gopubmed logo
find other proteinsAll proteins
GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

CNDP dipeptidase 2

cytosolic nonspecific dipeptidase
Top mentioned proteins: ACID, PAP, Prolactin, metalloprotease, fibrillin-1
Papers on cytosolic nonspecific dipeptidase
N-lactoyl-amino acids are ubiquitous metabolites that originate from CNDP2-mediated reverse proteolysis of lactate and amino acids.
van de Wetering et al., Amsterdam, Netherlands. In Proc Natl Acad Sci U S A, Jun 2015
Using parallel protein fractionation in conjunction with shotgun proteomics on fractions containing N-lactoyl-Phe-forming activity, we unexpectedly found that a protease, cytosolic nonspecific dipeptidase 2 (CNDP2), catalyzes their formation.
Proteomic analysis of seminal plasma in men with different spermatogenic impairment.
Plaseska-Karanfilska et al., Скопје, Macedonia. In Andrologia, 2012
The differentially expressed spots were fibronectin, prostatic acid phosphatase (PAP), proteasome subunit alpha type-3, beta-2-microglobulin, galectin-3-binding protein, prolactin-inducible protein and cytosolic nonspecific dipeptidase.
Purification and identification of a novel primitive secretory enzyme catalyzing the hydrolysis of imidazole-related dipeptides in the jawless vertebrate Lethenteron reissneri.
Yamada et al., Kagoshima, Japan. In Peptides, 2011
All of the known enzymes that catalyze the hydrolysis of these dipeptides belong to the M20A metallopeptidase subfamily; two secretory enzymes, serum carnosinase (EC and anserinase (EC, and one non-secretory enzyme, cytosolic nonspecific dipeptidase (EC
Purification and sequence identification of anserinase.
Ando et al., Kagoshima, Japan. In Febs J, 2005
Sequence analysis showed that anserinase is a member of the M20A metallopeptidase subfamily in MEROPS peptidase database, to which 'serum' carnosinase (EC and cytosolic nonspecific dipeptidase (EC,
Sequence identification and characterization of human carnosinase and a closely related non-specific dipeptidase.
Smirnova et al., Strasbourg, France. In J Biol Chem, 2003
Based on their substrate specificity and biophysical and biochemical properties CN1 was identified as human carnosinase (EC ), whereas CN2 corresponds to the cytosolic nonspecific dipeptidase (EC ).
share on facebooktweetadd +1mail to friends