Crystallization (Comment) | Organism |
---|---|
mutants H243A, D260A, D271A, H350A, H354A, H361A, E383A | Escherichia coli |
Protein Variants | Comment | Organism |
---|---|---|
D260A | no enzymic activity | Escherichia coli |
D260A | MnA is bound at the active site, but the MnB site is empty. Loss of catalytic activity | Escherichia coli |
D271A | no enzymic activity | Escherichia coli |
D271A | no atoms of Mn(II) are bound at the active site. Loss of catalytic activity | Escherichia coli |
E383A | no enzymic activity | Escherichia coli |
E383A | both Mn-(II) atoms are present in the active site, but the bridging solvent molecule is located significantly farther from the metals than in wild-type. Loss of catalytic activity | Escherichia coli |
H243A | no enzymic activity | Escherichia coli |
H243A | loss of catalytic acitivity. H243 stabilizes substrate binding | Escherichia coli |
H350A | reduced enzymic activity | Escherichia coli |
H350A | loss of catalytic activity. H350 forms part of a hydrophobic binding pocket that gives the enzym its proline specificity | Escherichia coli |
H354A | no enzymic activity | Escherichia coli |
H354A | MnB is present at the active site at less than full occupancy, and a water molecule occupies the MnA site. Loss of catalytic activity | Escherichia coli |
H361A | no enzymic activity | Escherichia coli |
H361A | loss of catalytic activity | Escherichia coli |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
L-Ala-(N-methyl)L-Ala-L-Ala | competitive | Escherichia coli | |
L-Ala-L-Ala-L-Ala | competitive | Escherichia coli | |
L-Ala-L-Pro-L-Ala | competitive; competitive, 50% inhibition at 0.22 mM | Escherichia coli | |
additional information | not inhibitory: L-Ala-(N-methyl)-L-Ala-L-Ala, L-Ala-L-Ala-L-Ala | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.087 | - |
Abz-L-Lys-L-Pro-L-Pro-4-nitroanilide | wild-type, pH 8.1, 37°C | Escherichia coli | |
0.087 | - |
2-aminobenzoyl-L-Lys-L-Pro-L-Pro-4-nitroanilide | wild-type, pH 8.1, 37°C | Escherichia coli | |
0.14 | - |
Abz-L-Lys-L-Pro-L-Pro-4-nitroanilide | mutant H350, pH 8.1, 37°C | Escherichia coli | |
0.14 | - |
2-aminobenzoyl-L-Lys-L-Pro-L-Pro-4-nitroanilide | mutant H350A, pH 8.1, 37°C | Escherichia coli | |
0.77 | - |
L-Ala-L-Pro-L-Ala | wild-type, pH 8.1, 37°C | Escherichia coli |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mn2+ | 2 mol of Mn2+ ions per mol of enzyme | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P15034 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide | H243 stabilizes substrate binding, H361 stabilizes substrate binding and the gem-diol catalytic intermediate. H350 forms part of a hydrophobic binding pocket that gives the enzyme its proline specificity | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2-aminobenzoyl-L-Lys-L-Pro-L-Pro-4-nitroanilide + H2O | - |
Escherichia coli | ? | - |
? | |
Abz-L-Lys-L-Pro-L-Pro-4-nitroanilide + H2O | - |
Escherichia coli | Abz-L-Lys + L-Pro-L-Pro-4-nitroanilide | - |
? | |
L-Ala-L-Pro-L-Ala | - |
Escherichia coli | L-Ala + L-Pro-L-Ala | - |
? | |
L-Ala-L-Pro-L-Ala + H2O | - |
Escherichia coli | L-Ala + L-Pro-L-Ala | - |
? | |
additional information | peptides in which L-Pro is replaced by N-methyl-L-Ala or L-Ala are extremely poor substrates | Escherichia coli | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
APPro | - |
Escherichia coli |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.77 | - |
L-Ala-L-Pro-L-Ala | wild-type, pH 8.1, 37°C | Escherichia coli | |
7.3 | - |
Abz-L-Lys-L-Pro-L-Pro-4-nitroanilide | mutant H350, pH 8.1, 37°C | Escherichia coli | |
95 | - |
Abz-L-Lys-L-Pro-L-Pro-4-nitroanilide | wild-type, pH 8.1, 37°C | Escherichia coli |
IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|
0.22 | - |
wild-type, pH 8.1, 37°C | Escherichia coli | L-Ala-L-Pro-L-Ala |