BRENDA - Enzyme Database
show all sequences of 3.4.11.9

Structure and substrate fingerprint of aminopeptidase P from Plasmodium falciparum

Drinkwater, N.; Sivaraman, K.K.; Bamert, R.S.; Rut, W.; Mohamed, K.; Vinh, N.B.; Scammells, P.J.; Drag, M.; McGowan, S.; Biochem. J. 473, 3189-3204 (2016)

Data extracted from this reference:

Application
Application
Commentary
Organism
drug development
the enzyme PfAPP might be a potential target for an antimalarial therapeutic strategy
Plasmodium falciparum
Cloned(Commentary)
Cloned (Commentary)
Organism
recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
Plasmodium falciparum
Crystallization (Commentary)
Crystallization (Commentary)
Organism
purified recombinant enzyme PfAPP both unliganded and in complex with inhibitor apstatin, hanging drop vapor diffusion method, mixing of 2:1 vl/v ratio of 6 mg/ml protein solution with reservoir containing 40-50% 2-methyl-2,4-pentanediol, and 0.1 M sodium cacodylate, pH 5.6-6.2, 3-7 days, X-ray diffraction structure determination and analysis at 2.30-2.35 A resolution. Crystals of the apstatin:PfAPP complex are obtained by soaking unliganded crystals in mother liquor supplemented with 2 mM apstatin for 1 h. For the unliganded PfAPP structure, the molecular replacement search model is prepared from the structure of human APP1 (PDB ID 3CTZ)
Plasmodium falciparum
Inhibitors
Inhibitors
Commentary
Organism
Structure
apstatin
a APP inhibitor
Plasmodium falciparum
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mn2+
the active site is internally located at the junction of the three domains and shows a di-metal coordination consistent with the presence of two catalytic manganese ions
Plasmodium falciparum
Organism
Organism
UniProt
Commentary
Textmining
Plasmodium falciparum
-
-
-
Purification (Commentary)
Purification (Commentary)
Organism
recombinant C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
Plasmodium falciparum
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
1480
-
purified recombinant enzyme, pH 8.0, 37°C
Plasmodium falciparum
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
FPHFD + H2O
a hemoglobin peptide
752716
Plasmodium falciparum
L-Phe + PHFD
-
-
-
?
Gly-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
-
752716
Plasmodium falciparum
Gly + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
?
L-Ala-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
-
752716
Plasmodium falciparum
L-Ala + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
?
L-Arg-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
-
752716
Plasmodium falciparum
L-Arg + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
?
L-Asn-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
-
752716
Plasmodium falciparum
L-ASn + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
?
L-Asp-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
low activity
752716
Plasmodium falciparum
L-Asp + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
?
L-Gln-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
-
752716
Plasmodium falciparum
L-Gln + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
?
L-Glu-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
-
752716
Plasmodium falciparum
L-Glu + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
?
L-His-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
-
752716
Plasmodium falciparum
L-His + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
?
L-Ile-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
-
752716
Plasmodium falciparum
L-Ile + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
?
L-Leu 7-amido-4-carbamoylmethylcoumarin + H2O
-
752716
Plasmodium falciparum
L-Leu + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
?
L-Lys-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
-
752716
Plasmodium falciparum
L-Lys + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
?
L-Met-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
-
752716
Plasmodium falciparum
L-Met + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
?
L-Nle-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
-
752716
Plasmodium falciparum
L-Nle + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
?
L-Phe-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
-
752716
Plasmodium falciparum
L-Phe + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
?
L-Pro-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
-
752716
Plasmodium falciparum
L-Pro + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
?
L-Ser-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
-
752716
Plasmodium falciparum
L-Ser + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
?
L-Thr-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
-
752716
Plasmodium falciparum
L-Thr + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
?
L-Trp-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
best substrate
752716
Plasmodium falciparum
L-Trp + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
?
L-Tyr-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
-
752716
Plasmodium falciparum
L-Tyr + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
?
