Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.24.11 (CD10)
 9,792 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Exopeptidases identified as dipeptidyl peptidase III and leucine aminopeptidase, and an endopeptidase, prolyl endopeptidase, were found in the Emory Mouse cataract and the Cataract Resistant mouse lens extracts. The specific activity measured on Arg-Arg-2-NNap for DPP III and the hydrolysis of Boc-Arg-Pro-2-NNap for prolyl endopeptidase were higher in the Emory Mouse cataractous lens extract. A relatively high rate of hydrolysis of the beta-naphthylamide of leucine aminopeptidase was present in both mouse categories; however, the Cataract Resistant mouse lens had approximately double the protease activity of the Emory Mouse cataract.
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PMID:Proteases in the Emory mouse cataract. 389 68

A partial purification of dipeptidyl peptidase III has been achieved from human cataractous lens. The specific activity was increased 45.5-fold over that of the original aqueous extract. The exopeptidase exhibited a marked preference for the release of Arg-Arg from Arg-Arg-2-NNap at the optimum pH 8.8 and 37 degrees. The Km for this substrate was estimated to be 6.061 X 10(-3). Lens DPP III was inhibited by EDTA, p-chloromercuriphenyl sulfonate, puromycin and DFP. The preparation contained leucyl aminopeptidase and a neutral endopeptidase as contaminating proteases.
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PMID:Dipeptidyl peptidase III of human cataractous lenses. Partial purification. 636 31

Dipeptidyl-peptidases III (DPP III) are zinc-dependent enzymes that specifically cleave the first two amino acids from the N terminus of different length peptides. In mammals, DPP III is associated with important physiological functions and is a potential biomarker for certain types of cancer. Here, we present the 1.95-A crystal structure of yeast DPP III representing the prototype for the M49 family of metallopeptidases. It shows a novel fold with two domains forming a wide cleft containing the catalytic metal ion. DPP III exhibits no overall similarity to other metallopeptidases, such as thermolysin and neprilysin, but zinc coordination and catalytically important residues are structurally conserved. Substrate recognition is accomplished by a binding site for the N terminus of the peptide at an appropriate distance from the metal center and by a series of conserved arginine residues anchoring the C termini of different length substrates.
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PMID:The first structure of dipeptidyl-peptidase III provides insight into the catalytic mechanism and mode of substrate binding. 1855 May 18

Almost all naturally occurring metalloproteases are monozinc enzymes. The zinc in any number of zinc metalloproteases has been substituted by some other divalent cation. Almost all Co(II)- or Mn(II)-substituted enzymes maintain the catalytic activity of their zinc counterparts. However, in the case of Cu(II) substitution of zinc proteases, a great number of enzymes are not active, for example, thermolysin, carboxypeptidase A, endopeptidase from Lactococcus lactis, or aminopeptidase B, while some do have catalytic activity, for example, astacin (37%) and DPP III (100%). Based on structural studies of various metal-substituted enzymes, for example, thermolysin, astacin, aminopeptidase B, dipeptidyl peptidase (DPP) III, and del-DPP III, the metal coordination geometries of both active and inactive Cu(II)-substituted enzymes are shown to be the same as those of the wild-type Zn(II) enzymes. Therefore, the enzyme activity of a copper-ion-substituted zinc metalloprotease may depend on the flexibility of catalytic domain.
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PMID:Metal preferences of zinc-binding motif on metalloproteases. 2231 63

The main aim of this work was to find parameters for the zinc ion in human dipeptidyl peptidase III (DPP III) active site that would enable its reliable modeling. Since the parameters publicly available failed to reproduce the zinc ion coordination in the enzyme, we developed a new set of the hybrid bonded/nonbonded parameters for the zinc ion suitable for molecular modeling of the human DPP III, dynamics, and ligand binding. The parameters allowed exchange of the water molecules coordinating the zinc ion and proved to be robust enough to enable reliable modeling not only of human DPP III and its orthologues but also of the other zinc-dependent peptidases with the zinc ion coordination similar to that in dipeptidyl peptidases III, i.e., peptidases with the zinc ion coordinated with two histidines and one glutamate. The new parameters were tested on a set of 21 different systems comprising 8 different peptidases, 5 DPP III orthologues, thermolysin, neprilysin, and aminopeptidase N, and the results are summarized in the second part of the article.
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PMID:New Zinc Ion Parameters Suitable for Classical MD Simulations of Zinc Metallopeptidases. 3127 4