| IED ID | IndEnz0002016631 |
| Enzyme Type ID | protease016631 |
| Protein Name |
Probable cytosol aminopeptidase EC 3.4.11.1 Leucine aminopeptidase LAP EC 3.4.11.10 Leucyl aminopeptidase |
| Gene Name | pepA Pput_1018 |
| Organism | Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Pseudomonadales Pseudomonadaceae Pseudomonas Pseudomonas putida group Pseudomonas putida (Arthrobacter siderocapsulatus) Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1) |
| Enzyme Sequence | MELVVKSVAAASVKTATLVLPVGENRKLGAVAKAVDQASEGAISAVLKRGDLAGKPGQTLLLQNLPGLKAERVLLVGSGKEEALGDRAWRKLVASVAGVLKGLNGTDAVLALDDIAVSNRDAHYGKYRLLAETLLDGEYVFDRFKSQKAEPRALKKVTLLADKAGQAEVERAVKHASAIASGMAFTRDLGNLPPNLCHPSFLAEQAKELGKAHKALKVEVLDEKKIKDLGMGAFYAVGQGSDQPPRLIMLNYQGGKKADKPFVLVGKGITFDTGGISLKPGAGMDEMKYDMCGAASVFGTLRAVLELQLPINLVCLLACAENMPSGGATRPGDIVTTMSGQTVEILNTDAEGRLVLCDTLTYAERFKPQAVIDIATLTGACIVALGSHTSGLMGNNDDLVGQLLDAGKRADDRAWQLPLFDEYQEQLDSPFADMGNIGGPKAGTITAGCFLSRFAKAYNWAHMDIAGTAWVSGGKDKGATGRPVPLLTQYLLDRAGA |
| Enzyme Length | 497 |
| Uniprot Accession Number | A5VZ69 |
| Absorption | |
| Active Site | ACT_SITE 279; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; ACT_SITE 353; /evidence=ECO:0000255|HAMAP-Rule:MF_00181 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low.; EC=3.4.11.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00181}; CATALYTIC ACTIVITY: Reaction=Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.; EC=3.4.11.10; Evidence={ECO:0000255|HAMAP-Rule:MF_00181}; |
| DNA Binding | |
| EC Number | 3.4.11.1; 3.4.11.10 |
| Enzyme Function | FUNCTION: Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. {ECO:0000255|HAMAP-Rule:MF_00181}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Metal binding (7) |
| Keywords | Aminopeptidase;Cytoplasm;Hydrolase;Manganese;Metal-binding;Protease |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00181}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 52,429 |
| Kinetics | |
| Metal Binding | METAL 267; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 272; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 272; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 290; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 349; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 351; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 351; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181 |
| Rhea ID | |
| Cross Reference Brenda |