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Literature summary for 3.5.1.119 extracted from

  • Laederach, J.; Cui, H.; Weber-Ban, E.
    Pupylated proteins are subject to broad proteasomal degradation specificity and differential depupylation (2019), PLoS ONE, 14, e0215439 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.5.1.119

Organism

Organism UniProt Comment Textmining
Mycolicibacterium smegmatis A0QZ49
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Mycolicibacterium smegmatis ATCC 700084 A0QZ49
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information steric hindrance in positioning the isopeptide bond in the active site of Dop might be responsible for the observed differences in depupylation rather than differences in the overall affinity of pupylated substrate for Dop Mycolicibacterium smegmatis ?
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 ?
additional information steric hindrance in positioning the isopeptide bond in the active site of Dop might be responsible for the observed differences in depupylation rather than differences in the overall affinity of pupylated substrate for Dop Mycolicibacterium smegmatis ATCC 700084 ?
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 ?

Synonyms

Synonyms Comment Organism
deamidase/depupylase
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 Mycolicibacterium smegmatis
depupylase Dop
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 Mycolicibacterium smegmatis
Dop
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 Mycolicibacterium smegmatis