
Would anyone be able to create or dig up a cartoon to depict the dehydrogenation mechanism? The step-by-step description is good but it would be nice if we could have an illustration. Thanks! :) Isopropyl ( talk) 20:28, 27 December 2008 (UTC)
Perhaps someone could change the link to BRENDA in the "Notation" part for all enzymes. The link should be:
http://www.brenda-enzymes.org/literature/lit.php4?e=1.1.1.1
The reason is that we try to establish this adress as the main one.
Best regards,
Andreas
The statement "Alcohol dehydrogenase was first discovered in the mid-1960s in Drosophila melanogaster" is not true. In the mid-1960 ADH was discovered in drosophilla though had been discovered in other organisms before this. However I am unable to find the exact date of discovery. Can anyone else help with this? —Preceding unsigned comment added by 94.192.232.151 ( talk) 21:00, 30 April 2009 (UTC)
I think the following explanation for the differences among populations is essentially wrong:
In fact, the Alcohol Dehydrogenase (ADH) enzymatic activity of those alleles more frequent in Asian populations is not lower but higher and the overall effect may be exacerbated by a lower activity than normal in the prevalent alleles of the following enzyme in the alcohol catabolic pathway: the Aldehyde Dehydrogenase (ALDH2).
I have copied an extract from a recent scientific article on the topic to reference my previous assertion:
Farhanasadmohamed ( talk) 00:06, 7 December 2015 (UTC)
References
I think the line ″Humans have at least six slightly different alcohol dehydrogenases. ″ might be outdated as the RSCB's PBD-101 page on alcohol dehydrogenases says "Our bodies create at least nine different forms of alcohol dehydrogenase, each with slightly different properties.″ Here's the web address: http://pdb101.rcsb.org/motm/13
Dan McCulloch ( talk) 19:29, 14 March 2019 (UTC)
![]() | This article is rated C-class on Wikipedia's
content assessment scale. It is of interest to the following WikiProjects: | |||||||||||||
|
This article is or was the subject of a Wiki Education Foundation-supported course assignment. Further details are available
on the course page.
Above undated message substituted from Template:Dashboard.wikiedu.org assignment by PrimeBOT ( talk) 13:46, 16 January 2022 (UTC)
I think the link to acetate is wrong, but I don't know what the right link should be. -- Walt Pohl 03:39, 17 Nov 2004 (UTC)
Er, now that I have your attention...a recent edit begs a question: how can it be possible that a sexual dichotomy exists in digestive enzyme production? I could imagine sexual dimorphism, but this article seems to assert that all women have a different gene coding for this enzyme than all men...or that some digestive enzyme genes are turned off in women, but active in men, which seems only slightly less plausible. I want to know whose theory this is.-- Joel 23:32, 11 July 2005 (UTC)
"It is believed that alcohol dehydrogenase in women is less effective than that in men, which can cause women to be more affected by alcohol than men." This suggests that women have a different type of alcohol dehydrogenase. I think it would be more appropriate to state that the activity of alcohol dehydrogenase is lower.
-I agree; I believe the expression level is lower, but I don't have time to find a source, sorry! Also, shouldn't the statement about ethnic variation be re-written? It doesn't make a lot of sense as is. Are asians lower or higher in ADH? What about Jews? -- Eirinn 13:25, 25 October 2005 (UTC)
-its not so black and white - certain populations show polymorphisms of 2 ADH genes, so if an individual is from that population they are more likely to contain those alleles. This means they have more genes producing ADH, which leads to the problem with not being able to take alcohol as well. Asian populations tend to show higher frequencies of those genes compared to Western populations. Not sure about Jews offhand.
-Alcohol has three main different mechanisms for breakdown; P450's, ADH and peroxide, so any one pathway could be deficient in women. The ADH pathway may be perfect. Paul, 14-12-06
I got in an argument with a friend of the family once - me claiming the metabolism of alcohol provides the body no useful energy, her claiming it does. Does anyone know who is right? - GSchjetne 08:52, 2 April 2006 (UTC)
Your freind is right, alcohol is a metabolic precursor to Acteyl CoA (takes a few steps to get there). This is the molecule that enters the Krebs cycle, which generates NADH for use in oxidative phosphorylation in the electron transport chain.
