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Literature summary extracted from
- Structures and activities of widely conserved small prokaryotic aminopeptidases-P clarify classification of M24B peptidases (2018), Proteins, 87, 212-225 .
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.4.11.9 | recombinant expression of the His-tagged enzyme in Escherichia coli strain BL21(DE3) pLysS | Escherichia coli |
| 3.4.11.9 | recombinant expression of wild-type and mutant His-tagged enzyme in Escherichia coli strain BL21(DE3) pLysS | Deinococcus radiodurans |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 3.4.11.9 | purified recombinant enzyme, mixing of 0.002 ml of about 15 mg/ml protein in 20 mM Tris-HCl pH 8.0, 200 mM NaCl, with 0.002 ml crystallization solution containing 0.1 M phospho-citrate, pH 4.6, 0.2 M NaCl, and 22% PEG 8000, X-ray diffraction structure determination and analysis at 1.8 A resolution, molecular replacement using the putative prolidase from Telmatobius sibiricus (PDB ID: 4FKC) as template | Deinococcus radiodurans |
| 3.4.11.9 | purified recombinant enzyme, mixing of 0.002 ml of about 15 mg/ml protein in 20 mM Tris-HCl pH 8.0, 200 mM NaCl, with 0.002 ml of crystallization solution containing 1.4 M trisodium citrate, 0.1 M sodium cacodylate, pH 6.5, 10% glycerol, and 0.5 mM ZnCl2, X-ray diffraction structure determination and analysis at 2.6 A resolution, molecular replacement using the putative prolidase from Telmatobius sibiricus (PDB ID: 4FKC) as template | Escherichia coli |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.4.11.9 | D53A | site-directed mutagenesis, mutant D53A is significantly less active than the wild-type protein toward Xaa-Pro-Ala tripeptides | Deinococcus radiodurans |
| 3.4.11.9 | H193A | site-directed mutagenesis, inactive mutant, the mutant shows 4fold reduced activity compared to the wild-type | Deinococcus radiodurans |
| 3.4.11.9 | H281A | site-directed mutagenesis, the H281A mutation leads to 10fold reduction in the activity compared to wild-type possibly because of poor substrate binding | Deinococcus radiodurans |
| 3.4.11.9 | R298A | site-directed mutagenesis | Deinococcus radiodurans |
| 3.4.11.9 | R55A | site-directed mutagenesis, mutant R55A is significantly less active than the wild-type protein toward Xaa-Pro-Ala tripeptides | Deinococcus radiodurans |
| 3.4.11.9 | Y56A | site-directed mutagenesis, mutant Y56A is significantly less active than the wild-type protein toward Xaa-Pro-Ala tripeptides | Deinococcus radiodurans |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.4.11.9 | 0.15 | - |
Met-Ala-Ala | pH 8.0, 55°C, recombinant wild-type | Deinococcus radiodurans |  |
| 3.4.11.9 | 0.23 | - |
Met-Ala-Ala | pH 8.0, 55°C, recombinant wild-type | Escherichia coli | |
| 3.4.11.9 | 0.46 | - |
Met-Ala-Ala | pH 8.0, 55°C, recombinant wild-type | Mycobacterium tuberculosis | |
| 3.4.11.9 | 1.9 | - |
Met-Pro-Ala | pH 8.0, 55°C, recombinant wild-type | Deinococcus radiodurans | |
| 3.4.11.9 | 2.1 | - |
Arg-Pro-Ala | pH 8.0, 55°C, recombinant wild-type | Deinococcus radiodurans | |
