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Literature summary for 3.4.11.9 extracted from

  • Graham, S.C.; Lilley, P.E.; Lee, M.; Schaeffer, P.M.; Kralicek, A.V.; Dixon, N.E.; Guss, J.M.
    Kinetic and crystallographic analysis of mutant Escherichia coli aminopeptidase P: insights into substrate recognition and the mechanism of catalysis (2006), Biochemistry, 45, 964-975.
    View publication on PubMed
Search for more literature for 3.4.11.9

Crystallization (Commentary)

Crystallization (Comment) Organism
mutants H243A, D260A, D271A, H350A, H354A, H361A, E383A Escherichia coli

Protein Variants

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

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 [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

Metals/Ions Comment Organism Structure
Mn2+ 2 mol of Mn2+ ions per mol of enzyme Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P15034
-
-

Reaction

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
a

Substrates and Products (Substrate)

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

Synonyms Comment Organism
APPro
-
 Escherichia coli

Turnover Number [1/s]

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 IC50 Value Maximum Comment Organism Inhibitor Structure
0.22
-
 wild-type, pH 8.1, 37°C Escherichia coli L-Ala-L-Pro-L-Ala