Activating Compound | Comment | Organism | Structure |
---|---|---|---|
additional information | - |
Squalus acanthias | |
additional information | substrate activation by some substrates | Bos taurus |
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 | 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 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 | 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 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 | 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 | 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 | Comment | Organism | Textmining |
---|---|---|---|
pancreas | - |
Squalus acanthias | - |
pancreas | elaborated as inactive proenzyme by acinar cells | Bos taurus | - |
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 | 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 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 Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | 8 | - |
Bos taurus |
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 |