| 3.4.11.9 | 3 | - |
Met-Pro-Ala | pH 8.0, 55°C, recombinant wild-type | Escherichia coli | |
| 3.4.11.9 | 3.5 | - |
Arg-Pro-Ala | pH 8.0, 55°C, recombinant mutant R55A | Deinococcus radiodurans | |
| 3.4.11.9 | 3.9 | - |
Met-Pro-Ala | pH 8.0, 55°C, recombinant mutant Y56A | Deinococcus radiodurans | |
| 3.4.11.9 | 4 | - |
Met-Pro-Ala | pH 8.0, 55°C, recombinant mutant D53A | Deinococcus radiodurans | |
| 3.4.11.9 | 6 | - |
Arg-Pro-Ala | pH 8.0, 55°C, recombinant mutant D53A | Deinococcus radiodurans | |
| 3.4.11.9 | 6.1 | - |
Met-Pro-Ala | pH 8.0, 55°C, recombinant mutant R55A | Deinococcus radiodurans | |
| 3.4.11.9 | 6.3 | - |
Met-Pro | pH 8.0, 55°C, recombinant wild-type | Mycobacterium tuberculosis | |
| 3.4.11.9 | 7.9 | - |
Met-Pro | pH 8.0, 55°C, recombinant wild-type | Escherichia coli | |
| 3.4.11.9 | 8.4 | - |
Arg-Pro-Ala | pH 8.0, 55°C, recombinant mutant Y56A | Deinococcus radiodurans | |
| 3.4.11.9 | 9 | - |
Met-Pro-Ala | pH 8.0, 55°C, recombinant wild-type | Mycobacterium tuberculosis | |
| 3.4.11.9 | 11.9 | - |
Met-Pro | pH 8.0, 55°C, recombinant wild-type | Deinococcus radiodurans | |
| 3.4.13.9 | 0.91 | - |
Met-Ala-Ala | pH 7.0, 97°C, recombinant wild-type | Pyrococcus furiosus | |
| 3.4.13.9 | 1.8 | - |
Met-Pro-Ala | pH 7.0, 97°C, recombinant wild-type | Pyrococcus furiosus | |
| 3.4.13.9 | 9.8 | - |
Met-Pro | pH 7.0, 97°C, recombinant wild-type | Pyrococcus furiosus | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.4.11.9 | cytoplasm | - |
Mycobacterium tuberculosis | 5737 | - |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.11.9 | Mn2+ | required | Escherichia coli | |
| 3.4.11.9 | Mn2+ | required | Deinococcus radiodurans | |
| 3.4.11.9 | Mn2+ | required | Mycobacterium tuberculosis | |
| 3.4.11.9 | Zn2+ | required, di-metal center, one metal ion (ZnA) is penta-coordinated and exhibits distorted trigonal bipyramidal geometry, whereas the other (ZnB) is tetra-coordinated and exhibits a tetrahedral geometry. Metal ZnA is coordinated by O1 of cacodylate ion, Glu335 Oepsilon2, Glu321 Oepsilon2, His292 Nepsilon2, and Asp223 Odelta2. Metal ZnB is coordinated by O1 of cacodylate ion, Glu335 Oepsilon1, Asp212 Odelta1, and Asp223 Odelta1. Glu335 and Asp223 act as bidentate ligands and bind to both the metals | Escherichia coli | |
| 3.4.11.9 | Zn2+ | required, di-metal center, one metal ion (ZnA) is penta-coordinated and exhibits distorted trigonal bipyramidal geometry, whereas the other (ZnB) is tetra-coordinated and exhibits a tetrahedral geometry. Metal ZnA of Dr-smAPP is coordinated by O3 of phosphate ion, His285 Nepsilon2, and Glu328 Oepsilon1 in the equatorial plane and Asp221 Odelta2 and Glu314 Oepsilon2 in the axial sites. Metal ZnB of Dr-smAPP is coordinated by O3 of phosphate ion, Asp210 Odelta1, Asp221 Odelta1, and Glu328 Oepsilon2. Glu328 and Asp221 act as bidentate ligands and bind to both the metals | Deinococcus radiodurans | |
| 3.4.13.9 | Co2+ | required | Pyrococcus furiosus | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.11.9 | Deinococcus radiodurans | Q9RUY4 | - |
