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Literature summary extracted from

  • Nishioka, M.; Tanimoto, K.; Higashi, N.; Fukada, H.; Ishikawa, K.; Taya, M.
    Alteration of metal ions improves the activity and thermostability of aminoacylase from hyperthermophilic archaeon Pyrococcus horikoshii (2008), Biotechnol. Lett., 30, 1639-1643.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.1.14
-
 Pyrococcus horikoshii

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.5.1.14 Mn2+ Zn2+ substituted by Mn2+: increased activity (substrate: N-acetyl-L-methionine) Pyrococcus horikoshii
3.5.1.14 Ni2+ Zn2+ substituted by Ni2+: increased activity (substrate: N-acetyl-L-methionine) Pyrococcus horikoshii
3.5.1.14 Zn2+
-
 Pyrococcus horikoshii

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.14 Pyrococcus horikoshii
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.1.14
-
 Pyrococcus horikoshii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.14 N-acetyl-L-methionine + H2O
-
 Pyrococcus horikoshii acetic acid + L-methionine
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.5.1.14 L-aminoacylase
-
 Pyrococcus horikoshii

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.5.1.14 90
-
 no loss of activity during 12 h (Zn2+)-enzyme, half-life time: 4 h (Mn2+)-enzyme, 12 h (Ni2+)-enzyme Pyrococcus horikoshii
3.5.1.14 100
-
 half activity after 1 h (Zn2+)-enzyme Pyrococcus horikoshii