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Literature summary for 3.4.22.69 extracted from

  • Phakthanakanok, K.; Ratanakhanokchai, K.; Kyu, K.L.; Sompornpisut, P.; Watts, A.; Pinitglang, S.
    A computational analysis of SARS cysteine proteinase-octapeptide substrate interaction: implication for structure and active site binding mechanism (2009), BMC Bioinformatics, 10 Suppl 1, S48.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.22.69

Organism

Organism UniProt Comment Textmining
Severe acute respiratory syndrome-related coronavirus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the S3 subsite of the SARS CoVMpro has a negative character. The electrostatic interactions between Glu47 and P3Lys play a key role in specific binding. These observations are very important and provide further information for structural-based drug design against SARS virus Severe acute respiratory syndrome-related coronavirus ?
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 ?
TVILQAGF + H2O
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 Severe acute respiratory syndrome-related coronavirus TVILQ + Ala-Gly-Phe
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 ?
TVKLQAGF + H2O
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 Severe acute respiratory syndrome-related coronavirus TVKLQ + Ala-Gly-Phe
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 ?
TVRLQAGF + H2O
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 Severe acute respiratory syndrome-related coronavirus TVRLQ + Ala-Gly-Phe
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 ?

Synonyms

Synonyms Comment Organism
SARS coronavirus main proteinase
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 Severe acute respiratory syndrome-related coronavirus
SARS CoVMpro
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 Severe acute respiratory syndrome-related coronavirus
severe acute respiratory syndrome coronavirus main proteinase
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 Severe acute respiratory syndrome-related coronavirus