- |
| 3.4.11.9 | Deinococcus radiodurans ATCC 13939 | Q9RUY4 | - |
- |
| 3.4.11.9 | Deinococcus radiodurans DSM 20539 | Q9RUY4 | - |
- |
| 3.4.11.9 | Deinococcus radiodurans JCM 16871 | Q9RUY4 | - |
- |
| 3.4.11.9 | Deinococcus radiodurans LMG 4051 | Q9RUY4 | - |
- |
| 3.4.11.9 | Deinococcus radiodurans NBRC 15346 | Q9RUY4 | - |
- |
| 3.4.11.9 | Deinococcus radiodurans NCIMB 9279 | Q9RUY4 | - |
- |
| 3.4.11.9 | Deinococcus radiodurans R1 | Q9RUY4 | - |
- |
| 3.4.11.9 | Deinococcus radiodurans VKM B-1422 | Q9RUY4 | - |
- |
| 3.4.11.9 | Escherichia coli | P76524 | - |
- |
| 3.4.11.9 | Mycobacterium tuberculosis | I6YDN6 | - |
- |
| 3.4.11.9 | Mycobacterium tuberculosis ATCC 25618 | I6YDN6 | - |
- |
| 3.4.11.9 | Mycobacterium tuberculosis H37Rv | I6YDN6 | - |
- |
| 3.4.13.9 | Pyrococcus furiosus | P81535 | - |
- |
| 3.4.13.9 | Pyrococcus furiosus ATCC 43587 | P81535 | - |
- |
| 3.4.13.9 | Pyrococcus furiosus JCM 8422 | P81535 | - |
- |
| 3.4.13.9 | Pyrococcus furiosus Vc1 | P81535 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.4.11.9 | recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography, tag cleavage by TEV protease, dialysis, and gel filtration | Escherichia coli |
| 3.4.11.9 | recombinant wild-type and mutant His-tagged enzyme from Escherichia coli by nickel affinity chromatography, tag cleavage by TEV protease, dialysis, and gel filtration | Deinococcus radiodurans |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.11.9 | Arg-Pro-Ala + H2O | - |
Deinococcus radiodurans | Arg + Pro-Ala | - |
? | |
| 3.4.11.9 | Arg-Pro-Ala + H2O | - |
Deinococcus radiodurans R1 | Arg + Pro-Ala | - |
? | |
| 3.4.11.9 | Arg-Pro-Ala + H2O | - |
Deinococcus radiodurans DSM 20539 | Arg + Pro-Ala | - |
? | |
| 3.4.11.9 | Arg-Pro-Ala + H2O | - |
Deinococcus radiodurans VKM B-1422 | Arg + Pro-Ala | - |
? | |
| 3.4.11.9 | Arg-Pro-Ala + H2O | - |
Deinococcus radiodurans NCIMB 9279 | Arg + Pro-Ala | - |
? | |
| 3.4.11.9 | Arg-Pro-Ala + H2O | - |
Deinococcus radiodurans JCM 16871 | Arg + Pro-Ala | - |
? | |
| 3.4.11.9 | Arg-Pro-Ala + H2O | - |
Deinococcus radiodurans LMG 4051 | Arg + Pro-Ala | - |
? | |
| 3.4.11.9 | Arg-Pro-Ala + H2O | - |
Deinococcus radiodurans ATCC 13939 | Arg + Pro-Ala | - |
? | |
| 3.4.11.9 | Arg-Pro-Ala + H2O | - |
Deinococcus radiodurans NBRC 15346 | Arg + Pro-Ala | - |
? | |
| 3.4.11.9 | Met-Ala-Ala + H2O | - |
Escherichia coli | Met + Ala-Ala | - |
? | |
| 3.4.11.9 | Met-Ala-Ala + H2O | - |
Deinococcus radiodurans | Met + Ala-Ala | - |
? | |
| 3.4.11.9 | Met-Ala-Ala + H2O | - |
Mycobacterium tuberculosis | Met + Ala-Ala | - |
? | |
| 3.4.11.9 | Met-Ala-Ala + H2O | - |
Deinococcus radiodurans R1 | Met + Ala-Ala | - |
? | |
| 3.4.11.9 | Met-Ala-Ala + H2O | - |
Deinococcus radiodurans DSM 20539 | Met + Ala-Ala | - |
? | |
| 3.4.11.9 | Met-Ala-Ala + H2O | - |
Deinococcus radiodurans VKM B-1422 | Met + Ala-Ala | - |
? | |
| 3.4.11.9 | Met-Ala-Ala + H2O | - |
Mycobacterium tuberculosis H37Rv | Met + Ala-Ala | - |
? | |
| 3.4.11.9 | Met-Ala-Ala + H2O | - |
Mycobacterium tuberculosis ATCC 25618 | Met + Ala-Ala | - |
