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Literature summary for 3.4.17.1 extracted from

  • Auld, D.S.; Vallee, B.L.
    Kinetics of carboxypeptidase A. II. Inhibitors of the hydrolysis of oligopeptides (1970), Biochemistry, 9, 602-609.
    View publication on PubMed
Search for more literature for 3.4.17.1

Inhibitors

Inhibitors Comment Organism Structure
3-Phenylpropionic acid noncompetitive, Ki: 0.12 mM Bos taurus
Carbobenzoxyglycine activator of dipeptide hydrolysis, inhibitor of tripeptide hydrolysis, Ki: 27 mM Bos taurus
Gly-L-Tyr Ki: 0.1 mM Bos taurus
indole acetic acid noncompetitive, Ki: 0.17 mM Bos taurus
additional information enzyme acetylation reduces activity by 97% Bos taurus
phenylacetic acid noncompetitive, Ki: 0.73 mM Bos taurus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information comparison of affinities of various substituted metalloenzymes Bos taurus

Metals/Ions

Metals/Ions Comment Organism Structure
Cd2+ efficiency of metals in decreasing order: Zn, Co, Ni, Mn, Cd Bos taurus
Co2+ efficiency of metals in decreasing order: Zn, Co, Ni, Mn, Cd Bos taurus
Mn2+ efficiency of metals in decreasing order: Zn, Co, Ni, Mn, Cd Bos taurus
Ni2+ efficiency of metals in decreasing order: Zn, Co, Ni, Mn, Cd Bos taurus
Zn2+
-
 Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
pancreas
-
 Bos taurus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
benzoyl-Gly-Gly-L-Phe + H2O
-
 Bos taurus benzoyl-Gly-Gly + L-Phe
-
 ir
carbobenzoxy-Gly-L-Phe + H2O
-
 Bos taurus carbobenzoxy-Gly + L-Phe
-
 ir

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.1
-
 Gly-L-Tyr
-
 Bos taurus