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6.2.1.45: E1 ubiquitin-activating enzyme

This is an abbreviated version!
For detailed information about E1 ubiquitin-activating enzyme, go to the full flat file.

Word Map on EC 6.2.1.45

Reaction

ATP
+
ubiquitin
 +
[E1 ubiquitin-activating enzyme]-L-cysteine
=
AMP
 +
diphosphate
 +
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine

Synonyms

AtUBA1, AtUBA2, E1, E1 ubiquitin-activating enzyme, HsUba1a, non-canonical ubiquitin activating enzyme, SUMO E1, UB activating enzyme, Ub E1 activating enzyme, Ub-activating enzyme, Ub-activating ligase, Uba1, Uba1/E1, Uba1a, UBA1p, UBA2, UBA5, Uba6, UBA7, UBE1, UBE1DC1, UBE1DC1A, UBE1DC1B, UBE1L, UBE1L2, ubiquitin activating enzyme, ubiquitin activating enzyme 2, ubiquitin activating enzyme E1, ubiquitin activating enzyme E1-like, ubiquitin E1, ubiquitin protein ligase E1, Ubiquitin-activating enzyme, ubiquitin-activating enzyme (E1), ubiquitin-activating enzyme 1, ubiquitin-activating enzyme 5, ubiquitin-activating enzyme 6, ubiquitin-activating enzyme E1, ubiquitin-activating enzyme E1 domain-containing protein 1, ubiquitin-activating enzyme E1-domain containing 1, ubiquitin-activating enzyme, UBE1, ubiquitin-conjugating enzyme, ubiquitin-like modifier-activating enzyme 1, ubiquitin-like modifier-activating enzyme 5, ubiquitin-like modifier-activating enzyme 6, ubiquitin-like modifier-activating enzyme 7 isoform X2

ECTree

     6 Ligases
         6.2 Forming carbon-sulfur bonds
             6.2.1 Acid-thiol ligases
                6.2.1.45 E1 ubiquitin-activating enzyme

Inhibitors

Inhibitors on EC 6.2.1.45 - E1 ubiquitin-activating enzyme

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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(3E)-4-[(5R,8S)-5-methyl-6,9,13-trioxo-8-(propan-2-yl)-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1~2,5~]icosa-1(18),2(20),16(19)-trien-11-yl]but-3-en-1-yl octanoate
(5R,8S)-11-ethenyl-5-methyl-8-(propan-2-yl)-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1~2,5~]icosa-1(18),2(20),16(19)-triene-6,9,13-trione
(5R,8S)-5-methyl-11-[(1E)-6-oxotridec-1-en-1-yl]-8-(propan-2-yl)-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1~2,5~]icosa-1(18),2(20),16(19)-triene-6,9,13-trione
(5R,8S)-5-methyl-8-(propan-2-yl)-11-[(1E)-4-sulfanylbut-1-en-1-yl]-10-oxa-3,17-dithia-7,14,19,20-tetraazatricyclo[14.2.1.1~2,5~]icosa-1(18),2(20),16(19)-triene-6,9,13-trione
1-(3-chloro-4-fluorophenyl)-4-[(5-nitro-2-furyl)methylene]-3,5-pyrazolidinedione
4[4-(5-nitro-furan-2-ylmethylene)-3,5-dioxo-pyrazolidin-1-yl]-benzoic acid ethyl ester
5'-[[(L-cysteinylglycylglycyl)sulfamoyl]amino]-5'-deoxyadenosine
-
inhibits Uba1-S-Ub thioester formation in a dose-dependent manner. The inhibitor is highly selective for its cognate E1 enzyme and does not inhibit the corresponding non-cognate E1s
AtMUB3
the MUB3 protein of Arabidopsis thaliana strongly reduces the E2-ubiquitin formation by E1. Inhibitory effects of wild-type and mutant MUB3 proteins, overview; the MUB3 protein of Arabidopsis thaliana strongly reduces the E2-ubiquitin formation by E1. Inhibitory effects of wild-type and mutant MUB3 proteins, overview
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ginsenoside Re
-
inhibits ubiquitin-activating enzyme, from Panax ginseng roots, a traditional herbal medicine or food
ginsenoside Rg1
-
inhibit ubiquitin-activating enzyme, from Panax ginseng roots, a traditional herbal medicine or food, causes 89.2% inhibition at 0.05 mM
largazole
-
largazole and its ester and ketone analogues selectively inhibit human UBA1 enzyme and inhibit ubiquitin conjugation to cyclin-dependent kinase inhibitor p27Kip1 and TRF1 in vitro, mechanism of E1 inhibition, overview. Largazole and its derivatives specifically inhibit the adenylation step of the E1 reaction while having no effect on thioester bond formation between ubiquitin and E1. Upon incubation with E1, largazole or largazole ester reduce the amount of ubiquitin molecules that are transferred from E1 to E2 in a dose-dependent fashion. E1 inhibition appears to be specific to human E1. Largazole analogues do not significantly inhibit SUMO E1
LMO2
interaction between LMO2 and UBA6 blocks the recruitment of USE1 by UBA6 in a dose-dependent manner.. The LMO2 protein interacts with the E1 ubiquitin-activating enzyme UBA6 at the C-terminal ubiquitin fold domain (UFD), which mediates the recognition and recruitment of the E2-conjugating enzyme USE1. The LMO2-UBA6 interaction leads to the decline of the overall cellular FAT10ylation level as well as the FAT10ylation and degradation of a known FAT10 substrate p62. Interaction analysis of LMO2 with isolated UBA6 domains, LMO2 interacts with UBA6 at the ubiquitin-fold domain, overview. LMO2 co-localizes with UBA6 and USE1 primarily in the cytoplasm of epithelium-derived cells
-
PYR-41
an Uba1 inhibitor
S-[(3E)-5-hydroxy-7-({[(4R)-4-{[(3S)-2-methoxy-4-methylpent-1-en-3-yl]carbamoyl}-4-methyl[4,5-dihydro[2,4'-bi-1,3-thiazole]]-2'-yl]methyl}amino)-7-oxohept-3-en-1-yl] octanethioate
trichostatin A
-
-
[ubiquitin carrier protein Ubc4]-L-cysteine
-
-
-
additional information
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