| IED ID | IndEnz0002002921 |
| Enzyme Type ID | protease002921 |
| Protein Name |
Leupeptin-inactivating enzyme 1 LIE1 EC 3.4.24.- |
| Gene Name | lieA |
| Organism | Streptomyces exfoliatus (Streptomyces hydrogenans) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Streptomycetales Streptomycetaceae Streptomyces Streptomyces exfoliatus (Streptomyces hydrogenans) |
| Enzyme Sequence | MSLSVSRRLAAVTAFAVAGLFASAVPAALAAPSAVAAAPTPPDIPLANVKAHLSQLSTIAANNGGNRAHGRAGYKASIDYVKGKLDAAGFTTTLQTFTSSGATGYNLIADWPGGDPNSVLMAGSHLDSVTSGAGINDNGSGSAAVLETALAVSRAGLQPTKHLRFGWWGAEELGLIGSKYYVNNLPAAEKAKISGYLNFDMIGSPNPGYFVYDDDPTIEQTFKNYYAGLGVPTEIETEGDGRSDHAPFKNAGIPVGGLFSGADYTKTAAQAQKWGGTSGQAFDRCYHSSCDSLTNINDTALDRNSDAVAYAIWTLGAGTPVPPGQSFENTADVNVPDSPAAAVSSPITVSGVTGNAPATTKVDVNIVHTYRGDLVVDLVAPDGTVYNLHNRSGGSADNLVQTYTVNASSEVANGVWNLRVKDTAAQDVGYINSWKITF |
| Enzyme Length | 438 |
| Uniprot Accession Number | P81715 |
| Absorption | |
| Active Site | ACT_SITE 171; /note=Proton acceptor; /evidence=ECO:0000250|UniProtKB:P80561 |
| Activity Regulation | ACTIVITY REGULATION: Activity is inhibited by metalloprotease inhibitors and activated by Mg(2+) and Ca(2+). |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: A leucine-specific metalloprotease that plays a role in controlling the amount of leupeptin during colony development. Degrades leupeptin into three components, acetyl-leucine, leucine and argininal. Has a strict preference for leucine at the P1 site. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius.; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0.; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (1); Domain (1); Metal binding (6); Sequence conflict (1); Signal peptide (1); Site (1) |
| Keywords | Calcium;Direct protein sequencing;Disulfide bond;Hydrolase;Metal-binding;Metalloprotease;Protease;Secreted;Signal;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..37; /evidence=ECO:0000269|PubMed:9531495 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 45,302 |
| Kinetics | |
| Metal Binding | METAL 125; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:P80561; METAL 137; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:P80561; METAL 137; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P80561; METAL 172; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P80561; METAL 200; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:P80561; METAL 287; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P80561 |
| Rhea ID | |
| Cross Reference Brenda |