L-Val-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
-
752716
Plasmodium falciparum
L-Val + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
?
additional information
substrate specificity, overview. Design and synthesis of a library composed of 20 fluorogenic substrates, which is used to determine the substrate fingerprint of mature PfAPP (PfAPP, residues 121-777). The enzyme from Plasmodium falciparum can catalyze the removal of any residue immediately prior to a proline. The coupled assay uses a prolyl iminopeptidase (EC 3.4.11.5) to release the free 7-amino-4-carbamoylmethylcoumarin for fluorogenic detection
752716
Plasmodium falciparum
?
-
-
-
?
RPPGFSPFR + H2O
i.e. bradykinin
752716
Plasmodium falciparum
L-Arg + PPGFSPFR
-
-
-
?
YPWTQ + H2O
a hemoglobin peptide
752716
Plasmodium falciparum
L-Tyr + PWTQ
-
-
-
?
Subunits
Subunits
Commentary
Organism
homodimer
the enzyme structure shows a homodimer associated by an extensive interface between the catalytic domains (domain III) of both monomers. The active site is internally located at the junction of the three domains and shows a di-metal coordination consistent with the presence of two catalytic manganese ions
Plasmodium falciparum
Synonyms
Synonyms
Commentary
Organism
aminopeptidase P
-
Plasmodium falciparum
PfAPP
-
Plasmodium falciparum
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Plasmodium falciparum
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Plasmodium falciparum
Application (protein specific)
Application
Commentary
Organism
drug development
the enzyme PfAPP might be a potential target for an antimalarial therapeutic strategy
Plasmodium falciparum
Cloned(Commentary) (protein specific)
Commentary
Organism
recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
Plasmodium falciparum
Crystallization (Commentary) (protein specific)
Crystallization
Organism
purified recombinant enzyme PfAPP both unliganded and in complex with inhibitor apstatin, hanging drop vapor diffusion method, mixing of 2:1 vl/v ratio of 6 mg/ml protein solution with reservoir containing 40-50% 2-methyl-2,4-pentanediol, and 0.1 M sodium cacodylate, pH 5.6-6.2, 3-7 days, X-ray diffraction structure determination and analysis at 2.30-2.35 A resolution. Crystals of the apstatin:PfAPP complex are obtained by soaking unliganded crystals in mother liquor supplemented with 2 mM apstatin for 1 h. For the unliganded PfAPP structure, the molecular replacement search model is prepared from the structure of human APP1 (PDB ID 3CTZ)
Plasmodium falciparum
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
apstatin
a APP inhibitor
Plasmodium falciparum
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mn2+
the active site is internally located at the junction of the three domains and shows a di-metal coordination consistent with the presence of two catalytic manganese ions
Plasmodium falciparum
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
Plasmodium falciparum
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
1480
-
purified recombinant enzyme, pH 8.0, 37°C
Plasmodium falciparum
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
FPHFD + H2O
a hemoglobin peptide
752716
Plasmodium falciparum
L-Phe + PHFD
-
-
-
?
Gly-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
-
752716
Plasmodium falciparum
Gly + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
?
L-Ala-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
-
752716
Plasmodium falciparum
L-Ala + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
?
L-Arg-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
-
752716
Plasmodium falciparum
L-Arg + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
?
L-Asn-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
-
752716
Plasmodium falciparum
L-ASn + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
?
L-Asp-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
low activity
752716
Plasmodium falciparum
L-Asp + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
?
L-Gln-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
-
752716
Plasmodium falciparum
L-Gln + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
?
L-Glu-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
-
752716
Plasmodium falciparum
L-Glu + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
?
L-His-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
-
752716
Plasmodium falciparum
L-His + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
?
L-Ile-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
-
752716
Plasmodium falciparum
L-Ile + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
?
L-Leu 7-amido-4-carbamoylmethylcoumarin + H2O
-
752716
Plasmodium falciparum
L-Leu + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
?
L-Lys-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
-
752716
Plasmodium falciparum
L-Lys + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
?
