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UniProt functional annotation for Q3T905 | ||
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| UniProt code: Q3T905. |
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| Organism: | |
Helicoverpa zea (Corn earworm moth) (Heliothis zea). |
| Taxonomy: | |
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea; Noctuidae; Heliothinae; Helicoverpa. |
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| Function: | |
Metalloprotease which cleaves a single amino acid from the C- terminal end of polypeptide chains. Shows a strong preference for peptides with a terminal lysine residue. {ECO:0000269|PubMed:16260742}. |
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| Catalytic activity: | |
Reaction=Preferential release of a C-terminal lysine or arginine amino acid.; EC=3.4.17.2; Evidence={ECO:0000269|PubMed:16260742}; |
| Cofactor: | |
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305|PubMed:16260742}; |
| Activity regulation: | |
Highly resistant to inhibition by potato carboxypeptidase inhibitor (PCI). Moderately inhibited by leech carboxypeptidase inhibitor (LCI) and tick carboxypeptidase inhibitor (TCI). {ECO:0000269|PubMed:16260742}. |
| Biophysicochemical properties: | |
Kinetic parameters: KM=0.26 mM for benzoyl-glycyl-lysine (Bz-Gly-Lys) {ECO:0000269|PubMed:16260742}; KM=0.061 mM for N-(4-furylacryloyl)-Ala-Lys (FAAK) {ECO:0000269|PubMed:16260742}; Note=kcat is 45.7 sec(-1) for benzoyl-glycyl-lysine (Bz-Gly-Lys). kcat is 15.3 sec(-1) for N-(4-furylacryloyl)-Ala-Lys (FAAK). {ECO:0000269|PubMed:16260742}; |
| Subcellular location: | |
Secreted {ECO:0000305}. |
| Similarity: | |
Belongs to the peptidase M14 family. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.