| IED ID | IndEnz0002014184 |
| Enzyme Type ID | protease014184 |
| Protein Name |
Aminopeptidase HP_1037 EC 3.4.11.- |
| Gene Name | HP_1037 C694_05365 |
| Organism | Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria delta/epsilon subdivisions Epsilonproteobacteria Campylobacterales Helicobacteraceae Helicobacter Helicobacter pylori (Campylobacter pylori) Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori) |
| Enzyme Sequence | MKGLERESHFTLNENAMFFECAYSCDNALFLQLDDRSFFITDSRYTQEAKESVQPKNGVLAEVVESSDLVQSAIDLIVKSSVKKLFFDPNQVNLQTYKRLNSALGDKVALEGVPSYHRQKRIIKNEHEIQLLKKSQALNVEAFENFAEYVKKIFDEKESLSERYLQHKVKDFLTREGVYDLSFEPILALNANASKPHALPSAKDFLKAEHSILLDMGIKYERYCSDRTRTAFFDPKDFVFKREQSFKDKERQKIYDIVKEAQEKAISGIRAGMTGKEADSLARGVISDYGYGQYFTHSTGHGIGLDIHELPYISSRSETILEEGMVFSVEPGIYIPGFFGVRIEDLVVIKNSRSELL |
| Enzyme Length | 357 |
| Uniprot Accession Number | O25681 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.11.- |
| Enzyme Function | FUNCTION: Hydrolyzes the N-terminal amino acid residue from a polypeptide chain, with a preference for substrates containing multiple alanine residues. {ECO:0000269|PubMed:23825549}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is about 40 degrees Celsius. {ECO:0000269|PubMed:23825549}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.0-5.0. {ECO:0000269|PubMed:23825549}; |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Metal binding (7) |
| Keywords | Aminopeptidase;Cobalt;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11196647; |
| Motif | |
| Gene Encoded By | |
| Mass | 40,796 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.38 mM for N-succinyl-Ala-Ala-Ala-Pro-Phe-p-nitroanilide {ECO:0000269|PubMed:23825549}; KM=7.56 mM for pyroglutamyl-Pro-Arg-p-nitroanilide {ECO:0000269|PubMed:23825549}; KM=1.12 mM for N-succinyl-Ala-Ala-Ala-p-nitroanilide {ECO:0000269|PubMed:23825549}; KM=7.43 mM for Phe-Arg-methylcoumarine amide {ECO:0000269|PubMed:23825549}; KM=4.06 mM for N-succinyl-Leu-Leu-Val-Tyr-methylcoumarine amide {ECO:0000269|PubMed:23825549}; Note=kcat is 1145 min(-1) and 122 min(-1) with N-succinyl-Ala-Ala-Ala-Pro-Phe-p-nitroanilide and N-succinyl-Ala-Ala-Ala-p-nitroanilide as substrate, respectively.; |
| Metal Binding | METAL 215; /note=Cobalt 2; /evidence=ECO:0000250; METAL 226; /note=Cobalt 1; /evidence=ECO:0000250; METAL 226; /note=Cobalt 2; /evidence=ECO:0000250; METAL 301; /note=Cobalt 1; /evidence=ECO:0000250; METAL 330; /note=Cobalt 1; /evidence=ECO:0000250; METAL 344; /note=Cobalt 1; /evidence=ECO:0000250; METAL 344; /note=Cobalt 2; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |