Talk:Glutamine synthetase

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Relevant to Eukaryotes

I saw references to bacteria and plants in the text, is this Enzyme Relevant to humans? — Preceding unsigned comment added by Leopardtail (talk • contribs) 18:58, 29 April 2014 (UTC)[reply]

I believe so because it says astrocytes... 2A02:1812:1126:5D00:7487:A569:C09A:8ACD (talk) 07:14, 21 September 2023 (UTC)[reply]

few remarks about regulation

1- I think that the adenylylation reaction miss a word: I suppose you mean:

(Adenylyl transferase and PA reduces GS activity by attaching an AMP unit to GS) instead of saying:

(PA reduces GS activity by attaching an AMP unit to GS).

the reason is what has been already said earlier:

→ ("Adenylyl transferase" catalyzes the adenylylation and phosphorolysis reactions.[8] Adenyl transferase activity is "influenced" by two regulatory proteins: PA and PD)

so the reaction caused by the enzyme & PA only influence it, when mentioned alone it looks as it carry out the reaction alone which contradict the above statement (the arrow)

2- I will try to re-explain this phrase:

(Glutamate is another product of glutamine metabolism; however, glutamate is a substrate for GS inhibiting it to act as a regulator to GS.)

what I got from that line: in glutamine synthetase: not only the product (glutamine) show feedback inhibition, but also the downstream metabolites of this product (the farther away products) one of them is glutamine (apparently by some other enzyme) so this particular product is an exception (it stimulate the GS) because this metabolism "re-create" the substrate

3- this is a question rather than a remark: you said:

Methionine Sulfoximine is an irreversible, non-covalent inhibition of GS. (but aren't all irreversible inhibitors covalent? and if it is non-covalent it means reversible? that what I was thinking ??)

Yasir muhammed ali (talk) 07:54, 12 April 2016 (UTC)[reply]

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Acamprosate

Evidence that acamprosate treatment in alcohol use disorder promotes GS activity, which may be a potential mechanism explaining the reduction of glutamate levels by acamprosate in responders: https://www.nature.com/articles/tp2015120

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Regulation of glutamine synthetase through covalent modification.jpg

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