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Literature summary extracted from

  • Huzil, J.T.; Pannu, R.; Ptak, C.; Garen, G.; Ellison, M.J.
    Direct catalysis of lysine 48-linked polyubiquitin chains by the ubiquitin-activating enzyme (2007), J. Biol. Chem., 282, 37454-37460.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.2.1.45 His6-tagged E1 expressed and purified in Saccharomyces cerevisiae MHY-501 cells Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
6.2.1.45 additional information mutagenesis of key residues of E1 reveals that its conserved catalytic cysteine residue is essential for the formation of these poyubiquitin chains. Inactivation of the ubiquitin-conjugating enzyme E2 has no effect on the ability of E1 to catalyze ubiquitin chain formation, suggesting E1 is not only responsible for the activaton of ubiquitin but also for the direct extension of the lysine 48-linked polyubiquitin chain by the direct transfer of the ubiquitin-thiolester from the active site of E1 to the terminal Lys48 of the growing chain Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.2.1.45 additional information Escherichia coli a lysine 48-linked polyubiquitin chain, assembled upon an internal lysine residue of a substrate protein, becomes the principle signal for recognition and target degradation by the 26S proteasome. E1 is not only essential for the initial ATP-dependent activation of ubiquitin in the ubiquitin degradtion pathway, but also capable of the catalytic extension of the polyubiquitin chain on a mono-ubiquitinated substrate ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.2.1.45 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.2.1.45 His6-tagged E1 expressed and purified in Saccharomyces cerevisiae MHY-501 cells Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.2.1.45 ATP + ubiquitin + [ubiquitin-activating protein E1]-L-cysteine a carboxylgroup is first activated as an adenylate followed by its direct transfer to an autonomous molecular moiety in a single enzymatic step Escherichia coli AMP + diphosphate + [ubiquitin-activating protein E1]-S-ubiquitinyl-L-cysteine
-
 ?
6.2.1.45 additional information a lysine 48-linked polyubiquitin chain, assembled upon an internal lysine residue of a substrate protein, becomes the principle signal for recognition and target degradation by the 26S proteasome. E1 is not only essential for the initial ATP-dependent activation of ubiquitin in the ubiquitin degradtion pathway, but also capable of the catalytic extension of the polyubiquitin chain on a mono-ubiquitinated substrate Escherichia coli ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
6.2.1.45 ubiquitin-activating enzyme E1
-
 Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
6.2.1.45 30
-
 assay at Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.2.1.45 7.5
-
 assay at Escherichia coli

General Information

EC Number General Information Comment Organism
6.2.1.45 physiological function a lysine 48-linked polyubiquitin chain, assembled upon an internal lysine residue of a substrate protein, becomes the principle signal for recognition and target degradation by the 26S proteasome. E1 is not only essential for the initial ATP-dependent activation of ubiquitin in the ubiquitin degradtion pathway, but also capable of the catalytic extension of the polyubiquitin chain on a mono-ubiquitinated substrate Escherichia coli