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Literature summary for 6.2.1.45 extracted from

  • Pickart, C.M.; Kasperek, E.M.; Beal, R.; Kim, A.
    Substrate properties of site-specific mutant ubiquitin protein (G76A) reveal unexpected mechanistic features of ubiquitin-activating enzyme (E1) (1994), J. Biol. Chem., 269, 7115-7123.
    View publication on PubMed
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Organism

Organism UniProt Comment Textmining
Bos taurus
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Source Tissue

Source Tissue Comment Organism Textmining
erythrocyte
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 Bos taurus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + ubiquitin + [ubiquitin-activating protein E1]-L-cysteine
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 Bos taurus AMP + diphosphate + [ubiquitin-activating protein E1]-S-ubiquitinyl-L-cysteine
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 ?
ATP + ubiquitin mutant G76A + [ubiquitin-activating protein E1]-L-cysteine
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 Bos taurus AMP + diphosphate + [ubiquitin-activating protein E1]-S-(ubiquitin mutant G76A)yl-L-cysteine mutant ubiquitin G76A, bearing a Gly to Ala substitution at the COOH terminus is a substrate for El enzyme. Ubiquitin G76A supports PPI-ATP exchange with 500fold decrease in kcat/Km compared to wild-type ubiquitin, does not produce detectable AMP-Ub with native El, produces stoichiometric AMP-Ub with thiol-blocked El, gives a stoichiometric burst of ATP consumption with either native or thiol-blocked El, support El-ubiquitin thiol ester formation with native El, and supports several downstream reactions of the proteolytic pathway with a 20% decrease to the rate of wild type ubiquitin ?