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Literature summary for 3.4.24.27 extracted from

  • Chura-Chambi, R.M.; Fraga, T.R.; da Silva, L.B.; Yamamoto, B.B.; Isaac, L.; Barbosa, A.S.; Morganti, L.
    Leptospira interrogans thermolysin refolded at high pressure and alkaline pH displays proteolytic activity against complement C3 (2018), Biotechnol. Rep., 19, e00266 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
an efficient method of production of enzymatically active thermolysin by refolding the protein expressed as inclusion bodies in Escherichia coli. Association of high pressure and alkaline pH is very efficient for solubilization Leptospira interrogans serovar Copenhageni

Organism

Organism UniProt Comment Textmining
Leptospira interrogans serovar Copenhageni Q72M68
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Leptospira interrogans serovar Copenhageni Fiocruz L1-130 Q72M68
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Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification thermolysin encoded by LIC13322 has a signal peptide for secretion, a fungalin/thermolysin propeptide (FTP) domain, a propeptide (PepSY) domain, and a catalytic domain M4 that includes peptidase_M4 and peptidase_M4_C Leptospira interrogans serovar Copenhageni

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
complement component C3 + H2O proteolytic activity of thermolysin against C3 is time and dose-dependent Leptospira interrogans serovar Copenhageni ?
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complement component C3 + H2O proteolytic activity of thermolysin against C3 is time and dose-dependent Leptospira interrogans serovar Copenhageni Fiocruz L1-130 ?
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?

Synonyms

Synonyms Comment Organism
LIC13322
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Leptospira interrogans serovar Copenhageni