? | |
| 3.4.11.9 | Met-Ala-Ala + H2O | - |
Deinococcus radiodurans NCIMB 9279 | Met + Ala-Ala | - |
? | |
| 3.4.11.9 | Met-Ala-Ala + H2O | - |
Deinococcus radiodurans JCM 16871 | Met + Ala-Ala | - |
? | |
| 3.4.11.9 | Met-Ala-Ala + H2O | - |
Deinococcus radiodurans LMG 4051 | Met + Ala-Ala | - |
? | |
| 3.4.11.9 | Met-Ala-Ala + H2O | - |
Deinococcus radiodurans ATCC 13939 | Met + Ala-Ala | - |
? | |
| 3.4.11.9 | Met-Ala-Ala + H2O | - |
Deinococcus radiodurans NBRC 15346 | Met + Ala-Ala | - |
? | |
| 3.4.11.9 | Met-Pro + H2O | - |
Escherichia coli | Met + Pro | - |
? | |
| 3.4.11.9 | Met-Pro + H2O | - |
Deinococcus radiodurans | Met + Pro | - |
? | |
| 3.4.11.9 | Met-Pro + H2O | - |
Mycobacterium tuberculosis | Met + Pro | - |
? | |
| 3.4.11.9 | Met-Pro + H2O | - |
Deinococcus radiodurans R1 | Met + Pro | - |
? | |
| 3.4.11.9 | Met-Pro + H2O | - |
Deinococcus radiodurans DSM 20539 | Met + Pro | - |
? | |
| 3.4.11.9 | Met-Pro + H2O | - |
Deinococcus radiodurans VKM B-1422 | Met + Pro | - |
? | |
| 3.4.11.9 | Met-Pro + H2O | - |
Mycobacterium tuberculosis H37Rv | Met + Pro | - |
? | |
| 3.4.11.9 | Met-Pro + H2O | - |
Mycobacterium tuberculosis ATCC 25618 | Met + Pro | - |
? | |
| 3.4.11.9 | Met-Pro + H2O | - |
Deinococcus radiodurans NCIMB 9279 | Met + Pro | - |
? | |
| 3.4.11.9 | Met-Pro + H2O | - |
Deinococcus radiodurans JCM 16871 | Met + Pro | - |
? | |
| 3.4.11.9 | Met-Pro + H2O | - |
Deinococcus radiodurans LMG 4051 | Met + Pro | - |
? | |
| 3.4.11.9 | Met-Pro + H2O | - |
Deinococcus radiodurans ATCC 13939 | Met + Pro | - |
? | |
| 3.4.11.9 | Met-Pro + H2O | - |
Deinococcus radiodurans NBRC 15346 | Met + Pro | - |
? | |
| 3.4.11.9 | Met-Pro-Ala + H2O | - |
Escherichia coli | Met + Pro-Ala | - |
? | |
| 3.4.11.9 | Met-Pro-Ala + H2O | - |
Deinococcus radiodurans | Met + Pro-Ala | - |
? | |
| 3.4.11.9 | Met-Pro-Ala + H2O | - |
Mycobacterium tuberculosis | Met + Pro-Ala | - |
? | |
| 3.4.11.9 | Met-Pro-Ala + H2O | - |
Deinococcus radiodurans R1 | Met + Pro-Ala | - |
? | |
| 3.4.11.9 | Met-Pro-Ala + H2O | - |
Deinococcus radiodurans DSM 20539 | Met + Pro-Ala | - |
? | |
| 3.4.11.9 | Met-Pro-Ala + H2O | - |
Deinococcus radiodurans VKM B-1422 | Met + Pro-Ala | - |
? | |
| 3.4.11.9 | Met-Pro-Ala + H2O | - |
Mycobacterium tuberculosis H37Rv | Met + Pro-Ala | - |
? | |
| 3.4.11.9 | Met-Pro-Ala + H2O | - |
Mycobacterium tuberculosis ATCC 25618 | Met + Pro-Ala | - |
? | |
| 3.4.11.9 | Met-Pro-Ala + H2O | - |
Deinococcus radiodurans NCIMB 9279 | Met + Pro-Ala | - |
? | |
| 3.4.11.9 | Met-Pro-Ala + H2O | - |
Deinococcus radiodurans JCM 16871 | Met + Pro-Ala | - |
? | |
| 3.4.11.9 | Met-Pro-Ala + H2O | - |
Deinococcus radiodurans LMG 4051 | Met + Pro-Ala | - |
? | |
| 3.4.11.9 | Met-Pro-Ala + H2O | - |
Deinococcus radiodurans ATCC 13939 | Met + Pro-Ala | - |
? | |
| 3.4.11.9 | Met-Pro-Ala + H2O | - |
Deinococcus radiodurans NBRC 15346 | Met + Pro-Ala | - |
? | |
| 3.4.11.9 | additional information | substrate specificity for Xaa-Pro dipeptides and Xaa-Pro-Ala tripeptides is analyzed, the enzyme is significantly more active toward the tripeptides than the corresponding dipeptides | Escherichia coli | ? | - |