L-Met-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
-
752716
Plasmodium falciparum
L-Met + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
?
L-Nle-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
-
752716
Plasmodium falciparum
L-Nle + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
?
L-Phe-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
-
752716
Plasmodium falciparum
L-Phe + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
?
L-Pro-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
-
752716
Plasmodium falciparum
L-Pro + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
?
L-Ser-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
-
752716
Plasmodium falciparum
L-Ser + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
?
L-Thr-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
-
752716
Plasmodium falciparum
L-Thr + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
?
L-Trp-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
best substrate
752716
Plasmodium falciparum
L-Trp + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
?
L-Tyr-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
-
752716
Plasmodium falciparum
L-Tyr + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
?
L-Val-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
-
752716
Plasmodium falciparum
L-Val + Pro-7-amido-4-carbamoylmethylcoumarin
-
-
-
?
additional information
substrate specificity, overview. Design and synthesis of a library composed of 20 fluorogenic substrates, which is used to determine the substrate fingerprint of mature PfAPP (PfAPP, residues 121-777). The enzyme from Plasmodium falciparum can catalyze the removal of any residue immediately prior to a proline. The coupled assay uses a prolyl iminopeptidase (EC 3.4.11.5) to release the free 7-amino-4-carbamoylmethylcoumarin for fluorogenic detection
752716
Plasmodium falciparum
?
-
-
-
?
RPPGFSPFR + H2O
i.e. bradykinin
752716
Plasmodium falciparum
L-Arg + PPGFSPFR
-
-
-
?
YPWTQ + H2O
a hemoglobin peptide
752716
Plasmodium falciparum
L-Tyr + PWTQ
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
homodimer
the enzyme structure shows a homodimer associated by an extensive interface between the catalytic domains (domain III) of both monomers. The active site is internally located at the junction of the three domains and shows a di-metal coordination consistent with the presence of two catalytic manganese ions
Plasmodium falciparum
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Plasmodium falciparum
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Plasmodium falciparum
General Information
General Information
Commentary
Organism
metabolism
four metalloaminopeptidases (MAPs) play a role in peptide turnover in Pf parasites: leucyl aminopeptidase (PfA-M17), alanyl aminopeptidase (PfA-M1), aspartyl aminopeptidase (PfM18AAP), and aminopeptidase P (PfAPP). The substrate profile shows that PfAPP has the capacity to catalyze the removal of any N-terminal amino acid residue from peptides with a P1' proline, and that the other MAPs in Plasmodium falciparum are unable to perform this function
Plasmodium falciparum
additional information
three-dimensional structure analysis and structure-function analysis, structure comparisons, overview
Plasmodium falciparum
physiological function
peptide recycling, the process by which cellular proteins are broken down to single amino acid residues, is critical to parasite survival. In blood-stage malaria parasites, two major processes are responsible for peptide turnover: proteasomal (within the cytosol) and vacuolar (in the specialized digestive food vacuole). The vacuolar pathway is responsible for the digestion of 60-80% of host cell hemoglobin, which is imported into the digestive vacuole and degraded into free amino acids. This process is absolutely necessary for parasite growth and development. The final step of peptide turnover, the removal of N-terminal amino acids from short polypeptide chains, is catalyzed by a panel of aminopeptidases, which work in concert according to different substrate specificities, to complete protein digestion. During the blood stage, the parasites utilise a proteolytic cascade to digest host hemoglobin, which produces free amino acids absolutely necessary for parasite growth and reproduction. The enzymes required for hemoglobin digestion are therefore attractive therapeutic targets. The final step of the cascade is catalyzed by several metalloaminopeptidases, including aminopeptidase P (APP)