A chemical mechanism (preferably including residues and cofactors) would be nice Paul, 14-12-06
No mention has been made of elevated gene expression, in response to continuous exposure to the substrate and why this means the person has to consume progressively larger quantities to achieve the desired level of intoxication. This leads to 'stockpiling' of the enzyme and liver damage from the increased amounts of the reaction products. I don't have any sources to quote, at present. EatYerGreens 13:27, 21 February 2007 (UTC)
There are two problems with methanol: 1) "Alcohol dehydrogenase is also involved in the toxicity of other types of alcohol: for instance, it oxidizes methanol to produce formaldehyde, " well in fact the formaldehyde is the toxic compound and not the methanol itself. So in this case this enzyme is not reducing the methanol toxicity, but instead it is aggravating the problems. 2) Alcohol dehydrogenase is marginarly catalisyng the methanol oxidation, its prefered substrate being ethanol. In fact only some isoenzymes are able to oxidise the methanol and even those at much lower speed compared with ethanol. The enzyme that preferes methanol to ethanol is the alcohol oxidase (1.1.3.13). Sorry I do not have references to modify the main page. BdB-18 18:36, 21 May 2007 (UTC)BdB-18
It seems a little inappropriate to say that ADH does not work well on primary alcohols, as its primary function is with the primary alcohol methanol, and one of its most toxicologically important substrates (ethylene glycol) is also primary. —Preceding unsigned comment added by Mah159 ( talk • contribs) 04:10, 1 March 2008 (UTC)
"For example, populations from Europe have been found to express an allele for the alcohol dehydrogenase gene that makes it much more active than those found in populations from Asia or the Americas."
This statements are incorrect, a faster metabolizing form of ADH means a decreased risk of alcoholism (because of the production of toxic aldehydes). Many Asians have a faster metabolizing form of ADH, (but a ineffective version of the aldehydes dehydrogenase)
"If the variants of these genes encode slower metabolizing forms of ADH2 and ADH3, there is increased risk of alcoholism. The studies have found that mutations of ADH2 and ADH3 are related to alcoholism in Asian populations"
This statement is confusing, it seems to say alcoholism is a bigger problem in Asian populations, which is contrary to the facts.
Clacker ( talk) 21:03, 21 July 2008 (UTC)
Would anyone be able to create or dig up a cartoon to depict the dehydrogenation mechanism? The step-by-step description is good but it would be nice if we could have an illustration. Thanks! :) Isopropyl ( talk) 20:28, 27 December 2008 (UTC)
Perhaps someone could change the link to BRENDA in the "Notation" part for all enzymes. The link should be:
http://www.brenda-enzymes.org/literature/lit.php4?e=1.1.1.1
The reason is that we try to establish this adress as the main one.
Best regards,
Andreas
The statement "Alcohol dehydrogenase was first discovered in the mid-1960s in Drosophila melanogaster" is not true. In the mid-1960 ADH was discovered in drosophilla though had been discovered in other organisms before this. However I am unable to find the exact date of discovery. Can anyone else help with this? —Preceding unsigned comment added by 94.192.232.151 ( talk) 21:00, 30 April 2009 (UTC)
I think the following explanation for the differences among populations is essentially wrong:
In fact, the Alcohol Dehydrogenase (ADH) enzymatic activity of those alleles more frequent in Asian populations is not lower but higher and the overall effect may be exacerbated by a lower activity than normal in the prevalent alleles of the following enzyme in the alcohol catabolic pathway: the Aldehyde Dehydrogenase (ALDH2).
I have copied an extract from a recent scientific article on the topic to reference my previous assertion:
Farhanasadmohamed ( talk) 00:06, 7 December 2015 (UTC)
References
I think the line ″Humans have at least six slightly different alcohol dehydrogenases. ″ might be outdated as the RSCB's PBD-101 page on alcohol dehydrogenases says "Our bodies create at least nine different forms of alcohol dehydrogenase, each with slightly different properties.″ Here's the web address: http://pdb101.rcsb.org/motm/13
Dan McCulloch ( talk) 19:29, 14 March 2019 (UTC)