? | |
| 3.4.11.9 | additional information | substrate specificity for Xaa-Pro dipeptides and Xaa-Pro-Ala tripeptides is analyzed, the enzyme is significantly more active toward the tripeptides than the corresponding dipeptides | Deinococcus radiodurans | ? | - |
? | |
| 3.4.11.9 | additional information | substrate specificity for Xaa-Pro dipeptides and Xaa-Pro-Ala tripeptides is analyzed, the enzyme is significantly more active toward the tripeptides than the corresponding dipeptides | Mycobacterium tuberculosis | ? | - |
? | |
| 3.4.11.9 | additional information | substrate specificity for Xaa-Pro dipeptides and Xaa-Pro-Ala tripeptides is analyzed, the enzyme is significantly more active toward the tripeptides than the corresponding dipeptides | Deinococcus radiodurans R1 | ? | - |
? | |
| 3.4.11.9 | additional information | substrate specificity for Xaa-Pro dipeptides and Xaa-Pro-Ala tripeptides is analyzed, the enzyme is significantly more active toward the tripeptides than the corresponding dipeptides | Deinococcus radiodurans DSM 20539 | ? | - |
? | |
| 3.4.11.9 | additional information | substrate specificity for Xaa-Pro dipeptides and Xaa-Pro-Ala tripeptides is analyzed, the enzyme is significantly more active toward the tripeptides than the corresponding dipeptides | Deinococcus radiodurans VKM B-1422 | ? | - |
? | |
| 3.4.11.9 | additional information | substrate specificity for Xaa-Pro dipeptides and Xaa-Pro-Ala tripeptides is analyzed, the enzyme is significantly more active toward the tripeptides than the corresponding dipeptides | Mycobacterium tuberculosis H37Rv | ? | - |
? | |
| 3.4.11.9 | additional information | substrate specificity for Xaa-Pro dipeptides and Xaa-Pro-Ala tripeptides is analyzed, the enzyme is significantly more active toward the tripeptides than the corresponding dipeptides | Mycobacterium tuberculosis ATCC 25618 | ? | - |
? | |
| 3.4.11.9 | additional information | substrate specificity for Xaa-Pro dipeptides and Xaa-Pro-Ala tripeptides is analyzed, the enzyme is significantly more active toward the tripeptides than the corresponding dipeptides | Deinococcus radiodurans NCIMB 9279 | ? | - |
? | |
| 3.4.11.9 | additional information | substrate specificity for Xaa-Pro dipeptides and Xaa-Pro-Ala tripeptides is analyzed, the enzyme is significantly more active toward the tripeptides than the corresponding dipeptides | Deinococcus radiodurans JCM 16871 | ? | - |
? | |
| 3.4.11.9 | additional information | substrate specificity for Xaa-Pro dipeptides and Xaa-Pro-Ala tripeptides is analyzed, the enzyme is significantly more active toward the tripeptides than the corresponding dipeptides | Deinococcus radiodurans LMG 4051 | ? | - |
? | |
| 3.4.11.9 | additional information | substrate specificity for Xaa-Pro dipeptides and Xaa-Pro-Ala tripeptides is analyzed, the enzyme is significantly more active toward the tripeptides than the corresponding dipeptides | Deinococcus radiodurans ATCC 13939 | ? | - |
? | |