Plasmodium falciparum
General Information (protein specific)
General Information
Commentary
Organism
metabolism
four metalloaminopeptidases (MAPs) play a role in peptide turnover in Pf parasites: leucyl aminopeptidase (PfA-M17), alanyl aminopeptidase (PfA-M1), aspartyl aminopeptidase (PfM18AAP), and aminopeptidase P (PfAPP). The substrate profile shows that PfAPP has the capacity to catalyze the removal of any N-terminal amino acid residue from peptides with a P1' proline, and that the other MAPs in Plasmodium falciparum are unable to perform this function
Plasmodium falciparum
additional information
three-dimensional structure analysis and structure-function analysis, structure comparisons, overview
Plasmodium falciparum
physiological function
peptide recycling, the process by which cellular proteins are broken down to single amino acid residues, is critical to parasite survival. In blood-stage malaria parasites, two major processes are responsible for peptide turnover: proteasomal (within the cytosol) and vacuolar (in the specialized digestive food vacuole). The vacuolar pathway is responsible for the digestion of 60-80% of host cell hemoglobin, which is imported into the digestive vacuole and degraded into free amino acids. This process is absolutely necessary for parasite growth and development. The final step of peptide turnover, the removal of N-terminal amino acids from short polypeptide chains, is catalyzed by a panel of aminopeptidases, which work in concert according to different substrate specificities, to complete protein digestion. During the blood stage, the parasites utilise a proteolytic cascade to digest host hemoglobin, which produces free amino acids absolutely necessary for parasite growth and reproduction. The enzymes required for hemoglobin digestion are therefore attractive therapeutic targets. The final step of the cascade is catalyzed by several metalloaminopeptidases, including aminopeptidase P (APP)
Plasmodium falciparum
Other publictions for EC 3.4.11.9
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Synonyms
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
753576
Singh
Crystal structures and bioche ...
Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508
FEBS Lett.
593
443-454
2019
-
-
1
1
-
-
3
3
-
1
1
-
-
3
-
-
1
-
-
-
-
-
8
2
1
1
-
-
3
1
-
-
-
1
-
-
-
-
1
-
1
-
-
-
3
1
3
-
1
1
-
-
-
-
1
-
-
-
-
8
2
1
-
-
3
1
-
-
-
-
-
-
-
3
3
753399
Baik
Characterization of aminopept ...
Synechocystis sp. PCC 6803
Dokl. Biochem. Biophys.
481
190-194
2018
-
-
1
-
-
-
10
1
-
2
-
-
-
4
-
-
1
-
-
-
-
-
3
1
4
1
1
-
-
1
1
-
-
-
-
-
-
-
1
-
-
-
-
-
10
-
1
-
2
-
-
-
-
-
1
-
-
-
-
3
1
1
1
-
-
1
1
-
-
-
3
3
-
-
-
753628
Giannoglou
Effect of high pressure on st ...
Streptococcus thermophilus, Streptococcus thermophilus ACA DC 0022
Food Chem.
248
304-311
2018
1
1
-
-
-
-
1
-
-
-
1
-
-
4
-
-
1
-
-
-
-
-
3
2
1
2
-
-
-
1
-
-
-
-
-
-
1
1
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
1
-
-
-
-
3
2
2
-
-
-
1
-
-
-
-
-
-
-
-
-
754700
Arreola
Trichomonas vaginalis metallo ...
Trichomonas vaginalis
Mol. Biotechnol.
60
563-575
2018
-
-
1
1
-
-
-
-
-
2
-
-
-
7
-
-
1
-
-
-
-
-
-
2
2
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
2
-
-
-
-
-
1
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
2
2
-
-
-
755161
Chang
Investigation of the proton r ...
Homo sapiens
PLoS ONE
13
e0190816
2018
4
-
1
-
3
-
2
7
2
3
-
-
-
3
-
-
1
-
-
-
-
-
2
2
4
1
-
1
6
1
-
-
-
-
-
-
4
-
1
-
-
3
-
-
2
-
7
2
3
-
-
-
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1
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2
2
1
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1
6
1
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6
6
755354
Are
Structures and activities of ...
