| IED ID | IndEnz0002010460 |
| Enzyme Type ID | protease010460 |
| Protein Name |
L-amino acid amidase EC 3.5.1.101 |
| Gene Name | laaA |
| Organism | Pseudomonas azotoformans |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Pseudomonadales Pseudomonadaceae Pseudomonas Pseudomonas fluorescens group (fluorescent pseudomonads) Pseudomonas azotoformans |
| Enzyme Sequence | MEFIEKIREGYAAFGAYQTWYRVTGDLSSGRTPLVVIHGGPGCTHDYVDAFKDVAASGHAVIHYDQLGNGRSTHLPDKDPSFWTVGLFLEELNNLLDHLQISDNYAILGQSWGGMLGSEHAILQPKGLRAFIPANSPTCMRTWVSEANRLRKLLPEGVHETLLKHETAGTYQDPEYLAASRVFYDHHVCRVIPWPEEVARTFAAVDADPTVYHAMSGPTEFHVIGSLKDWKSTGRLSAINVPTLVISGRHDEATPLVVKPFLDEIADVRWALFEDSSHMPHVEERQACMGTVVKFLDEVCSAKYKVLKAS |
| Enzyme Length | 310 |
| Uniprot Accession Number | Q76KX0 |
| Absorption | |
| Active Site | ACT_SITE 111; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 251; /evidence=ECO:0000250; ACT_SITE 278; /note=Proton donor; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Completely inhibited by ZnSO(4), ZnCl(2), AgNO(3), CdCl(2) and HgCl(2). Partially inhibited by PbCl(2), NiCl(2) and CoCl(2). Unaffected by LiBr, H(2)BO(3), NaCl, MgSO(4), AlCl(3), KCl, CaCl(2), CrCl(3), MnCl(2), FeSO(4), Fe(NH(4))(2)(SO(4))(2), CuSO(4), RbCl, Na(2)MoO(4), (NH(4))(6)Mo(7)O(24), SnCl(2), CsCl and BaCl(2). Completely inhibited by phenylhydrazine, but not by the other carbonyl reagents hydroxylamine, hydrazine, D,L-penicillamine and D-cycloserine. Unaffected by the chelating agents o-phenanthroline, 8-hydroxyquinoline, enthylenediaminetetraacetic acid and alpha,alpha'-dipyridyl. Partially inhibited by the thiol reagents p-chloromercuribenzoate, iodoacetate and N-ethylmaleimide. Not affected by the serine protease inhibitor phenylmethanesulfonyl fluoride, the serine/cysteine protease inhibitor leupeptine or the aspartic protease inhibitor pepstatin. {ECO:0000269|PubMed:15066172}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=(S)-piperazine-2-carboxamide + H2O = (S)-piperazine-2-carboxylate + NH4(+); Xref=Rhea:RHEA:26550, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:58919, ChEBI:CHEBI:58920; EC=3.5.1.101; Evidence={ECO:0000269|PubMed:15066172}; CATALYTIC ACTIVITY: Reaction=H2O + L-prolinamide = L-proline + NH4(+); Xref=Rhea:RHEA:26510, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:58495, ChEBI:CHEBI:60039; EC=3.5.1.101; Evidence={ECO:0000269|PubMed:15066172}; |
| DNA Binding | |
| EC Number | 3.5.1.101 |
| Enzyme Function | FUNCTION: Hydrolyzes L-prolinamide, L-proline-p-nitroanilide, L-alaninamide, L-methioninamide, piperidine-2-carboxamide and piperazine-2-carboxamide. Has a much lower activity towards piperazine-2-tert-butylcarboxamide. Does not hydrolyze dipeptides and D-prolinamide. {ECO:0000269|PubMed:15066172}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45 degrees Celsius, activity decreases rapidly above 45 degrees Celsius possibly due to instability at higher temperatures. Inactivated following 5 minutes incubation at 55 degrees Celsius, and only retains 25% of activity after 5 minutes incubation at 50 degrees Celsius. {ECO:0000269|PubMed:15066172}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0. Stable from pH 6.0 to 9.5. {ECO:0000269|PubMed:15066172}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Domain (1) |
| Keywords | Direct protein sequencing;Hydrolase |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 34,514 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.58 mM for L-proline-p-nitroanilide {ECO:0000269|PubMed:15066172}; Vmax=80.9 umol/min/mg enzyme with L-proline-p-nitroanilide as substrate {ECO:0000269|PubMed:15066172}; |
| Metal Binding | |
| Rhea ID | RHEA:26550; RHEA:26510 |
| Cross Reference Brenda | 3.5.1.101; |