Detail Information for IndEnz0002018838
IED ID IndEnz0002018838
Enzyme Type ID protease018838
Protein Name Carboxypeptidase M
CPM
EC 3.4.17.12
Gene Name CPM
Organism Homo sapiens (Human)
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 Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human)
Enzyme Sequence MDFPCLWLGLLLPLVAALDFNYHRQEGMEAFLKTVAQNYSSVTHLHSIGKSVKGRNLWVLVVGRFPKEHRIGIPEFKYVANMHGDETVGRELLLHLIDYLVTSDGKDPEITNLINSTRIHIMPSMNPDGFEAVKKPDCYYSIGRENYNQYDLNRNFPDAFEYNNVSRQPETVAVMKWLKTETFVLSANLHGGALVASYPFDNGVQATGALYSRSLTPDDDVFQYLAHTYASRNPNMKKGDECKNKMNFPNGVTNGYSWYPLQGGMQDYNYIWAQCFEITLELSCCKYPREEKLPSFWNNNKASLIEYIKQVHLGVKGQVFDQNGNPLPNVIVEVQDRKHICPYRTNKYGEYYLLLLPGSYIINVTVPGHDPHITKVIIPEKSQNFSALKKDILLPFQGQLDSIPVSNPSCPMIPLYRNLPDHSAATKPSLFLFLVSLLHIFFK
Enzyme Length 443
Uniprot Accession Number P14384
Absorption
Active Site ACT_SITE 281; /note=Proton donor/acceptor; /evidence=ECO:0000305|PubMed:12457462
Activity Regulation ACTIVITY REGULATION: Inhibited by O-phenanthroline and MGTA and activated by cobalt.
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Cleavage of C-terminal arginine or lysine residues from polypeptides.; EC=3.4.17.12; Evidence={ECO:0000269|PubMed:12457462};
DNA Binding
EC Number 3.4.17.12
Enzyme Function FUNCTION: Specifically removes C-terminal basic residues (Arg or Lys) from peptides and proteins. It is believed to play important roles in the control of peptide hormone and growth factor activity at the cell surface, and in the membrane-localized degradation of extracellular proteins. {ECO:0000269|PubMed:12457462}.
Temperature Dependency
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. {ECO:0000269|PubMed:12457462};
Pathway
nucleotide Binding
Features Active site (1); Beta strand (18); Chain (1); Disulfide bond (3); Glycosylation (5); Helix (13); Lipidation (1); Metal binding (3); Mutagenesis (5); Natural variant (2); Propeptide (1); Signal peptide (1); Site (1); Turn (5)
Keywords 3D-structure;Carboxypeptidase;Cell membrane;Direct protein sequencing;Disulfide bond;GPI-anchor;Glycoprotein;Hydrolase;Lipoprotein;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Signal;Zinc
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12457462}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:12457462}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..17; /evidence="ECO:0000269|PubMed:12457462, ECO:0000269|PubMed:2753907"
Structure 3D X-ray crystallography (1)
Cross Reference PDB 1UWY;
Mapped Pubmed ID 11072085; 11891060; 18187413; 18292211; 18617639; 19820690; 20360068; 20673876; 20711500; 21278420; 21454694; 22106087; 22157720; 23172796; 24108126; 2443973; 26496610; 28186967; 2914904; 30674606; 31218444; 3422494; 8635221; 8796265;
Motif
Gene Encoded By
Mass 50,514
Kinetics BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=59 uM for synthetic dansyl-Ala-Arg {ECO:0000269|PubMed:12457462}; KM=57 uM for placental peptide hormones {ECO:0000269|PubMed:12457462};
Metal Binding METAL 83; /note="Zinc; catalytic"; /evidence="ECO:0000269|PubMed:15066430, ECO:0007744|PDB:1UWY"; METAL 86; /note="Zinc; catalytic"; /evidence="ECO:0000269|PubMed:15066430, ECO:0007744|PDB:1UWY"; METAL 190; /note="Zinc; catalytic"; /evidence="ECO:0000269|PubMed:15066430, ECO:0007744|PDB:1UWY"
Rhea ID
Cross Reference Brenda 3.4.17.12;