Detail Information for IndEnz0002016529
IED ID IndEnz0002016529
Enzyme Type ID protease016529
Protein Name Angiotensin-converting enzyme
EC 3.4.15.1
Dipeptidyl carboxypeptidase I
Kininase II
TtACE
Gene Name ACE
Organism Theromyzon tessulatum (Duck leech)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Spiralia Lophotrochozoa Annelida Clitellata Hirudinea (leeches) Rhynchobdellida Glossiphoniidae Theromyzon Theromyzon tessulatum (Duck leech)
Enzyme Sequence MNLINFSYLNLLFGAGLFSVLESATILNTESDAKKWLTTYNDEAGKYIYDATEAEWNYNTNLTDHNLGISIKKSNDLATFTEQKAIEANKKFVWKNFTDPLLKREFSKITDIGTASLSDEDFQKMSGLNSDLTKIYSTAKVCNKPNDPSGKCYPLDPDLSDIISKSNDLEELTWAWKGWRDASGKHMPDKYDEFVQLLNKAANINGYEDNGDYWRSWYESPTFRKDCEDLWQEIKPFYEQLHAYVRRKLQKKYPQIAFPKEGHIPAHLLGNMWAQSWENIEYLLRPAPDLPSMDITEELVKQNYTALKLFQLSDTFFKSLGLIQMPQPFWEKSMIEKPADRDVVCHASAWDFYNRKDFRIKQCTVVDMHWFMTTHHEMGHIEYYLHYKDQPISFRSGANPGFHEAIADIASLSVATPEYMQSVSLLPNFTDDPNGDLNFLMNQALTKVAFLPFGYLIDQWRWDVFSGDTPRPKYNSKWWHNRCKYQGVYPPVIRSEQDFDAGSKFHVPNNTPYIRYFVAHIIQFQFHEALCKAANNSRPLHRCNIANSKEAGKKLAELMKSGSSIPWPKVLENLTGSEKMSAKSLMAYYKPLIDWPEKRKPRAENWMGGKMSSWIV
Enzyme Length 616
Uniprot Accession Number Q6Q4G4
Absorption
Active Site ACT_SITE 377; /evidence=ECO:0000250
Activity Regulation ACTIVITY REGULATION: Activated by chloride. Inhibited by captopril and lisinopril, and to a lesser extent by delaprilat. {ECO:0000269|PubMed:15175004}.
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Release of a C-terminal dipeptide, oligopeptide-|-Xaa-Yaa, when Xaa is not Pro, and Yaa is neither Asp nor Glu. Thus, conversion of angiotensin I to angiotensin II, with increase in vasoconstrictor activity, but no action on angiotensin II.; EC=3.4.15.1; Evidence={ECO:0000269|PubMed:15175004};
DNA Binding
EC Number 3.4.15.1
Enzyme Function
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Chain (1); Glycosylation (6); Metal binding (2); Signal peptide (1)
Keywords Carboxypeptidase;Glycoprotein;Hydrolase;Metal-binding;Metalloprotease;Protease;Secreted;Signal;Zinc
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000305}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..23; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 71,481
Kinetics
Metal Binding METAL 376; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 380; /note=Zinc; catalytic; /evidence=ECO:0000250
Rhea ID
Cross Reference Brenda