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Literature summary extracted from

  • Bai, Y.; Hayashi, R.
    Properties of the single sulfhydryl group of carboxypeptidase Y. Effects of alkyl and aromatic mercurials on activities toward various synthetic substrates (1979), J. Biol. Chem., 254, 8473-8479.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.4.16.5 3-Phenyl-1-propanol inhibits hydrolysis of benzyloxycarbonyl-Phe-Leu, activates hydrolysis of benzyloxycarbonyl-Gly-Phe Saccharomyces cerevisiae
3.4.16.5 CH3-CH2-CH2-CH2-Hg mercurials inhibit the hydrolysis of the good substrate benzyloxycarbonyl-L-Phe-L-Leu, the inhibition is repressed by the competitive inhibitors benzyloxycarbonyl-D-Phe-D-Leu-Leu-Phe, trans-cinnamate and acetyl-D-Phe ethyl ester. Aromatic, methyl and ethyl mercurials do not cause complete inactivation with the poor substrates benzyloxycarbonyl-Gly-Phe and benzoyl-Gly-beta,L-phenyllactate. Propyl and butyl-mercurials enhance these activities Saccharomyces cerevisiae
3.4.16.5 CH3-CH2-CH2-Hg mercurials inhibit the hydrolysis of the good substrate benzyloxycarbonyl-L-Phe-L-Leu, the inhibition is repressed by the competitive inhibitors benzyloxycarbonyl-D-Phe-D-Leu-Leu-Phe, trans-cinnamate and acetyl-D-Phe ethyl ester. Aromatic, methyl and ethyl mercurials do not cause complete inactivation with the poor substrates benzyloxycarbonyl-Gly-Phe and benzoyl-Gly-beta,L-phenyllactate. Propyl and butyl-mercurials enhance these activities Saccharomyces cerevisiae

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.16.5 3-Phenyl-1-propanol inhibits hydrolysis of benzyloxycarbonyl-Phe-Leu, activates hydrolysis of benzyloxycarbonyl-Gly-Phe Saccharomyces cerevisiae
3.4.16.5 Hg2+
-
 Saccharomyces cerevisiae
3.4.16.5 p-hydroxymercuribenzene sulfonate mercurials inhibit the hydrolysis of the good substrate benzyloxycarbonyl-L-Phe-L-Leu, the inhibition is repressed by the competitive inhibitors benzyloxycarbonyl-D-Phe-D-Leu-Leu-Phe, trans-cinnamate and acetyl-D-Phe ethyl ester. Aromatic, methyl and ethyl mercurials do not cause complete inactivation with the poor substrates benzyloxycarbonyl-Gly-Phe and benzoyl-Gly-beta,L-phenyllactate. Propyl and butyl-mercurials enhance these activities Saccharomyces cerevisiae
3.4.16.5 p-hydroxymercuribenzoate mercurials inhibit the hydrolysis of the good substrate benzyloxycarbonyl-L-Phe-L-Leu, the inhibition is repressed by the competitive inhibitors benzyloxycarbonyl-D-Phe-D-Leu-Leu-Phe, trans-cinnamate and acetyl-D-Phe ethyl ester. Aromatic, methyl and ethyl mercurials do not cause complete inactivation with the poor substrates benzyloxycarbonyl-Gly-Phe and benzoyl-Gly-beta,L-phenyllactate. Propyl and butyl-mercurials enhance these activities Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.16.5 additional information
-
 additional information influence of mercurials Saccharomyces cerevisiae

Organism

EC Number Organism UniProt Comment Textmining
3.4.16.5 Saccharomyces cerevisiae
-
 baker's yeast
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.16.5 acetyl-Phe ethyl ester + H2O
-
 Saccharomyces cerevisiae ?
-
 ?
3.4.16.5 acetyl-Phe-Leu + H2O
-
 Saccharomyces cerevisiae acetyl-Phe + Leu
-
 ?
3.4.16.5 acetyl-Phe-NH2 + H2O
-
 Saccharomyces cerevisiae ?
-
 ?
3.4.16.5 benzoyl-Gly-beta-phenyllactate + H2O poor substrate Saccharomyces cerevisiae ?
-
 ?
3.4.16.5 Benzyloxycarbonyl-Gly-Phe + H2O poor substrate Saccharomyces cerevisiae Benzyloxycarbonyl-Gly + Phe
-
 ?
3.4.16.5 benzyloxycarbonyl-Phe-Gly + H2O
-
 Saccharomyces cerevisiae benzyloxycarbonyl-Phe + Gly
-
 ?
3.4.16.5 benzyloxycarbonyl-Phe-Leu + H2O
-
 Saccharomyces cerevisiae benzyloxycarbonyl-Phe + Leu
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.4.16.5 additional information
-
 additional information influence of mercurials Saccharomyces cerevisiae