| 3.4.11.9 | additional information | substrate specificity for Xaa-Pro dipeptides and Xaa-Pro-Ala tripeptides is analyzed, the enzyme is significantly more active toward the tripeptides than the corresponding dipeptides | Deinococcus radiodurans NBRC 15346 | ? | - |
? | |
| 3.4.13.9 | Met-Ala-Ala + H2O | - |
Pyrococcus furiosus | Met + Ala-Ala | - |
? | |
| 3.4.13.9 | Met-Ala-Ala + H2O | - |
Pyrococcus furiosus ATCC 43587 | Met + Ala-Ala | - |
? | |
| 3.4.13.9 | Met-Ala-Ala + H2O | - |
Pyrococcus furiosus Vc1 | Met + Ala-Ala | - |
? | |
| 3.4.13.9 | Met-Ala-Ala + H2O | - |
Pyrococcus furiosus JCM 8422 | Met + Ala-Ala | - |
? | |
| 3.4.13.9 | Met-Pro + H2O | - |
Pyrococcus furiosus | Met + Pro | - |
? | |
| 3.4.13.9 | Met-Pro + H2O | - |
Pyrococcus furiosus ATCC 43587 | Met + Pro | - |
? | |
| 3.4.13.9 | Met-Pro + H2O | - |
Pyrococcus furiosus Vc1 | Met + Pro | - |
? | |
| 3.4.13.9 | Met-Pro + H2O | - |
Pyrococcus furiosus JCM 8422 | Met + Pro | - |
? | |
| 3.4.13.9 | Met-Pro-Ala + H2O | - |
Pyrococcus furiosus | Met + Pro-Ala | - |
? | |
| 3.4.13.9 | Met-Pro-Ala + H2O | - |
Pyrococcus furiosus ATCC 43587 | Met + Pro-Ala | - |
? | |
| 3.4.13.9 | Met-Pro-Ala + H2O | - |
Pyrococcus furiosus Vc1 | Met + Pro-Ala | - |
? | |
| 3.4.13.9 | Met-Pro-Ala + H2O | - |
Pyrococcus furiosus JCM 8422 | Met + Pro-Ala | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.4.11.9 | homodimer | 2 * 37100, SDS-PAGE | Deinococcus radiodurans |
| 3.4.11.9 | homodimer | 2 * 39600, SDS-PAGE | Escherichia coli |
| 3.4.11.9 | homodimer | 2 * 38700, SDS-PAGE | Mycobacterium tuberculosis |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.4.11.9 | Dr-smAPP | - |
Deinococcus radiodurans |
| 3.4.11.9 | Ec-smAPP | - |
Escherichia coli |
| 3.4.11.9 | M24B peptidase | - |
Escherichia coli |
| 3.4.11.9 | M24B peptidase | - |
Deinococcus radiodurans |
| 3.4.11.9 | M24B peptidase | - |
Mycobacterium tuberculosis |
| 3.4.11.9 | Mt-smAPP | - |
Mycobacterium tuberculosis |
| 3.4.11.9 | PepQ | - |
Mycobacterium tuberculosis |
| 3.4.11.9 | peptidase PepQ | - |
Mycobacterium tuberculosis |
| 3.4.11.9 | small aminopeptidase-P | - |
Escherichia coli |
| 3.4.11.9 | small aminopeptidase-P | - |
Deinococcus radiodurans |
| 3.4.11.9 | small aminopeptidase-P | - |
Mycobacterium tuberculosis |
| 3.4.11.9 | YpdF | - |
Escherichia coli |
| 3.4.13.9 | M24B peptidase | - |
Pyrococcus furiosus |
| 3.4.13.9 | PepQ | - |
Pyrococcus furiosus |
| 3.4.13.9 | Pf-peptidase | - |
Pyrococcus furiosus |
| 3.4.13.9 | prolidase | - |
Pyrococcus furiosus |
| 3.4.13.9 | X-Pro dipeptidase | - |
Pyrococcus furiosus |
| 3.4.13.9 | Xaa-Pro dipeptidase | - |
Pyrococcus furiosus |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.4.11.9 | 55 | - |
assay at | Escherichia coli |
| 3.4.11.9 | 55 | - |
assay at | Deinococcus radiodurans |
| 3.4.11.9 | 55 | - |
assay at | Mycobacterium tuberculosis |
| 3.4.13.9 | 97 | - |
assay at | Pyrococcus furiosus |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.4.11.9 | 1.5 | - |
Met-Ala-Ala | pH 8.0, 55°C, recombinant wild-type | Escherichia coli | |
