Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.16.2 (PCP)
 3,761 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

After gel filtration the supernatant of Triton X-100 treated membrane sediments of Acinetobacter calcoaceticus shows activities for alanyl aminopeptidase, leucyl aminopeptidase, glutamyl aminopeptidase, prolyl aminopeptidase, aminopeptidase My, gamma-glutamyl arylamidase, dipeptidylpeptidase IV and prolyl carboxypeptidase. The intracellular localization of the enzymes was analyzed by sucrose density gradient centrifugation of the DNase/RNase pretreated membrane sediments. Most of the exopeptidases are located in the inner membrane fractions (band L). Only gamma-glutamyl arylamidase is located with its main activity in the cytoplasmic membrane (band M). Only small exopeptidase activities could be found in the outer membrane (band H).
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PMID:[Identification and localization of exopeptidase activities bound to membranes of Acinetobacter calcoaceticus]. 269 71

In spite of the numerous studies regarding prolyl aminopeptidase, little is known about its mechanism and the significance of its similarity to a number of hydrolases of diverse specificity that belong to the alpha/beta hydrolase-fold family (Pseudomonas 2-hydroxymuconic semialdehyde hydrolase, atropinesterase, and 2-hydroxy-6-oxophenylhexa-2,4-dienoic acid hydrolase; human and rat epoxide hydrolases). We report the cloning and sequencing of the novel prolyl aminopeptidase gene from Flavobacterium meningosepticum (FPAP) which allowed a more comprehensive sequence comparison. FPAP was found to be a 35-kDa monomeric enzyme, releasing N-terminal proline but not hydroxyproline residues from small peptides and naphthylamide esters. Using the unweighted pair group method with arithmetic mean method, an evolutionary tree that depicts the probable relationship between the prolyl aminopeptidases and the alpha/beta hydrolase-fold enzymes was constructed. Since the alpha/beta hydrolase-fold family might also include the members of the prolyl oligopeptidase family (prolyl oligopeptidase, dipeptidyl peptidase IV, and prolyl carboxypeptidase), this proposal links all the known Pro-Y bond-cleaving proline-specific peptidases (prolyl oligopeptidase family, prolyl aminopeptidases, and prolinase) as enzymes with similar scaffolds and hydrolytic mechanisms. On the other hand, the enzymes that cleave X-Pro bonds are metalloenzymes grouped within the "pita-bread" fold family (aminopeptidase P and prolidase). Although the latter two enzymes show significant sequence homology, prolyl aminopeptidase, prolinase, and the members of the prolyl oligopeptidase family do not, and might share the alpha/beta hydrolase-fold scaffold. This rationale would explain the failure in finding a common "proline-recognizing motif" in the primary structures of these proline-specific peptidases.
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PMID:Prolyl aminopeptidase gene from Flavobacterium meningosepticum: cloning, purification of the expressed enzyme, and analysis of its sequence. 895 Oct 32