Aminopeptidase B (EC 3.4.11.6).
Aminopeptidase B (EC 3.4.11.6) is a Zn(2+)-dependent exopeptidase which selectively removes arginine and/or lysine residues from the NH2-terminus of several peptide substrates including Arg0-Leu-enkephalin, Arg0-Met-enkephalin and Arg-1-Lys0-somatostatin-14. Analysis of its primary structure showed that aminopeptidase-B is structurally related to leukotriene A4 hydrolase, an important enzyme of the arachidonic acid pathway. This structural relationship is further supported by the capacity of aminopeptidase-B to hydrolyse leukotriene A4. Aminopeptidase-B is widely distributed in a number of tissues, including endocrine and non-endocrine cells. Moreover, in rat PC12 pheochromocytoma cells, the enzyme is secreted and associated with the external face of the plasma membrane. Together these data strongly argue in favour of a role of this bi-functional enzyme in the final stages of precursor processing mechanisms occurring either in the secretory pathway, at the plasma membrane, or at both locations.
Foulon
T
T
Laboratoire de Biochimie des Signaux Régulateurs Cellulaires et Moléculaires, Université Pierre et Marie Curie, Paris, France. foulon@ccr.jussieu.fr
Cadel
S
S
Cohen
P
P
D000595:Amino Acid Sequence; D000626:Aminopeptidases / Q000737:chemistry* / Q000235:genetics / Q000502:physiology*; D000818:Animals; D001120:Arginine / Q000378:metabolism; D004851:Epoxide Hydrolases / Q000737:chemistry / Q000235:genetics; D006801:Humans; D008239:Lysine / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D051381:Rats
D001120:Arginine; D004851:Epoxide Hydrolases; D000626:Aminopeptidases; C019721:aminopeptidase B; D008239:Lysine; C043134:leukotriene A4 hydrolase