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Literature summary for 3.4.22.69 extracted from

  • Tan, J.; Verschueren, K.H.; Anand, K.; Shen, J.; Yang, M.; Xu, Y.; Rao, Z.; Bigalke, J.; Heisen, B.; Mesters, J.R.; Chen, K.; Shen, X.; Jiang, H.; Hilgenfeld, R.
    pH-dependent conformational flexibility of the SARS-CoV main proteinase (M(pro)) dimer: molecular dynamics simulations and multiple X-ray structure analyses (2005), J. Mol. Biol., 354, 25-40.
    View publication on PubMed
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Crystallization (Commentary)

Crystallization (Comment) Organism
X-ray, resolution of 2.0 A for tetragonal crystals, 2.14 A for monoclinic crystals and 2.8 A for orthorhombic crystals, pH-dependent change of structure Severe acute respiratory syndrome-related coronavirus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
61.9
-
 SWTSAVLQSGFRKWA HPLC-based cleavage assay, measurement of fluorescence emission at 353 nm Severe acute respiratory syndrome-related coronavirus

Organism

Organism UniProt Comment Textmining
Severe acute respiratory syndrome-related coronavirus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
SWTSAVLQSGFRKWA + H2O
-
 Severe acute respiratory syndrome-related coronavirus ?
-
 ?

Synonyms

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
-
 Severe acute respiratory syndrome-related coronavirus