Any feedback?
Literature summary for 6.2.1.45 extracted from
- Structural and functional characterisation of the domains of ubiquitin-activating enzyme (E1) of Saccharomyces cerevisiae (2020), Cell Biochem. Biophys., 78, 309-319 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene UBA1, recombinant expression of isolated and His-tagged enzyme domains FCCH, 4HB, SCCH and UFD in Escherichia coli strain BL21(DE3) | Saccharomyces cerevisiae |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | reduced survival rates of Saccharomyces cerevisiae strain MHY501 expressing the domains of ubiquitin-activating enzyme E1 under heat stress with or without inducer CuSO4, overview. Under antibiotic and heat stresses expression of the domains SCCH and UFD prove to be detrimental to cell survival | Saccharomyces cerevisiae |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | individual E1 enzyme domains like SCCH show the potential to interfere with cellular processes by acting as competitive inhibitors in protein-protein interactions involving complete proteins | Saccharomyces cerevisiae |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Saccharomyces cerevisiae |  |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine | Saccharomyces cerevisiae | - |
AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine | - |
? | |
| ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine | Saccharomyces cerevisiae ATCC 204508 | - |
AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharomyces cerevisiae | P22515 | - |
- |
| Saccharomyces cerevisiae ATCC 204508 | P22515 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged enzyme domains FCCH, 4HB, SCCH and UFD from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, incase of domain UFD purification containing 6 M urea, followed by dialysis, and ultrafiltration | Saccharomyces cerevisiae |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine | - |
Saccharomyces cerevisiae | AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine | - |
? | |
| ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine | - |
Saccharomyces cerevisiae ATCC 204508 | AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | the structure of E1 is organised into six domains namely, inactive adenylation domain (IAD), first catalytic cysteine half-domain (FCCH), four-helix bundles (4HB), active adenylation domain (AAD), second catalytic cysteine half-domain (SCCH) and Ub fold domain (UFD). E1 displays complex architecture due to the discontinuous and interspersed organisation of its six domains. The domains carrying the catalytic cysteine exist as two parts namely, FCCH and SCCH, which are found inserted into each of the adenylation domains. SCCH domain consisting of catalytic cysteine forms a thioester bond with ubiquitin. On the other hand FCCH, which associates with IAD is non-functional. 4HB domain present immediately after the FCCH, represents the second insertion in the IAD. UFD present in the C-terminus of E1 has a role in the recruitment of specific E2s to the ubiquitination pathway. Secondary structure analysis of enzyme domains, overview | Saccharomyces cerevisiae |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Uba1 | - |
Saccharomyces cerevisiae |
| Uba1/E1 | - |
Saccharomyces cerevisiae |
| Ubiquitin-activating enzyme | - |
Saccharomyces cerevisiae |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | - |
Saccharomyces cerevisiae | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | yeast Ub-activating enzyme E1 is a modular protein, evolved from small prokaryotic proteins, which had specific functions, and in E1 enzyme they form domains that work together as part of a big enzyme | Saccharomyces cerevisiae |
| malfunction | a defect in the UBA1 gene results in detrimental effects on cell cycle progression, and deletion of the UBA1 gene is lethal to the organism | Saccharomyces cerevisiae |
| metabolism | ubiquitin-activating enzyme (E1) is the first enzyme of the ubiquitination pathway and is required to activate ubiquitin | Saccharomyces cerevisiae |
| physiological function | ubiquitin-activating enzyme (E1) is the first enzyme of the ubiquitination pathway and is required to activate ubiquitin. E1 along with other enzymes plays a role in the regulation of cell cycle proteins like histone H2A and p53, which are essential for cell cycling | Saccharomyces cerevisiae |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
