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Literature summary extracted from

  • Prabha, C.
    Structural and functional characterisation of the domains of ubiquitin-activating enzyme (E1) of Saccharomyces cerevisiae (2020), Cell Biochem. Biophys., 78, 309-319 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.2.1.45 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

EC Number Protein Variants Comment Organism
6.2.1.45 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

EC Number Inhibitors Comment Organism Structure
6.2.1.45 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

EC Number Metals/Ions Comment Organism Structure
6.2.1.45 Mg2+ required Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.2.1.45 ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine Saccharomyces cerevisiae
-
AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine
-
?
6.2.1.45 ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine Saccharomyces cerevisiae ATCC 204508
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AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine
-
?

Organism

EC Number Organism UniProt Comment Textmining
6.2.1.45 Saccharomyces cerevisiae P22515
-
-
6.2.1.45 Saccharomyces cerevisiae ATCC 204508 P22515
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.2.1.45 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)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.2.1.45 ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine
-
Saccharomyces cerevisiae AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine
-
?
6.2.1.45 ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine
-
Saccharomyces cerevisiae ATCC 204508 AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine
-
?

Subunits

EC Number Subunits Comment Organism
6.2.1.45 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

EC Number Synonyms Comment Organism
6.2.1.45 Uba1
-
Saccharomyces cerevisiae
6.2.1.45 Uba1/E1
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Saccharomyces cerevisiae
6.2.1.45 Ubiquitin-activating enzyme
-
Saccharomyces cerevisiae

Cofactor

EC Number Cofactor Comment Organism Structure
6.2.1.45 ATP
-
Saccharomyces cerevisiae

General Information

EC Number General Information Comment Organism
6.2.1.45 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
6.2.1.45 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
6.2.1.45 metabolism ubiquitin-activating enzyme (E1) is the first enzyme of the ubiquitination pathway and is required to activate ubiquitin Saccharomyces cerevisiae
6.2.1.45 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