gopubmed logo
 
find other proteinsAll proteins
GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 08 Dec 2016.

Dipeptidyl-peptidase 3

dipeptidyl peptidase III, DPP III, dipeptidyl aminopeptidase III
This gene encodes a protein that is a member of the M49 family of metallopeptidases. This cytoplasmic protein binds a single zinc ion with its zinc-binding motif (HELLGH) and has post-proline dipeptidyl aminopeptidase activity, cleaving Xaa-Pro dipeptides from the N-termini of proteins. Increased activity of this protein is associated with endometrial and ovarian cancers. Alternatively spliced transcript variants have been found for this gene. [provided by RefSeq, Feb 2012] (from NCBI)
Top mentioned proteins: DSP, aminopeptidase, ACID, Enkephalin, HAD
Papers on dipeptidyl peptidase III
Prominent role of exopeptidase DPP III in estrogen-mediated protection against hyperoxia in vivo.
New
Balog et al., Zagreb, Croatia. In Redox Biol, Feb 2016
In particular, we investigate the E2-induced expression and cellular distribution of DPP III monozinc exopeptidase, a member of the Nrf-2/Keap-1 pathway, upon hyperoxia treatment.
Molecular simulations reveal that the long range fluctuations of human DPP III change upon ligand binding.
New
Tomić et al., Zagreb, Croatia. In Mol Biosyst, Nov 2015
The experimentally determined structures of human dipeptidyl peptidase III (DPP III) for the wild-type protein and for the complex of its E451A mutant with the peptide substrate, tynorphin, differ significantly in their overall shape.
Aspartate 496 from the subsite S2 drives specificity of human dipeptidyl peptidase III.
New
Jajčanin-Jozić et al., In Biol Chem, Apr 2015
Human dipeptidyl peptidase III (hDPP III) is a member of the M49 metallopeptidase family, which is involved in intracellular protein catabolism and oxidative stress response.
The effect of 17β-estradiol on the expression of dipeptidyl peptidase III and heme oxygenase 1 in liver of CBA/H mice.
New
Abramić et al., Zagreb, Croatia. In J Endocrinol Invest, Apr 2015
Dipeptidyl peptidase III (DPP III) is protease involved as activator in Keap1-Nrf2 signalling pathway, which is important in cellular defense to oxidative and electrophilic stress.
Synthesis, QSAR, and Molecular Dynamics Simulation of Amidino-substituted Benzimidazoles as Dipeptidyl Peptidase III Inhibitors.
Abramić et al., In Acta Chim Slov, 2014
A molecular modeling study is performed on series of benzimidazol-based inhibitors of human dipeptidyl peptidase III (DPP III).
Hunting the human DPP III active conformation: combined thermodynamic and QM/MM calculations.
Tomić et al., Zagreb, Croatia. In Dalton Trans, 2014
We used three different conformations of human dipeptidyl-peptidase III (DPP III) to investigate the influence of the protein environment on ligand binding and the Zn(2+) coordination.
Transcription factor C/EBP-β mediates downregulation of dipeptidyl-peptidase III expression by interleukin-6 in human glioblastoma cells.
Chauhan et al., New Delhi, India. In Febs J, 2014
Dipeptidyl-peptidase III (DPP III) is a cytosolic metallo-aminopeptidase implicated in various physiological and pathological processes.
Importance of the three basic residues in the vicinity of the zinc-binding motifs for the activity of the yeast dipeptidyl peptidase III.
Abramić et al., Zagreb, Croatia. In J Biochem, 2014
Yeast dipeptidyl peptidase III (yDPP III) is a member of the metallopeptidase family M49 involved in intracellular protein catabolism.
[Coordination chemical studies on the zinc enzymes].
Review
Hirose, Fukuyama, Japan. In Yakugaku Zasshi, 2013
The metal dissociation constants of bovine carbonic anhydrase II, bovine carboxypeptidase A, rat aminopeptidase B, and rat dipeptidyl peptidase III were measured using metal buffer solutions.
Hydrolysis of dipeptide derivatives reveals the diversity in the M49 family.
Abramić et al., Zagreb, Croatia. In Biol Chem, 2013
Dipeptidyl peptidase III, a metallopeptidase of the M49 family, was first identified (in the pituitary) by its specific cleavage of diarginyl arylamides, which have been used as preferred assay substrates until now.
Molecular determinants of human dipeptidyl peptidase III sensitivity to thiol modifying reagents.
Abramić et al., Zagreb, Croatia. In Biol Chem, 2012
Human dipeptidyl peptidase III (DPP III) is a member of the metallopeptidase family M49, involved in protein metabolism and oxidative stress response.
Effects of conversion of the zinc-binding motif sequence of thermolysin, HEXXH, to that of dipeptidyl peptidase III, HEXXXH, on the activity and stability of thermolysin.
Inouye et al., Kyoto, Japan. In Biosci Biotechnol Biochem, 2012
The zinc-binding motif sequence of thermolysin, H(142)ELTH(146), belongs to this motif sequence, while that of dipeptidyl peptidase III (DPP III), H(450)ELLGH(455), belongs to the motif sequence HEXXXH.
Entropy-driven binding of opioid peptides induces a large domain motion in human dipeptidyl peptidase III.
GeneRIF
Gruber et al., Graz, Austria. In Proc Natl Acad Sci U S A, 2012
results provide the basis for the design of specific inhibitors that enable the elucidation of the exact role of DPP III and the exploration of its potential as a target of pain intervention strategies
Dipeptidyl peptidase III: a multifaceted oligopeptide N-end cutter.
Review
Chauhan et al., New Delhi, India. In Febs J, 2011
Dipeptidyl peptidase III (DPP III), the sole member and representative of the M49 family of metallopeptidases, is a zinc-dependent aminopeptidase.
Ets-1/Elk-1 is a critical mediator of dipeptidyl-peptidase III transcription in human glioblastoma cells.
GeneRIF
Chauhan et al., New Delhi, India. In Febs J, 2010
Ets-1/Elk-1 is a critical mediator of DPP3 transcription in human glioblastoma cells.
Neuropeptidases and the metabolic inactivation of insect neuropeptides.
Review
Shirras et al., Leeds, United Kingdom. In Gen Comp Endocrinol, 2009
It focuses on five neuropeptidase families (neprilysin, dipeptidyl-peptidase IV, angiotensin-converting enzyme, aminopeptidase and dipeptidyl aminopeptidase III) that have been implicated in the metabolic inactivation of neuropeptides in the central nervous system of insects.
Functional tyrosine residue in the active center of human dipeptidyl peptidase III.
GeneRIF
Abramić et al., Zagreb, Croatia. In Biol Chem, 2008
the conserved tyrosine could be involved in transition state stabilization during the catalytic action of M49 peptidases.
Tumor cytosol dipeptidyl peptidase III activity is increased with histological aggressiveness of ovarian primary carcinomas.
GeneRIF
Abramić et al., Zagreb, Croatia. In Gynecol Oncol, 2003
In malignant neoplasms of the ovary DPP III activity increased with growing histologic grade.
Spinorphin as an endogenous inhibitor of enkephalin-degrading enzymes: roles in pain and inflammation.
Review
Hazato et al., Tokyo, Japan. In Curr Protein Pept Sci, 2002
It has been found that spinorphin inhibited the activity toward various enkephalin-degrading enzymes from monkey brain, especially dipeptidyl peptidase III (DPPIII, Ki=5.1 x 10(-7) M).
share on facebooktweetadd +1mail to friends