Mycobacterium tuberculosis, Escherichia coli, Deinococcus radiodurans, Deinococcus radiodurans R1, Deinococcus radiodurans DSM 20539, Deinococcus radiodurans VKM B-1422, Mycobacterium tuberculosis H37Rv, Mycobacterium tuberculosis ATCC 25618, Deinococcus radiodurans NCIMB 9279, Deinococcus radiodurans JCM 16871, Deinococcus radiodurans LMG 4051, Deinococcus radiodurans ATCC 13939, Deinococcus radiodurans NBRC 15346
Proteins
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2018
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2
2
6
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16
1
5
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13
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2
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61
3
13
3
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16
3
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2
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2
6
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16
1
5
-
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2
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61
3
3
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16
3
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5
5
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16
16
753683
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Structure-function relationsh ...
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Front. Microbiol.
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1
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1
2
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2
2
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Enzymatic characterization of ...
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11
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1
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12
1
1
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1
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1
1
1
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Drendel
Proteome profiling of clear c ...
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7
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1
2
1
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1
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1
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24
1
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3
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Crystal structure of X-prolyl ...
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Nandan
Unveiling aminopeptidase P fro ...
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Stressler
Production, active staining an ...
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1
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3
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Yoon
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Individuals with mutations in ...
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Arima
Streptomyces aminopeptidase P: ...
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La Corte
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pTONA5: a hyperexpression vect ...
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36056
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11
1
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1
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2
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1
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4
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1
2
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1
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1
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11
1
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1
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1
-
2
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36041
Hooper
Ectoenzymes of the kidney micr ...
Homo sapiens, Sus scrofa
FEBS Lett.
229
340-344
1988
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2
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2
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36042
Lasch
Enzymic properties of intestin ...
Rattus norvegicus
FEBS Lett.
227
171-174
1988
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5
1
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1
1
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1
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5
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1
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1
1
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1
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1
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36043
Holtzman
Aminopeptidase P activity in r ...
Homo sapiens, Rattus norvegicus
Anal. Biochem.
162
476-481
1987
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2
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2
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6
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19
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2
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19
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2
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36059
Orawski
Aminopeptidase P from bovine l ...
Bos taurus
Mol. Cell. Biochem.
75
123-132
1987
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6
1
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1
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1
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4
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6
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1
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1
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4
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1
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36045
Achstetter
Proteolysis in eucaryotic cell ...
Saccharomyces cerevisiae
Arch. Biochem. Biophys.
226
292-305
1983
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4
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2
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1
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4
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1
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1
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36046
Miller
Degradation of proline peptide ...
Salmonella enterica subsp. enterica serovar Typhimurium
J. Bacteriol.
153
350-356
1983
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1
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1
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1
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1
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36052
Fleminger
Fluorogenic substrates for bac ...
Bos taurus, Escherichia coli, Homo sapiens
Eur. J. Biochem.
125
609-615
1982
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8
2
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3
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2
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2
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3
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2
1
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8
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2
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2
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2
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3
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2
1
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35949
Chen
Hydrolases from Neisseria gono ...
Neisseria gonorrhoeae
J. Biol. Chem.
255
1704-1710
1980
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1
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3
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1
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14
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1
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3
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14
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36048
Lin
Kinetic mechanism for conforma ...
Escherichia coli, Escherichia coli B / ATCC 11303
Biochemistry
19
3055-3059
1980
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177
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1
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36053
Lin
Role of cis-trans isomerism of ...
Escherichia coli
Biochemistry
18
5037-5042
1979
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1
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1
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1
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36050
Yaron
-
Aminopeptidase-P ...
Escherichia coli
Methods Enzymol.
19
521-534
1970
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1
2
1
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2
2
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1
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1
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1
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1
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1
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1
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2
2
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1
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1
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1
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1
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36051
Yaron
Aminopeptidase-P ...
Escherichia coli, Escherichia coli B / ATCC 11303
Biochem. Biophys. Res. Commun.
32
658-663
1968
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1
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177
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1
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1
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13
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1
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1
1
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1
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1
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13
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