Nnjm2 at 18:19, 22 October 2018

2018-10-22T18:19:44Z

← Older revision		Revision as of 18:19, 22 October 2018
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	~~ ~~Ubiquitin- activating enzyme E3, alongside E1 and E2 enzymes and [[ATP\|ATP]], is required for the addition of at least 5~~ ~~[[Ubiquitin\|ubiquitin]]~~ ~~molecules, to form a chain, to protein substrates. Such substrates attach to a 26S [[Proteasome\|proteasome]]~~ ~~to be then converted into amino acids or used for [[Antigen\|antigen]] presentation. ~~Ubiquination~~, and therefore ubiquitin activating enzyme E3, is required for the activation of NF-kB, a nuclear factor if the kappa light chain in [[B-cells\|B cell antibodies]], which is utilised in responses to stress and infection		Ubiquitin-activating enzyme E3, alongside E1 and E2 enzymes and [[ATP\|ATP]], is required for the addition of at least 5 [[Ubiquitin\|ubiquitin]] molecules, to form a chain, to protein substrates. Such substrates attach to a 26S [[Proteasome\|proteasome]] to be then converted into amino acids or used for [[Antigen\|antigen]] presentation. Ubiquitination, and therefore ubiquitin-activating enzyme E3, is required for the activation of NF-kB, a nuclear factor if the kappa light chain in [[B-cells\|B cell antibodies]], which is utilised in responses to stress and infection

	The E3 enzyme is a [[Ligases\|ligase]]~~ ~~and works via mediating the attachment of ubiquitin molecules, previously attached to the E2 enzymes to the target protein<ref>Annual ~~Reveiew~~ of Biochemistry (1998) (67: 425-479) "The ubiquitin system" Hershko A, Ciechanover A. https://www.annualreviews.org/doi/10.1146/annurev.biochem.67.1.425</ref>.		The E3 enzyme is a [[Ligases\|ligase]] and works via mediating the attachment of ubiquitin molecules, previously attached to the E2 enzymes to the target protein<ref>Annual Review of Biochemistry (1998) (67: 425-479) "The ubiquitin system" Hershko A, Ciechanover A. https://www.annualreviews.org/doi/10.1146/annurev.biochem.67.1.425</ref>.

	There are many families of the ubiquitin ligase in which the mechanisms of attaching ubiquitin differ. Enzymes of the HECT domain type require an additional transthiolation reaction, one previously in order to remove E1 from ubiquitin and add E2 in replacement. Contrastingly, ligases of the RING finger type have the ability to remove ubiquitin from E2 onto protein substrates in one step<ref>Metzger MB, Hristova VA, Weissman AM (Feb 2012). HECT and RING finger families of E3 ubiquitin ligases at a glance. Journal of Cell Science. 125 (Pt 3): 531–7. doi:10.1242/jcs.091777</ref>.		There are many families of the ubiquitin ligase in which the mechanisms of attaching ubiquitin differ. Enzymes of the HECT domain type require an additional transthiolation reaction, one previously in order to remove E1 from ubiquitin and add E2 in replacement. Contrastingly, ligases of the RING finger-type have the ability to remove ubiquitin from E2 onto protein substrates in one step<ref>Metzger MB, Hristova VA, Weissman AM (Feb 2012). HECT and RING finger families of E3 ubiquitin ligases at a glance. Journal of Cell Science. 125 (Pt 3): 531–7. doi:10.1242/jcs.091777</ref>.

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	=== References ===		=== References ===

	~~===~~ <references />~~[[]] ===~~		<references />

170313698: Created page with " Ubiquitin- activating enzyme E3, alongside E1 and E2 enzymes and ATP, is required for the addition of at least 5 ubiquitin molecules, to for..."

2018-10-22T17:56:10Z

Created page with " Ubiquitin- activating enzyme E3, alongside E1 and E2 enzymes and ATP, is required for the addition of at least 5 ubiquitin molecules, to for..."

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 Ubiquitin- activating enzyme E3, alongside E1 and E2 enzymes and [[ATP|ATP]], is required for the addition of at least 5 [[Ubiquitin|ubiquitin]] molecules, to form a chain, to protein substrates. Such substrates attach to a 26S [[Proteasome|proteasome]] to be then converted into amino acids or used for [[Antigen|antigen]] presentation. Ubiquination, and therefore ubiquitin activating enzyme E3, is required for the activation of NF-kB, a nuclear factor if the kappa light chain in [[B-cells|B cell antibodies]], which is utilised in responses to stress and infection

The E3 enzyme is a [[Ligases|ligase]] and works via mediating the attachment of ubiquitin molecules, previously attached to the E2 enzymes to the target protein<ref>Annual Reveiew of Biochemistry (1998) (67: 425-479) "The ubiquitin system" Hershko A, Ciechanover A. https://www.annualreviews.org/doi/10.1146/annurev.biochem.67.1.425</ref>.

There are many families of the ubiquitin ligase in which the mechanisms of attaching ubiquitin differ. Enzymes of the HECT domain type require an additional transthiolation reaction, one previously in order to remove E1 from ubiquitin and add E2 in replacement. Contrastingly, ligases of the RING finger type have the ability to remove ubiquitin from E2 onto protein substrates in one step<ref>Metzger MB, Hristova VA, Weissman AM (Feb 2012). HECT and RING finger families of E3 ubiquitin ligases at a glance. Journal of Cell Science. 125 (Pt 3): 531–7. doi:10.1242/jcs.091777</ref>.

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=== References ===

=== <references />[[]] ===

Ubiquitin-activating enzyme E3 - Revision history

Nnjm2 at 18:19, 22 October 2018

170313698: Created page with " Ubiquitin- activating enzyme E3, alongside E1 and E2 enzymes and ATP, is required for the addition of at least 5 ubiquitin molecules, to for..."