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Literature summary for 3.4.17.19 extracted from

  • Lee, S.H.; Taguchi, H.; Yoshimura, E.; Minagawa, E.; Kaminogawa, S.; Ohta, T.; Matsuzawa, H.
    Carboxypeptidase Taq, a thermostable zinc enzyme, from Thermus aquaticus YT-1: molecular cloning, sequencing, and expression of the encoding gene in Escherichia coli (1994), Biosci. Biotechnol. Biochem., 58, 1490-1495.
    View publication on PubMed
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Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Thermus aquaticus

Inhibitors

Inhibitors Comment Organism Structure
Metal chelating reagents
-
 Thermus aquaticus

Metals/Ions

Metals/Ions Comment Organism Structure
Zinc one enzyme molecule contains one tightly bound zinc ion Thermus aquaticus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
56210
-
 Thermus aquaticus, calculation from nucleotide sequence Thermus aquaticus

Organism

Organism UniProt Comment Textmining
Thermus aquaticus
-
 YT-1
-
Thermus aquaticus YT-1
-
 YT-1
-

Purification (Commentary)

Purification (Comment) Organism
-
 Thermus aquaticus

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
 Thermus aquaticus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Carbobenzoxy-Phe-Tyr + H2O
-
 Thermus aquaticus Carbobenzoxy-Phe + Tyr
-
 ?
Carbobenzoxy-Phe-Tyr + H2O
-
 Thermus aquaticus YT-1 Carbobenzoxy-Phe + Tyr
-
 ?