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Literature summary for 3.5.1.14 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
Search for more literature for 3.5.1.14

Cloned(Commentary)

Cloned (Comment) Organism
-
 Pyrococcus horikoshii

Metals/Ions

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

Organism

Organism UniProt Comment Textmining
Pyrococcus horikoshii
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Pyrococcus horikoshii

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
L-aminoacylase
-
 Pyrococcus horikoshii

Temperature Stability [°C]

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