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Literature summary extracted from

  • Papaleo, E.; Renzetti, G.
    Coupled motions during dynamics reveal a tunnel toward the active site regulated by the N-terminal alpha-helix in an acylaminoacyl peptidase (2012), J. Mol. Graph. Model., 38, 226-234.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.19.1 expression in Escherichia coli Aeropyrum pernix

Organism

EC Number Organism UniProt Comment Textmining
3.4.19.1 Aeropyrum pernix Q9YBQ2
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3.4.19.1 Aeropyrum pernix DSM 11879 Q9YBQ2
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.19.1 additional information hundreds nanosecond all-atom atomistic molecular dynamics simulations of a representative member of the acylaminoacyl peptidase subfamily (Aeropyrum pernix K1) allow to identify the presence of a tunnel which from the surrounding of the N-terminal alpha1-helix bring to the catalytic site and it is regulated by conformational changes of the N-terminal alpha-helix itself and its surroundings in the native conformational ensemble Aeropyrum pernix ?
-
 ?
3.4.19.1 additional information hundreds nanosecond all-atom atomistic molecular dynamics simulations of a representative member of the acylaminoacyl peptidase subfamily (Aeropyrum pernix K1) allow to identify the presence of a tunnel which from the surrounding of the N-terminal alpha1-helix bring to the catalytic site and it is regulated by conformational changes of the N-terminal alpha-helix itself and its surroundings in the native conformational ensemble Aeropyrum pernix DSM 11879 ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.4.19.1 AAP
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 Aeropyrum pernix