Detail Information for IndEnz0002013980
IED ID IndEnz0002013980
Enzyme Type ID protease013980
Protein Name Angiotensin-converting enzyme
ACE
EC 3.2.1.-
EC 3.4.15.1
Dipeptidyl carboxypeptidase I
Kininase II
CD antigen CD143
Fragment
Gene Name ACE DCP1
Organism Bos taurus (Bovine)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Laurasiatheria Artiodactyla Ruminantia Pecora Bovidae Bovinae Bos (oxen cattle) Bos taurus (Bovine)
Enzyme Sequence MGAASGRRSPPLLLPLLLLLLPPPPVILELDPALQPGNFPADEAGAQIFAASFNSSAEQVLFQSTAASWAHDTNITEENARLQEEAALLSQEFSEAWGQK
Enzyme Length 100
Uniprot Accession Number P12820
Absorption
Active Site
Activity Regulation
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;
DNA Binding
EC Number 3.2.1.-; 3.4.15.1
Enzyme Function FUNCTION: Converts angiotensin I to angiotensin II by release of the terminal His-Leu, this results in an increase of the vasoconstrictor activity of angiotensin. Also able to inactivate bradykinin, a potent vasodilator. Has also a glycosidase activity which releases GPI-anchored proteins from the membrane by cleaving the mannose linkage in the GPI moiety (By similarity). {ECO:0000250}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Non-terminal residue (1); Region (1); Signal peptide (1); Topological domain (1)
Keywords Carboxypeptidase;Direct protein sequencing;Hydrolase;Metalloprotease;Protease;Reference proteome;Secreted;Signal;Zinc
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..28; /evidence="ECO:0000269|PubMed:2835538, ECO:0000269|PubMed:3028395"
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 17928627;
Motif
Gene Encoded By
Mass 10,681
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda 3.4.15.1;