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Literature summary for 3.4.17.1 extracted from

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

Activating Compound

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

Crystallization (Commentary)

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

Inhibitors

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

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
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
0.051 0.088 benzoyl-Gly-phenyllactate
-
Bos taurus
0.15 0.19 cinnamoyl-L-phenyllactate
-
Bos taurus
0.7
-
Gly-L-Tyr
-
Bos taurus
0.8 11 benzoyl-Gly-L-Phe
-
Bos taurus
1
-
benzoyl-Gly-Gly-L-Phe
-
Bos taurus
2 37 carbobenzoxy-Gly-L-Phe
-
Bos taurus

Metals/Ions

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

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
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
35470
-
alpha form, amino acid analysis Bos taurus
40000
-
1 * 40000, SDS-PAGE Bos taurus

Organism

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

Reaction

Reaction Comment Organism Reaction ID
release of a C-terminal amino acid, but little or no action with -Asp, -Glu, -Arg, -Lys or -Pro mechanism Bos taurus
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

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

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
monomer
-
Squalus acanthias
monomer 1 * 40000, SDS-PAGE Bos taurus
More
-
Squalus acanthias
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]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5 8
-
Bos taurus

Ki Value [mM]

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