| 3.4.11.9 | 2 | 8 | Met-Pro-Ala | pH 8.0, 55°C, recombinant wild-type | Escherichia coli | |
| 3.4.11.9 | 5 | - |
Met-Ala-Ala | pH 8.0, 55°C, recombinant wild-type | Mycobacterium tuberculosis | |
| 3.4.11.9 | 10.5 | - |
Met-Ala-Ala | pH 8.0, 55°C, recombinant wild-type | Deinococcus radiodurans | |
| 3.4.11.9 | 18 | - |
Met-Pro | pH 8.0, 55°C, recombinant wild-type | Mycobacterium tuberculosis | |
| 3.4.11.9 | 29 | - |
Arg-Pro-Ala | pH 8.0, 55°C, recombinant mutant D53A | Deinococcus radiodurans | |
| 3.4.11.9 | 33 | - |
Met-Pro | pH 8.0, 55°C, recombinant wild-type | Escherichia coli | |
| 3.4.11.9 | 35 | - |
Met-Pro-Ala | pH 8.0, 55°C, recombinant mutant D53A | Deinococcus radiodurans | |
| 3.4.11.9 | 97 | - |
Met-Pro | pH 8.0, 55°C, recombinant wild-type | Deinococcus radiodurans | |
| 3.4.11.9 | 101 | - |
Arg-Pro-Ala | pH 8.0, 55°C, recombinant mutant R55A | Deinococcus radiodurans | |
| 3.4.11.9 | 126 | - |
Met-Pro-Ala | pH 8.0, 55°C, recombinant wild-type | Mycobacterium tuberculosis | |
| 3.4.11.9 | 140 | - |
Met-Pro-Ala | pH 8.0, 55°C, recombinant mutant Y56A | Deinococcus radiodurans | |
| 3.4.11.9 | 144 | - |
Met-Pro-Ala | pH 8.0, 55°C, recombinant mutant R55A | Deinococcus radiodurans | |
| 3.4.11.9 | 152 | - |
Arg-Pro-Ala | pH 8.0, 55°C, recombinant mutant Y56A | Deinococcus radiodurans | |
| 3.4.11.9 | 240 | - |
Arg-Pro-Ala | pH 8.0, 55°C, recombinant wild-type | Deinococcus radiodurans | |
| 3.4.11.9 | 242 | - |
Met-Pro-Ala | pH 8.0, 55°C, recombinant wild-type | Deinococcus radiodurans | |
| 3.4.13.9 | 27 | - |
Met-Ala-Ala | pH 7.0, 97°C, recombinant wild-type | Pyrococcus furiosus | |
| 3.4.13.9 | 102 | - |
Met-Pro | pH 7.0, 97°C, recombinant wild-type | Pyrococcus furiosus | |
| 3.4.13.9 | 192 | - |
Met-Pro-Ala | pH 7.0, 97°C, recombinant wild-type | Pyrococcus furiosus | |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.4.11.9 | 8 | - |
assay at | Escherichia coli |
| 3.4.11.9 | 8 | - |
assay at | Deinococcus radiodurans |
| 3.4.11.9 | 8 | - |
assay at | Mycobacterium tuberculosis |
| 3.4.13.9 | 7 | - |
assay at | Pyrococcus furiosus |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.4.11.9 | evolution | the enzyme belongs to the M24B subfamily of aminoproteases | Escherichia coli |
| 3.4.11.9 | evolution | the enzyme belongs to the M24B subfamily of aminoproteases | Deinococcus radiodurans |
| 3.4.11.9 | additional information | the active site includes the DXRY motif. Structure comparisons of small aminopeptidases-P | Mycobacterium tuberculosis |
| 3.4.11.9 | additional information | the protein adopts a two-domain structure typical of the M24B subfamily with an N-terminal domain (residues 1-121) and a C-terminal domain (residues 122-349). The C-terminal domain, adopting a typical pitabread-fold, houses the metal binding active site. Residues Asp53, Arg55, and Tyr56 are part of the conserved DXRY motif, which is important for enzymatic activity, His193 is expected to interact with the DXRY motif in the closed conformation and may also be involved in substrate binding, His281 is expected to be part of the proline binding pocket, and