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Literature summary for 2.3.2.27 extracted from

  • Fraser, J.; Worrall, E.; Lin, Y.; Landre, V.; Pettersson, S.; Blackburn, E.; Walkinshaw, M.; Muller, P.; Vojtesek, B.; Ball, K.; Hupp, T.
    Phosphomimetic mutation of the N-terminal lid of MDM2 enhances the polyubiquitination of p53 through stimulation of E2-ubiquitin thioester hydrolysis (2014), J. Mol. Biol., 427, 1728-1747.
No PubMed abstract available

Protein Variants

Protein Variants Comment Organism
S17D phosphomimetic mutation, stimulates MDM2-mediated polyubiquitination of p53. The stimulation is independent of p53 substrate. Mutation alters the conformation of the isolated N-terminus, it induces increased thermostability of the isolated N-terminal domain, it stimulates the allosteric interaction of MDM2 with the DNA-binding domain of p53 and it stimulates a protein-protein interaction with the E2-ubiquitin complex in the absence of substrate p53 that, in turn, increases hydrolysis of the E2-ubiquitin thioester bond Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P51668
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-ubiquitinyl-[UbcH5a]-L-cysteine + [p53]-L-lysine
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Homo sapiens [UbcH5a]-L-cysteine + N6-ubiquitinyl-[p53]-L-lysine
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?

Synonyms

Synonyms Comment Organism
E3 ubiquitin-protein ligase Mdm2
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Homo sapiens
Mdm2
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Homo sapiens