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Literature summary for 3.4.21.62 extracted from

  • Tiberti, M.; Papaleo, E.
    Dynamic properties of extremophilic subtilisin-like serine-proteases (2011), J. Struct. Biol., 174, 69-83.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
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Vibrio sp.
a comparative study of psychrophilic, mesophilic and thermophilic subtilisin-like serine proteases by all-atom molecular dynamics simulations is performed. The thermophilic subtilisin presents a high affinity calcium binding site which is not structurally conserved in the mesophilic and psychrophilic counterparts, which at the same position show a stable salt bridge network and no stabilizing intra-molecular interactions, respectively Thermoactinomyces vulgaris

Organism

Organism UniProt Comment Textmining
Thermoactinomyces vulgaris
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Vibrio sp.
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Synonyms

Synonyms Comment Organism
psychrophilic subtilisin-like protease
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Vibrio sp.
thermophilic thermitase
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Thermoactinomyces vulgaris