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Literature summary for 3.4.16.5 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

Activating Compound Comment Organism Structure
3-Phenyl-1-propanol inhibits hydrolysis of benzyloxycarbonyl-Phe-Leu, activates hydrolysis of benzyloxycarbonyl-Gly-Phe Saccharomyces cerevisiae
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
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

Inhibitors Comment Organism Structure
3-Phenyl-1-propanol inhibits hydrolysis of benzyloxycarbonyl-Phe-Leu, activates hydrolysis of benzyloxycarbonyl-Gly-Phe Saccharomyces cerevisiae
Hg2+
-
Saccharomyces cerevisiae
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
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]

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

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
baker's yeast
-

Substrates and Products (Substrate)

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

Turnover Number [1/s]

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