Structure and function of human plasma carboxypeptidase N, the anaphylatoxin inactivator.
Human carboxypeptidase N (CPN) was discovered in the early 1960s as a plasma enzyme that inactivates bradykinin and was identified 8 years later as the major "anaphylatoxin inactivator" of blood. CPN plays an important role in protecting the body from excessive buildup of potentially deleterious peptides that normally act as local autocrine or paracrine hormones. This review summarizes the structure, enzymatic properties and function of this important human enzyme, including insights gained by the recent elucidation of the crystal structure of the CPN catalytic subunit and structural modeling of the non-catalytic regulatory 83 kDa subunit. We also discuss its physiological role in cleaving substrates such as kinins, anaphylatoxins, creatine kinase, plasminogen receptors, hemoglobin and stromal cell-derived factor-1alpha (SDF-1alpha).
Department of Pharmacology, University of Illinois at Chicago College of Medicine Chicago, IL 60612, USA. rskidgel@uic.edu
Randal A
RA
Skidgel
Ervin G
EG
Erdös
D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D018360:Crystallography, X-Ray; D006801:Humans; D001121:Lysine Carboxypeptidase / Q000097:blood* / Q000737:chemistry* / Q000235:genetics; D008958:Models, Molecular; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid; D013329:Structure-Activity Relationship
D001121:Lysine Carboxypeptidase