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

Differentiation of cartilage from precartilage mesenchyme in the chick embryo is accompanied by the loss of two abundant nonhistone proteins (Mr 35 500 and 125 000) termed PCP 35.5 and PCP 125. Here we examine the distribution of these and other developmentally regulated nonhistones in nuclease-sensitive regions of precartilage and cartilage chromatin. In particular, we show that PCP 35.5 is a tight DNA-binding protein that is localized near deoxyribonuclease I (DNase I) sensitive regions of precartilage chromatin. Localization of nonhistones was demonstrated by excising domains of precartilage chromatin with DNase II which are simultaneously highly enriched in PCP 35.5, in PCP 125, and DNase I sensitive DNA sequences. These domains comprise at least 25% of the cell's DNase I sensitive sequences, as well as small DNase I resistant regions with which the two nonhistones are associated. These findings suggest that PCP 35.5 (and possibly PCP 125) may play a developmentally regulated role nearby DNase I sensitive domains of the cartilage progenitor cell chromatin.
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PMID:Developmentally regulated nonhistone proteins: evidence for deoxyribonucleic acid binding role and localization near deoxyribonuclease I sensitive domains of precartilage cell chromatin. 628 99

Decomposing proteins into "molegos," building blocks that are conserved in sequence and 3D-structure, can identify functional elements. To demonstrate the specificity of the decomposition method, the PCPMer program suite was used to numerically define physical chemical property motifs corresponding to the molegos that make up the metal-containing active sites of three distinct enzyme families, from the dimetallic phosphatases, DNase 1 related nucleases/phosphatases, and dioxygenases. All three superfamilies bind metal ions in a beta-strand core region but differ in the number and type of ions needed for activity. The motifs were then used to automatically identify proteins in the ASTRAL40 database that contained similar motifs. The proteins with the highest PCPMer score in the database were primarily metal-binding enzymes that were related in function to those in the alignment used to generate the PCPMer motif lists. The proteins that contained motifs similar to the dioxygenases differed from those found with PCP-motifs for phosphatases and nucleases. Relatively few metal-binding enzymes were detected when the search was done with PCP-motifs defined for interleukin-1 related proteins, which have a beta-strand core but do not bind metal ions. While the box architecture was constant in each superfamily, the specificity for the metal ion preferred for enzymatic activity is determined by the pattern of carbonyl, hydroxyl or imadazole groups in key positions in the molegos. These results have implications for the design of metal-binding enzymes, and illustrate the ability of the PCPMer approach to distinguish, at the sequence level, structural and functional elements.
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PMID:Molego-based definition of the architecture and specificity of metal-binding sites. 1550 85