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Literature summary extracted from

  • Ludwig, M.
    Carboxypeptidase A and other peptidases (1973), Inorg. Biochem., 1, 438-487.
No PubMed abstract available

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.4.17.1 additional information
-
Squalus acanthias
3.4.17.1 additional information substrate activation by some substrates Bos taurus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.4.17.1 analysis of enzyme-substrate complex by difference Fourier techniques, analysis of enzyme-inhibitor complexes, mechanistic model based on crystal structure Bos taurus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.17.1 1,10-phenanthroline
-
Bos taurus
3.4.17.1 1,10-phenanthroline
-
Squalus acanthias
3.4.17.1 3-Phenylpropionic acid Ki: 0.062-0.19 mM Bos taurus
3.4.17.1 3-Phenylpropionic acid
-
Squalus acanthias
3.4.17.1 Chelating agents
-
Bos taurus
3.4.17.1 cinnamate Ki: 5 mM Bos taurus
3.4.17.1 D-Phe Ki: 2 mM Bos taurus
3.4.17.1 Hydroxyquinoline sulfonate
-
Bos taurus
3.4.17.1 L-Lys-L-tyrosineamide
-
Bos taurus
3.4.17.1 L-Phe
-
Bos taurus
3.4.17.1 L-Phenyllactate Ki: 0.058 mM Bos taurus
3.4.17.1 additional information substrate inhibition by: carbobenzoxy-Glyl-L-Phe, benzoyl-Gly-Phe Bos taurus
3.4.17.1 p-iodo-beta-phenylpropionate
-
Bos taurus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.17.1 additional information
-
additional information dissociation constant of enzyme GlyTyr complex: 0.001, no Michaelis-Menten kinetics with some substrates, larger substrates tend to have smaller Km-values than smaller substrates Bos taurus
3.4.17.1 0.051 0.088 benzoyl-Gly-phenyllactate
-
Bos taurus
3.4.17.1 0.15 0.19 cinnamoyl-L-phenyllactate
-
Bos taurus
3.4.17.1 0.7
-
Gly-L-Tyr
-
Bos taurus
3.4.17.1 0.8 11 benzoyl-Gly-L-Phe
-
Bos taurus
3.4.17.1 1
-
benzoyl-Gly-Gly-L-Phe
-
Bos taurus
3.4.17.1 2 37 carbobenzoxy-Gly-L-Phe
-
Bos taurus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.17.1 Cd2+ substitution for native Zn, activates apoenzyme Bos taurus
3.4.17.1 Co2+ substitution for native Zn Bos taurus
3.4.17.1 Co2+ association constant Bos taurus
3.4.17.1 Cu2+
-
Bos taurus
3.4.17.1 Mn2+ substitution for native Zn Bos taurus
3.4.17.1 Ni2+ substitution for native Zn Bos taurus
3.4.17.1 Zn2+ required Bos taurus
3.4.17.1 Zn2+ required Squalus acanthias
3.4.17.1 Zn2+ metalloenzyme Bos taurus
3.4.17.1 Zn2+ 1 mol Zn per mol of enzyme Bos taurus
3.4.17.1 Zn2+ His-69, Glu-72 and His-196 bind Zn to carboxypeptidase Bos taurus
3.4.17.1 Zn2+ Zn ligand is His, Zn involved in both binding and catalysis Bos taurus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.17.1 additional information
-
molecular weight of trimeric procarboxypeptidase 87000, molecular weight of carboxypeptidase precursor subunit 40000-42000, slight differences in molecular weight may be caused by different activation conditions Bos taurus
3.4.17.1 35470
-
alpha form, amino acid analysis Bos taurus
3.4.17.1 40000
-
1 * 40000, SDS-PAGE Bos taurus

Organism

EC Number Organism UniProt Comment Textmining
3.4.17.1 Bos taurus
-
also two allotypic forms known
-
3.4.17.1 Bos taurus
-
overview, forms alpha, beta, gamma, and delta may result from slightly different activation conditions
-
3.4.17.1 Squalus acanthias
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
3.4.17.1 release of a C-terminal amino acid, but little or no action with -Asp, -Glu, -Arg, -Lys or -Pro mechanism Bos taurus
3.4.17.1 release of a C-terminal amino acid, but little or no action with -Asp, -Glu, -Arg, -Lys or -Pro correlations between mechanism, kinetics, and structure, intermediates and rate-determining steps Bos taurus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.17.1 pancreas
-
Squalus acanthias
-
3.4.17.1 pancreas elaborated as inactive proenzyme by acinar cells Bos taurus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.17.1 (Ala)4 + H2O
-
Bos taurus (Ala)3 + L-Ala
-
ir
3.4.17.1 benzoyl-Gly-Gly-L-Phe + H2O
-
Bos taurus benzoyl-Gly-Gly + L-Phe
-
ir
3.4.17.1 benzoyl-Gly-L-Phe + H2O
-
Bos taurus benzoyl-Gly + L-Phe
-
ir
3.4.17.1 benzoyl-Gly-phenyllactate + H2O
-
Bos taurus benzoyl-Gly-phenyllactate + ?
-
ir
3.4.17.1 carbobenzoxy-Gly-L-Phe + H2O
-
Bos taurus carbobenzoxy-Gly + L-Phe
-
ir
3.4.17.1 carbobenzoxy-Gly-L-Phe + H2O
-
Squalus acanthias carbobenzoxy-Gly + L-Phe
-
ir
3.4.17.1 cinnamoyl-L-phenyllactate + H2O
-
Bos taurus cinnamic acid + L-phenyllactate
-
ir
3.4.17.1 Gly-L-Tyr + H2O
-
Bos taurus Gly + L-Tyr
-
ir

Subunits

EC Number Subunits Comment Organism
3.4.17.1 monomer
-
Squalus acanthias
3.4.17.1 monomer 1 * 40000, SDS-PAGE Bos taurus
3.4.17.1 More
-
Squalus acanthias
3.4.17.1 More structure of enzyme and its complex with substrate, overall conformation of the protein, analysis of secondary structures, structure of active center and zinc ligand complex Bos taurus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.4.17.1 0.015
-
Gly-L-Tyr
-
Bos taurus
3.4.17.1 20
-
benzoyl-Gly-Gly-L-Phe
-
Bos taurus
3.4.17.1 76.7
-
cinnamoyl-L-phenyllactate
-
Bos taurus
3.4.17.1 91.7 200 carbobenzoxy-Gly-L-Phe
-
Bos taurus
3.4.17.1 93.3 183 benzoyl-Gly-L-Phe
-
Bos taurus
3.4.17.1 100
-
(Ala)4
-
Bos taurus
3.4.17.1 467 583 benzoyl-Gly-phenyllactate
-
Bos taurus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.17.1 7.5 8
-
Bos taurus

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.4.17.1 0.058
-
L-Phenyllactate
-
Bos taurus
3.4.17.1 2
-
D-Phe
-
Bos taurus
3.4.17.1 5
-
cinnamate
-
Bos taurus