Results 11 to 20 of about 3,066 (177)

Real-time FRET assay for monitoring detyrosination by TMCP1 and VASH2. [PDF]

Protein Sci
Abstract Tubulin detyrosination is an important α‐tubulin specific posttranslational modification which has been implicated in various disorders including neurodegeneration and cancer. As such, the enzymes involved in the generation of this modification emerged as promising therapeutic targets.
Simon M, Espeut J, Juge F, Amblard M, Rogowski K, Vezenkov L.   +5 more
europepmc   +2 more sources

D-Arg0-Bradykinin-Arg-Arg, a Latent Vasoactive Bradykinin B2 Receptor Agonist Metabolically Activated by Carboxypeptidases

Frontiers in Pharmacology, 2018
We previously reported hypotensive and vasodilator effects from C-terminally extended bradykinin (BK) sequences that behave as B2 receptor (B2R) agonists activated by vascular or plasma peptidases.
Hélène Bachelard, Xavier Charest-Morin, François Marceau   +2 more
doaj   +1 more source

Co-Catalytic Metallopeptidases as Pharmaceutical Targets [PDF]

, 2003
Understanding the reaction mechanism of co-catalytic metallopeptidases provides a starting point for the design and synthesis of new molecules that can be screened as potential pharmaceuticals. Many of the enzymes that contain co-catalytic metallo-active
Bzymek, Krzysztof P., Holz, Richard C., Swierczek, Sabina I.   +2 more
core   +2 more sources

Aminopeptidase C of Aspergillus niger is a Novel Phenylalanine Aminopeptidase [PDF]

, 2003
A novel enzyme with a specific phenylalanine aminopeptidase activity (ApsC) from Aspergillus niger (CBS 120.49) has been characterized. The derived amino acid sequence is not similar to any previously characterized aminopeptidase sequence but does share ...
Basten, E.J.W., Dekker, P.J.T., Schaap, P.J.   +2 more
core   +2 more sources

In vivo effects of bradykinin B2 receptor agonists with varying susceptibility to peptidases.

Frontiers in Pharmacology, 2016
We reported evidence of bradykinin (BK) regeneration from C-terminal extended BK sequences that behave as peptidase-activated B2 receptor (B2R) agonists.
Mélissa eJean, Lajos eGera, Xavier eCharest-Morin, François eMarceau, Hélène eBachelard   +4 more
doaj   +1 more source

Pharmacological evidence of bradykinin regeneration from extended sequences that behave as peptidase-activated B2 receptor agonists

Frontiers in Pharmacology, 2014
While bradykinin (BK) is known to be degraded by angiotensin converting enzyme (ACE), we have recently discovered that Met-Lys-BK-Ser-Ser is paradoxically activated by ACE.
Xavier eCharest-Morin, Caroline eRoy, Émile-Jacques eFortin, Johanne eBouthillier, François eMarceau   +4 more
doaj   +1 more source

Dose-dependent effects of L-Arginine on PROP bitterness intensity and latency and characteristics of the chemical interaction between PROP and L-Arginine [PDF]

, 2015
Genetic variation in the ability to taste the bitterness of 6-n-propylthiouracil (PROP) is a complex trait that has been used to predict food preferences and eating habits.
Aragoni M C, Arca M, Cabras T, Caltagirone C, Castagnola M, Crnjar R, Melis M, Messana I, Tepper B J, Tomassini Barbarossa I   +9 more
core   +8 more sources

The nature of the ligand's side chain interacting with the S1'-subsite of metallocarboxypeptidase T (from Thermoactinomyces vulgaris) determines the geometry of the tetrahedral transition complex.

PLoS ONE, 2019
The carboxypeptidase T (CPT) from Thermoactinomyces vulgaris has an active site structure and 3D organization similar to pancreatic carboxypeptidases A and B (CPA and CPB), but differs in broader substrate specificity.
Valery Kh Akparov, Vladimir I Timofeev, Galina E Konstantinova, Ilyas G Khaliullin, Inna P Kuranova, Tatiana V Rakitina, Vytas Švedas   +6 more
doaj   +1 more source

High expression of human carboxypeptidase M in Pichia pastoris. Purification and partial characterization [PDF]

, 2006
Carboxypeptidase M (CPM) is an extracellular glycosylphosphatidylinositol-anchored membrane glycoprotein, which removes the C-terminal basic residues, lysine and arginine, from peptides and proteins at neutral pH.
Araujo, Ronaldo Carvalho [UNIFESP], Casarini, Dulce Elena [UNIFESP], Chagas, Jair Ribeiro [UNIFESP], Craveiro, Rogerio Bastos [UNIFESP], Pesquero, Jorge Luiz [UNIFESP], Pesquero, João Bosco [UNIFESP], Ramalho, João Daivison Silva [UNIFESP], Wang, Pamella Huey Mei [UNIFESP]   +7 more
core   +1 more source

Structure of the complex of carboxypeptidase B and N-sulfamoyl-L-arginine [PDF]

Acta Crystallographica Section F Structural Biology Communications, 2015
Porcine pancreatic carboxypeptidase B (EC 3.4.23.6) was complexed with a stable transition-state analogue, N-sulfamoyl-L-arginine, in which an S atom imitates the sp 3-hybridized carbon in the scissile-bond surrogate. Crystals were grown in a form belonging to the same space group, P41212, as the uncomplexed enzyme.
Valery, Akparov, Nikolay, Sokolenko, Vladimir, Timofeev, Inna, Kuranova   +3 more
openaire   +2 more sources