Detail Information for IndEnz0002016761
IED ID IndEnz0002016761
Enzyme Type ID protease016761
Protein Name Aminopeptidase N
AP-N
EC 3.4.11.2
CryIA
C
receptor
Fragment
Gene Name
Organism Helicoverpa armigera (Cotton bollworm) (Heliothis armigera)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Amphiesmenoptera Lepidoptera (butterflies and moths) Glossata Neolepidoptera Heteroneura Ditrysia Obtectomera Noctuoidea Noctuidae (owlet moths) Heliothinae Helicoverpa Helicoverpa armigera (Cotton bollworm) (Heliothis armigera)
Enzyme Sequence GMYTHEGSDP
Enzyme Length 10
Uniprot Accession Number P81731
Absorption
Active Site
Activity Regulation ACTIVITY REGULATION: Inhibited by the zinc-chelators 2,2-dipyridyl and 1,10-phenanthroline. {ECO:0000269|PubMed:11683359}.
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide.; EC=3.4.11.2; Evidence={ECO:0000269|PubMed:11683359};
DNA Binding
EC Number 3.4.11.2
Enzyme Function FUNCTION: Acts as a receptor for B.thuringiensis Cry1Ac delta-endotoxin. {ECO:0000269|PubMed:11683359}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Non-terminal residue (1)
Keywords Aminopeptidase;Direct protein sequencing;Hydrolase;Metalloprotease;Protease;Zinc
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 1,093
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda