| IED ID | IndEnz0002014486 |
| Enzyme Type ID | protease014486 |
| 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 | bapA |
| Organism | Sphingosinicella xenopeptidilytica |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Alphaproteobacteria Sphingomonadales Sphingosinicellaceae Sphingosinicella Sphingosinicella xenopeptidilytica |
| Enzyme Sequence | MTSTQRLWSGALPLLTALIVSIAATASLAGPRARDLGVPFEGTPGALNAITDVAGVEVGHTTVISGDGAMVIGKGPYRTGVTIIHPLGKTSLDGVAAGRAVINGTGEWTGMHLVDEVGQFLGPIALTGTGNVGLVHQSMMDWSVGKVPEEALFSRLLPVVAETLDNRLNDVFGHGLTRDHVFAALDGAKGGPVAEGNVGGGTGMIAYTFKGGIGTSSRVVSAGDTRYTVGVLVQANHGDRNDLRIAGVQIGKEIKGAWPEVNGIVAAGPDAGKPQDKNSLLIVIATDAPLMPHQLERMARRAALGVGRNGSTAGALSGEFALAFSTSHVIPLGGKPRLPAIINDTDSETMNALFRGVVQATEEALVNQLVASETMTGANNAKVYGIPHDQLARIMKARFPRR |
| Enzyme Length | 402 |
| Uniprot Accession Number | Q52VH2 |
| Absorption | |
| Active Site | ACT_SITE 279; /note=Nucleophile; /evidence=ECO:0000303|PubMed:22980995; ACT_SITE 317; /note=Proton donor/acceptor; /evidence=ECO:0000303|PubMed:22980995; ACT_SITE 319; /note=Proton donor/acceptor; /evidence=ECO:0000303|PubMed:22980995 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by AEBSF (4-(2-aminoethyl)benzenesulfonyl fluoride, Pefabloc SC), ampicillin and AMP(hyd) (ampillicin-derived penicilloic acid). {ECO:0000269|PubMed:17064315, ECO:0000269|PubMed:22961926, ECO:0000269|PubMed:22980995}. |
| 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:16109932, ECO:0000269|PubMed:17064315, ECO:0000269|PubMed:22961926, ECO:0000269|PubMed:22980995}; |
| 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. {ECO:0000269|PubMed:16109932, ECO:0000269|PubMed:17064315}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is between 8 and 9. {ECO:0000269|PubMed:17064315}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (13); Chain (2); Helix (13); Mutagenesis (6); Signal peptide (1); Turn (5) |
| Keywords | 3D-structure;Aminopeptidase;Direct protein sequencing;Hydrolase;Periplasm;Protease;Signal |
| Interact With | Itself |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Periplasm {ECO:0000303|PubMed:16109932}. |
| 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:0000303|PubMed:22980995}. |
| Signal Peptide | SIGNAL 1..29; /evidence=ECO:0000269|PubMed:16109932 |
| Structure 3D | X-ray crystallography (5) |
| Cross Reference PDB | 3N2W; 3N33; 3N5I; 3NDV; 3NFB; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 41,531 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=9.0 mM for beta-homoVal-beta-homoAla-beta-homoLeu {ECO:0000269|PubMed:17064315}; KM=20 mM for beta-homoAla-beta-homoLeu {ECO:0000269|PubMed:17064315}; KM=8.2 mM for beta-homoGly-pNA {ECO:0000269|PubMed:17064315}; KM=1.2 mM for beta-homoAla-pNA {ECO:0000269|PubMed:22961926}; Vmax=3.1 umol/min/mg enzyme with beta-homoVal-beta-homoAla-beta-homoLeu as substrate {ECO:0000269|PubMed:17064315}; Vmax=1.1 umol/min/mg enzyme with beta-homoAla-beta-homoLeu as substrate {ECO:0000269|PubMed:17064315}; Vmax=0.026 umol/min/mg enzyme with carnosine as substrate {ECO:0000269|PubMed:17064315}; Vmax=0.98 umol/min/mg enzyme with beta-homoVal-Ile-beta-homoTyr as substrate {ECO:0000269|PubMed:17064315}; Vmax=1.9 umol/min/mg enzyme with beta-homoVal-Ile-beta-homoTyr as substrate {ECO:0000269|PubMed:17064315}; Vmax=0.68 umol/min/mg enzyme with beta-homoPhe-Ile-beta-homoTyr as substrate {ECO:0000269|PubMed:17064315}; Vmax=0.47 umol/min/mg enzyme with beta-homoTyr-Ile-beta-homoTyr as substrate {ECO:0000269|PubMed:17064315}; Vmax=0.047 umol/min/mg enzyme with beta-homoTrp-Ile-beta-homoTyr as substrate {ECO:0000269|PubMed:17064315}; Vmax=0.095 umol/min/mg enzyme with beta-homoSer-Ile-beta-homoTyr as substrate {ECO:0000269|PubMed:17064315}; Vmax=0.068 umol/min/mg enzyme with beta-homoThr-Ile-beta-homoTyr as substrate {ECO:0000269|PubMed:17064315}; Vmax=0.017 umol/min/mg enzyme with beta-homoLys-Ile-beta-homoTyr as substrate {ECO:0000269|PubMed:17064315}; Vmax=0.028 umol/min/mg enzyme with D-beta-homoVal-Ile-beta-homoTyr as substrate {ECO:0000269|PubMed:17064315}; Vmax=16.4 umol/min/mg enzyme with beta-homoAla-pNA as substrate {ECO:0000269|PubMed:22961926}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.11.25; |