Catalyses the ATP-dependent activation of ubiquitin through the formation of a thioester bond between the C-terminal glycine of ubiquitin and the sulfhydryl side group of a cysteine residue in the E1 protein. The two-step reaction consists of the ATP-dependent formation of an E1-ubiquitin adenylate intermediate in which the C-terminal glycine of ubiquitin is bound to AMP via an acyl-phosphate linkage, then followed by the conversion to an E1-ubiquitin thioester bond via the cysteine residue on E1 in the second step.
E1 consumes ATP and converts ubiquitin to a transfer-competent, enzyme-bound thioester. The reaction begins with ubiquitin-adenylate formation and the release of diphosohate. The active site cysteine of the E1 then displaces the AMP leading to a ubiquitin-E1 thioester complex
Catalyses the ATP-dependent activation of ubiquitin through the formation of a thioester bond between the C-terminal glycine of ubiquitin and the sulfhydryl side group of a cysteine residue in the E1 protein. The two-step reaction consists of the ATP-dependent formation of an E1-ubiquitin adenylate intermediate in which the C-terminal glycine of ubiquitin is bound to AMP via an acyl-phosphate linkage, then followed by the conversion to an E1-ubiquitin thioester bond via the cysteine residue on E1 in the second step.
E1 consumes ATP and converts ubiquitin to a transfer-competent, enzyme-bound thioester. The reaction begins with ubiquitin-adenylate formation and the release of diphosohate. The active site cysteine of the E1 then displaces the AMP leading to a ubiquitin-E1 thioester complex
E1 consumes ATP and converts ubiquitin to a transfer-competent, enzyme-bound thioester. The reaction begins with ubiquitin-adenylate formation and the release of diphosohate. The active site cysteine of the E1 then displaces the AMP leading to a ubiquitin-E1 thioester complex
E1 activity is assesssed by the capacity of the enzyme to form a thiol ester conjugate with ubiquitin in an ATP-dependent process and to transfer this activated ubiquitin molecule to an conjugating enzyme
chimeric mutant Aos1-Uba2 SUMO-E1 enzyme shows SUMO-E1 activity. The E1 enzyme catalyzes the formation of a thioester-linked complex between SUMO and the E2 enzyme. This process is initiated by activation of the carboxyl terminus of SUMO by adenylation, followed by a thioesterification reaction in which SUMO is conjugated to a cysteine residue at the active site of Uba2 in the E1 enzyme. SUMO is then transferred to the active site cysteine of the E2 enzyme, Ubc9, via a trans-thioesterification reaction. A SUMO-charged E2 enzyme and substrate are finally bound with or without the assistance of a distinct class of SUMO E3-ligases, resulting in the activated SUMO bound to the substrate through an isopeptide linkage
E1 consumes ATP and converts ubiquitin to a transfer-competent, enzyme-bound thioester. The reaction begins with ubiquitin-adenylate formation and the release of diphosohate. The active site cysteine of the E1 then displaces the AMP leading to a ubiquitin-E1 thioester complex
E1 consumes ATP and converts ubiquitin to a transfer-competent, enzyme-bound thioester. The reaction begins with ubiquitin-adenylate formation and the release of diphosohate. The active site cysteine of the E1 then displaces the AMP leading to a ubiquitin-E1 thioester complex
i.e. PYZD-4409. In a mouse model of leukemia, intraperitoneal administration of PYZD-4409 decreases tumor weight and volume compared with control without untoward toxicity
in mouse embryo fibroblast cell A31N-ts20, which is thermosensitive for ubiquitin-activating enzyme E1, the enzymatic activity of the enzyme is heat-inactivatable in vitro; and a major mechanism responsible for E1 inactivation in vivo consists of accelerated destruction. In vivo, ubiquitination of the various protein substrates in A31N-ts20 cells requires different amounts of E1 enzyme
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
NMR structural studies of the first catalytic cysteine half domain FCCH, interaction studies of FCCH and the other catalytic E1 domain SCCH, second catalytic cysteine half-domain. The E1 has several domains, an adenylation domain, composed of an active and inactive adenylation subdomains, and a catalytic cysteine domain, and smaller accessory domains: a four helix bundle and a ubiquitin fold domain. NMR cannot detect interactions between the FCCH and ubiquitin, or betweenween FCCH and SCCH if they are on separate poypeptide chains
construction of a mouse Aos1-Uba2 chimeric SUMO(small ubiquitin-related modifier)-E1 enzyme, mAU. The SUMO-E1 enzyme consists of two subunits, a heterodimer of activation of Smt3p 1 (Aos1) and ubiquitin activating enzyme 2 (Uba2), which resembles the N- and C-terminal halves of ubiquitin E1 (Uba1), the functional domains appear to be arranged in a fashion similar to Uba1. mAU has SUMO-E1 activity, indicating that mAU can be expressed in baculovirus-insect cells and represents a suitable source of SUMO-E1, enzymatic mechanism and structure of SUMO-E1, overview
improved stability and activity compared to mutant A189T/W714C, but when incubated at 39°C, cells expressing the mutant show increased apoptotic rate ompared to wild-type. Mutant is able to monoubiquitinate histone H2A and to support growth of TS20 cells at 39°C. Compared to mutant A189T/W714C, mutation A189T significantly improves the ubiquitination-dependent disposal of HIF-1alpha
recombinant expression of His6-tagged chimeric mutant Aos1-Uba2 SUMO-E1 enzyme mAU in Spodoptera frugiperda Sf9 insect cells via baculovirus transformation, mAU has SUMO-E1 activity. Recombinant expression of GST-tagged mAU in Escherichia coli
in a mouse model of leukemia, intraperitoneal administration of inhibitor 1-(3-chloro-4-fluorophenyl)-4-[(5-nitro-2-furyl)methylene]-3,5-pyrazolidinedione, i.e. PYZD-4409, decreases tumor weight and volume compared with control without untoward toxicity
510 mg of histidine-tagged mouse ubiquitin-activating enzyme E1 can be easily obtained from a 1 l Escherichia coli culture. A low temperature during the protein induction step is critical to obtain an active enzyme
Salvat, C.; Acquaviva, C.; Scheffner, M.; Robbins, I.; Piechaczyk, M.; Jariel-Encontre, I.
Molecular characterization of the thermosensitive E1 ubiquitin-activating enzyme cell mutant A31N-ts20. Requirements upon different levels of E1 for the ubiquitination/degradation of the various protein substrates in vivo