Literature summary for 3.4.11.9 extracted from

Baik, A.S.; Mironov, K.S.; Arkhipov, D.V.; Piotrovskii, M.S.; Pojidaeva, E.S.
Characterization of aminopeptidase P from the unicellular cyanobacterium Synechocystis sp. PCC6803 (2018), Dokl. Biochem. Biophys., 481, 190-194 .

Search for more literature for 3.4.11.9

Cloned(Commentary)

Cloned (Comment)	Organism
gene sll0136, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of GST-tagged enzyme in Escherichia coli strain BL21(DE3)pLysS	Synechocystis sp. PCC 6803

Inhibitors

Inhibitors	Comment	Organism	Structure
1,10-phenanthroline	complete inhibition at 5.0 mM	Synechocystis sp. PCC 6803
Ba2+	slight inhibition at 1-5 mM	Synechocystis sp. PCC 6803
bestatin	50% inhibition at 0.1 mM	Synechocystis sp. PCC 6803
Ca2+	slight inhibition at 1-5 mM	Synechocystis sp. PCC 6803
Cd2+	complete inhibition at 0.01-5.0 mM	Synechocystis sp. PCC 6803
EDTA	90% inhibition at 0.1 mM	Synechocystis sp. PCC 6803
Mg2+	slight inhibition at 1-5 mM	Synechocystis sp. PCC 6803
pepstatin A	complete inhibition at 0.1-5.0 mM	Synechocystis sp. PCC 6803
PMSF	60% inhibition at 5.0 mM	Synechocystis sp. PCC 6803
Zn2+	complete inhibition at 0.01-5.0 mM	Synechocystis sp. PCC 6803

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.00883	-	N6-(2-aminobenzoyl)-L-Lys-L-Pro-L-Pro-4-nitroanilide	recombinant enzyme, pH 7.5, 30°C	Synechocystis sp. PCC 6803

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mn2+	activates 5fold at 0.01 mM, 2.5fold at 5 mM. The active site of PepP is involved in the binding of two Mn2+ ions	Synechocystis sp. PCC 6803
additional information	structure modeling reveals that residues Thr273 and Thr383 do not directly interact with metal ions but may be important for their retention in the protein active site	Synechocystis sp. PCC 6803

Organism

Organism	UniProt	Comment	Textmining
Synechocystis sp. PCC 6803	P74468	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant GST-tagged enzyme from Escherichia coli strain BL21(DE3)pLysS by glutathione affinity chromatography, tag cleavage through enterokinase, followed by another step of glutathione affinity chromatography for tag removal	Synechocystis sp. PCC 6803

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
Gly-Pro-Hyp + H2O	-	Synechocystis sp. PCC 6803	Gly + Pro-Hyp	-	?
additional information	aminopeptidase P catalyzes the cleavage of the first amino acid residue in peptides and proteins when it is followed by the proline residue. PepP is able to hydrolyze the Xaa-Pro-bond and belongs to the family of proline-specific aminopeptidases. Substrate specificity, overview	Synechocystis sp. PCC 6803	?	-	?
N6-(2-aminobenzoyl)-L-Lys-L-Pro-L-Pro-4-nitroanilide + H2O	-	Synechocystis sp. PCC 6803	N6-(2-aminobenzoyl)-L-Lys + Pro-Pro-4-nitroanilide	-	?

Subunits

Subunits	Comment	Organism
More	three-dimensional modeling of the Synechocystis sp. PCC6803 PepP protein, overview	Synechocystis sp. PCC 6803

Synonyms

Synonyms	Comment	Organism
aminopeptidase P	-	Synechocystis sp. PCC 6803
APP	-	Synechocystis sp. PCC 6803
PEPP	-	Synechocystis sp. PCC 6803
sll0136	-	Synechocystis sp. PCC 6803

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
30	32	-	Synechocystis sp. PCC 6803

Temperature Range [°C]

Temperature Minimum [°C]	Temperature Maximum [°C]	Comment	Organism
15	55	70% of maximal activity at 15°C, 20% at 50°C, recombinant enzyme, profile overview	Synechocystis sp. PCC 6803

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.5	-	-	Synechocystis sp. PCC 6803

pH Range

pH Minimum	pH Maximum	Comment	Organism
6.5	8.5	activity range, profile overview	Synechocystis sp. PCC 6803

General Information

General Information	Comment	Organism
evolution	enzyme PepP belongs to the family of proline-specific aminopeptidases	Synechocystis sp. PCC 6803
metabolism	the genome of the unicellular cyanobacterium Synechocystis sp. PCC6803 contains 25 genes of aminopeptidases, among which only the sll0136 gene encodes a aminopeptidase P (PepP)	Synechocystis sp. PCC 6803
additional information	three-dimensional modeling of the Synechocystis sp. PCC6803 PepP protein, overview. The PepP amino acid residues Asp260, Asp271, His354, Glu385, and Glu415 are involved in the formation of the enzym's catalytic site	Synechocystis sp. PCC 6803

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)