Arg298 is expected to interact with tripeptide and longer peptide substrates. Residue His93 is expected to interact with the DXRY motif in the closed conformation and may also be involved in substrate binding, His281 is expected to be part of the proline binding pocket, and Arg298 is expected to interact with tripeptide and longer peptide substratesBoth His281 and Arg298 residues are found to be disordered in the Dr-smAPP structure. The active site includes the DXRY motif. Structure comparisons of small aminopeptidases-P | Deinococcus radiodurans |
| 3.4.11.9 | additional information | the protein adopts a two-domain structure typical of the M24B subfamily with an N-terminal domain (residues 1-123) and a C-terminal domain (residues 124-360). The C-terminal domain, adopting a typical pita-bread-fold, houses the metal binding active site. The active site includes the DXRY motif. Structure comparisons of small aminopeptidases-P | Escherichia coli |
kcat/KM [mM/s]
| EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.4.11.9 | 2.85 | - |
Met-Pro | pH 8.0, 55°C, recombinant wild-type | Mycobacterium tuberculosis | |
| 3.4.11.9 | 4.17 | - |
Met-Pro | pH 8.0, 55°C, recombinant wild-type | Escherichia coli | |
| 3.4.11.9 | 4.8 | - |
Arg-Pro-Ala | pH 8.0, 55°C, recombinant mutant D53A | Deinococcus radiodurans | |
| 3.4.11.9 | 6.5 | - |
Met-Ala-Ala | pH 8.0, 55°C, recombinant wild-type | Escherichia coli | |
| 3.4.11.9 | 8.15 | - |
Met-Pro | pH 8.0, 55°C, recombinant wild-type | Deinococcus radiodurans | |
| 3.4.11.9 | 8.8 | - |
Met-Pro-Ala | pH 8.0, 55°C, recombinant mutant D53A | Deinococcus radiodurans | |
| 3.4.11.9 | 9.3 | - |
Met-Pro-Ala | pH 8.0, 55°C, recombinant wild-type | Escherichia coli | |
| 3.4.11.9 | 11 | - |
Met-Ala-Ala | pH 8.0, 55°C, recombinant wild-type | Mycobacterium tuberculosis | |
| 3.4.11.9 | 14 | - |
Met-Pro-Ala | pH 8.0, 55°C, recombinant wild-type | Mycobacterium tuberculosis | |
| 3.4.11.9 | 18 | - |
Arg-Pro-Ala | pH 8.0, 55°C, recombinant mutant Y56A | Deinococcus radiodurans | |
| 3.4.11.9 | 24 | - |
Met-Pro-Ala | pH 8.0, 55°C, recombinant mutant R55A | Deinococcus radiodurans | |
| 3.4.11.9 | 29 | - |
Arg-Pro-Ala | pH 8.0, 55°C, recombinant mutant R55A | Deinococcus radiodurans | |
| 3.4.11.9 | 36 | - |
Met-Pro-Ala | pH 8.0, 55°C, recombinant mutant Y56A | Deinococcus radiodurans | |
| 3.4.11.9 | 70 | - |
Met-Ala-Ala | pH 8.0, 55°C, recombinant wild-type | Deinococcus radiodurans | |
| 3.4.11.9 | 114 | - |
Arg-Pro-Ala | pH 8.0, 55°C, recombinant wild-type | Deinococcus radiodurans | |
| 3.4.11.9 | 127 | - |
Met-Pro-Ala | pH 8.0, 55°C, recombinant wild-type | Deinococcus radiodurans | |
| 3.4.13.9 | 30 | - |
Met-Ala-Ala | pH 7.0, 97°C, recombinant wild-type | Pyrococcus furiosus | |
| 3.4.13.9 | 107 | - |
Met-Pro-Ala | pH 7.0, 97°C, recombinant wild-type | Pyrococcus furiosus | |
| 3.4.13.9 | 127 | - |
Met-Pro | pH 7.0, 97°C, recombinant wild-type | Pyrococcus furiosus | |
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Release 2023.1 (January 2023)
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