| IED ID | IndEnz0002014485 |
| Enzyme Type ID | protease014485 |
| Protein Name |
Beta-peptidyl aminopeptidase BapA EC 3.4.11.25 Cleaved into: Beta-peptidyl aminopeptidase BapA alpha subunit; Beta-peptidyl aminopeptidase BapA beta subunit |
| Gene Name | |
| Organism | Sphingosinicella microcystinivorans |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Alphaproteobacteria Sphingomonadales Sphingosinicellaceae Sphingosinicella Sphingosinicella microcystinivorans |
| Enzyme Sequence | MHYLKFPAIIAGMLLAGAASAEGPRARDLGVPFAGKPGANNAITDVAGVEVGYVSLISGEGKLERGKGPVRTGVTAVLPRGKESRTPVYAGWETSNAAGEMTGTVWLEERGYFDGPMMITNTHSVGVVRDAVVGWLADVKWPGAWFTPVVAETYDGMLNDINGFHVKPEHALRAIQTAASGPVAEGNVGGGVGMQCFGFKGGTGTASRVVEMDGKSYTVGVLVQCNFGMRPWLRVAGAPVGEELAGKYLPETRGTQTAAATNNGVAPGDGSIIVVMATDAPMLPHQLKRLAKRAAAGMGRMGDAGSNGSGDIFVAFSTANANVQSVGGNVISVETMPNDKLTLIFEAATQATEEAITNVLVAADTLTGVNGYTIQRLPHAELRAILKKYRRLAAAK |
| Enzyme Length | 396 |
| Uniprot Accession Number | A0MTQ2 |
| Absorption | |
| Active Site | ACT_SITE 271; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:Q52VH2; ACT_SITE 309; /note=Proton donor/acceptor; /evidence=ECO:0000250|UniProtKB:Q52VH2; ACT_SITE 311; /note=Proton donor/acceptor; /evidence=ECO:0000250|UniProtKB:Q52VH2 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by AEBSF (4-(2-aminoethyl)benzenesulfonyl fluoride, Pefabloc SC). {ECO:0000269|PubMed:17064315}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Cleaves N-terminal beta-homoamino acids from peptides composed of 2 to 6 amino acids.; EC=3.4.11.25; Evidence={ECO:0000269|PubMed:17064315}; |
| DNA Binding | |
| EC Number | 3.4.11.25 |
| Enzyme Function | FUNCTION: Beta-aminopeptidase that can cleave synthetic beta-peptides which consist of backbone-elongated beta-amino acid residues that are not processed by common proteolytic enzymes. Can cleave the beta-peptides beta-homoVal-beta-homoAla-beta-homoLeu and beta-homoAla-beta-homoLeu. Requires a beta-amino acid at the N-terminus of peptide substrates and cleaves the peptide bond between the N-terminal beta-amino acid and the amino acid at the second position of tripeptidic substrates of the general structure H-betahXaa-Ile-betahTyr-OH according to the following preferences with regard to the side chain of the N-terminal beta-amino acid: aliphatic and aromatic > OH-containing > hydrogen, basic and polar. beta-homoVal-beta-homoAla-beta-homoLeu and beta-homoAla-beta-homoLeu. {ECO:0000269|PubMed:17064315}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 10. {ECO:0000269|PubMed:17064315}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (2); Signal peptide (1) |
| Keywords | Aminopeptidase;Hydrolase;Periplasm;Protease;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:Q52VH2}. |
| Modified Residue | |
| Post Translational Modification | PTM: Autoproteolytic processing to generate the alpha and beta subunit is required for self-activation and is proposed to use a similar mechanism as substrate cleavage. {ECO:0000250|UniProtKB:Q52VH2}. |
| Signal Peptide | SIGNAL 1..21; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 41,184 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=39 mM for beta-homoVal-beta-homoAla-beta-homoLeu; KM=41 mM for beta-homoAla-beta-homoLeu; KM=4.4 mM for beta-3homoAla-pNA; Vmax=0.84 umol/min/mg enzyme with beta-homoVal-beta-homoAla-beta-homoLeu as substrate; Vmax=3.1 umol/min/mg enzyme with beta-homoAla-beta-homoLeu as substrate; Vmax=0.063 umol/min/mg enzyme with carnosine as substrate {ECO:0000269|PubMed:17064315}; Vmax=0.047 umol/min/mg enzyme with beta-homoGly-Ile-beta-homoTyr as substrate {ECO:0000269|PubMed:17064315}; Vmax=0.45 umol/min/mg enzyme with beta-homoVal-Ile-beta-homoTyr as substrate {ECO:0000269|PubMed:17064315}; Vmax=0.38 umol/min/mg enzyme with beta-homoVal-Ile-beta-homoTyr as substrate {ECO:0000269|PubMed:17064315}; Vmax=0.46 umol/min/mg enzyme with beta-homoPhe-Ile-beta-homoTyr as substrate {ECO:0000269|PubMed:17064315}; Vmax=0.21 umol/min/mg enzyme with beta-homoTyr-Ile-beta-homoTyr as substrate {ECO:0000269|PubMed:17064315}; Vmax=0.040 umol/min/mg enzyme with beta-homoTrp-Ile-beta-homoTyr as substrate {ECO:0000269|PubMed:17064315}; Vmax=0.40 umol/min/mg enzyme with beta-homoSer-Ile-beta-homoTyr as substrate {ECO:0000269|PubMed:17064315}; Vmax=0.050 umol/min/mg enzyme with beta-homoThr-Ile-beta-homoTyr as substrate {ECO:0000269|PubMed:17064315}; Vmax=0.011 umol/min/mg enzyme with beta-homoHis-Ile-beta-homoTyr as substrate {ECO:0000269|PubMed:17064315}; Vmax=0.015 umol/min/mg enzyme with beta-homoLys-Ile-beta-homoTyr as substrate {ECO:0000269|PubMed:17064315}; Vmax=0.011 umol/min/mg enzyme with beta-homoArg-Ile-beta-homoTyr as substrate {ECO:0000269|PubMed:17064315}; Vmax=0.016 umol/min/mg enzyme with D-beta-homoVal-Ile-beta-homoTyr as substrate {ECO:0000269|PubMed:17064315}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.11.25; |