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Literature summary for 3.4.11.9 extracted from

  • Peng, C.T.; Liu, L.; Li, C.C.; He, L.H.; Li, T.; Shen, Y.L.; Gao, C.; Wang, N.Y.; Xia, Y.; Zhu, Y.B.; Song, Y.J.; Lei, Q.; Yu, L.T.; Bao, R.
    Structure-function relationship of aminopeptidase P from Pseudomonas aeruginosa (2017), Front. Microbiol., 8, 2385 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.11.9

Cloned(Commentary)

Cloned (Comment) Organism
gene pepP, sequence comparisons, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Pseudomonas aeruginosa

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant enzyme, X-ray diffraction structure determination and analysis at 1.78-1.85 A resolution Pseudomonas aeruginosa

Inhibitors

Inhibitors Comment Organism Structure
EDTA
-
 Pseudomonas aeruginosa
Mn2+ activates at up to 5 mM, a trimetal manganese cluster is observed at the active site involving residues Asp260, Asp271, Glu384, Glu408, and His354, elucidating the binding structure and mechanism of inhibition by metal ions. Inhibitory at 8-15 mM. There is a Mn2+ ion concentration-dependent activity regulation pattern Pseudomonas aeruginosa
Ni2+
-
 Pseudomonas aeruginosa
Zn2+ the Zn2+ ion has high affinity for APPro and inhibits the hydrolysis reaction by occupying a third metal binding site Pseudomonas aeruginosa

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ activates slightly Pseudomonas aeruginosa
Mg2+ activates slightly Pseudomonas aeruginosa
Mn2+ activates at up to 5 mM, a trimetal manganese cluster is observed at the active site involving residues Asp260, Asp271, Glu384, Glu408, and His354, elucidating the binding structure and mechanism of inhibition by metal ions. Inhibitory at 8-15 mM. There is a Mn2+ ion concentration-dependent activity regulation pattern Pseudomonas aeruginosa
additional information the enzyme activity is dependent on metal ions and influenced by different metal ions. This enzyme's pita-bread fold is commonly found in N-terminal amido-, imido-, and amidino-scissile bond-cleaving enzymes, and serves as a structural basis for the metal-dependent catalysis. Addition of Mn2+ significantly restores the Pa-PepP activity of the apoenzyme, while the limited enhancement of activity is observed upon addition of Ca2+ or Mg2+ Pseudomonas aeruginosa

Organism

Organism UniProt Comment Textmining
Pseudomonas aeruginosa A0A069Q0X9
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain strain BL21(DE3) Pseudomonas aeruginosa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information modeling of the Val-Pro-Leu bound Pa-PepP complex by superposing Pa-PepP structure with the substrate-bound Escherichia coli PepP structure (PDB ID 2BN7) Pseudomonas aeruginosa ?
-
 ?

Subunits

Subunits Comment Organism
More the recombinant enzyme exists as a monomer in solution, tetrameric oligomerization is observed in crystal packing. The monomer structure displays a two-domain organization where the N-domain (1-175) is composed of a mainly parallel beta-sheet core (B1-B6) flanked by seven alpha helices (A-G). In contrast, the catalytic C-domain (176-444) adopts a conserved pita-bread fold wth six beta sheets (B7-B12) in antiparallel configuration. This pita-bread fold is commonly found in N-terminal amido-, imido-, and amidino-scissile bond-cleaving enzymes, and serves as a structural basis for the metal-dependent catalysis Pseudomonas aeruginosa
tetramer the monomers are arranged as a dimer with an extended loop contributing to the active site of the adjacent subunit and an average interface area of approximately 2050.9 A2 per subunit. The dimer-of-dimers results in an 815.6 A2 buried area per subunit Pseudomonas aeruginosa

Synonyms

Synonyms Comment Organism
aminopeptidase P
-
 Pseudomonas aeruginosa
APPro
-
 Pseudomonas aeruginosa
Pa-PepP
-
 Pseudomonas aeruginosa
PEPP
-
 Pseudomonas aeruginosa
X-prolyl peptidase
-
 Pseudomonas aeruginosa

General Information

General Information Comment Organism
evolution pepP encodes an enzyme belonging to the aminopeptidases P (APPro) family, a type of metalloprotease that catalyzes the removal of the N-terminal residue from a polypeptide that has proline as the second residue. Enzyme PepP is highly conserved in all Pseudomonas aeruginosa genomes sequenced to date and has high genetic similarity with enzymes from other Pseudomonas species (82.4%-100% identity) Pseudomonas aeruginosa
additional information analysis of structure-function relationship of aminopeptidase P, structure modelling, overview. A loop extending from the active site is important for specific large-substrate binding, and this non-conserved surface loop is also critical for Pseudomonas aeruginosa virulence. The extended substrate binding site is identified to be responsible for virulence-related protein recognition. Pseudomonas aeruginosa