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

Carboxypeptidase A1

carboxypeptidase A
Three different forms of human pancreatic procarboxypeptidase A have been isolated. This gene encodes a monomeric pancreatic exopeptidase involved in zymogen inhibition. [provided by RefSeq, Jan 2009] (from NCBI)
Top mentioned proteins: carboxypeptidase, ACID, Trypsin, CAN, Chymotrypsin
Papers on carboxypeptidase A
Spontaneous cleavage of proteins at serine and threonine is facilitated by zinc.
Truscott et al., Wollongong, Australia. In Aging Cell, Feb 2016
NMR analysis indicated that the imidazole group co-ordinates zinc and that once zinc is co-ordinated, it can polarize the carbonyl group of the peptide bond in a manner analogous to that observed in the active site of the metalloexopeptidase, carboxypeptidase A. The hydroxyl side chain of Ser/Thr is then able to cleave the adjacent peptide bond.
A Bacterial Cell Shape-Determining Inhibitor.
Tanner et al., In Acs Chem Biol, Feb 2016
The results are consistent with the "promoted-water pathway" mechanism for carboxypeptidase A catalysis.
Mast cell tryptase and carboxypeptidase A expression in body fluid and gastrointestinal tract associated with drug-related fatal anaphylaxis.
Gao et al., Taiyuan, China. In World J Gastroenterol, Jan 2016
AIM: To investigate the expression of mast cell tryptase and carboxypeptidase A in drug-related fatal anaphylaxis.
Carboxyl-Terminal Cleavage of Apolipoprotein A-I by Human Mast Cell Chymase Impairs Its Anti-Inflammatory Properties.
Kovanen et al., Helsinki, Finland. In Arterioscler Thromb Vasc Biol, Jan 2016
APPROACH AND RESULTS: Activation of human mast cells triggered the release of granule-associated proteases chymase, tryptase, cathepsin G, carboxypeptidase A, and granzyme B. Among them, chymase cleaved apoA-I with the greatest efficiency and generated C-terminally truncated apoA-I, which failed to bind with high affinity to human coronary artery endothelial cells.
Structures and Activity of New Anabaenopeptins Produced by Baltic Sea Cyanobacteria.
Mazur-Marzec et al., Turku, Finland. In Mar Drugs, 2014
The activity of the peptides against carboxypeptidase A and protein phosphatase 1 as well as chymotrypsin, trypsin and thrombin was tested.
[Coordination chemical studies on the zinc enzymes].
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.
Serum procarboxypeptidase A and carboxypeptidase A levels in pancreatic disease.
Tuzun et al., Van, Turkey. In Hum Exp Toxicol, 2012
Serum pro-CPA and CPA levels were increased in either pancreatitis or pancreatic malignancy
Chapter 24: Anaphylaxis.
Ditto et al., Chicago, United States. In Allergy Asthma Proc, 2012
The preformed mediators from mast cells include histamine, tryptase, carboxypeptidase A, and proteoglycans (heparin and chondroitin sulfates).
Design of biomimetic catalysts by molecular imprinting in synthetic polymers: the role of transition state stabilization.
Liu et al., Düsseldorf, Germany. In Acc Chem Res, 2012
In particular, models for carboxypeptidase A were prepared through the molecular imprinting of synthetic polymers.
Actin-Capping Protein and the Hippo pathway regulate F-actin and tissue growth in Drosophila.
Janody et al., Portugal. In Development, 2011
findings show an interdependency between Hpo signaling activity and F-actin dynamics in which CP and Hpo pathway activities inhibit F-actin accumulation, and the reduction in F-actin in turn sustains Hpo pathway activity
Chymotrypsin C is a co-activator of human pancreatic procarboxypeptidases A1 and A2.
Sahin-Tóth et al., Boston, United States. In J Biol Chem, 2011
Chymotrypsin C is a co-activator of human pancreatic procarboxypeptidases A1 and A2.
Nerve injury evoked loss of latexin expression in spinal cord neurons contributes to the development of neuropathic pain.
Niederberger et al., Frankfurt am Main, Germany. In Plos One, 2010
Data indicate that AAV-mediated latexin transduction or administration of a small molecule carboxypeptidase A inhibitor significantly reduced acetone-evoked nociceptive behavior after SNI.
Progress in metallocarboxypeptidases and their small molecular weight inhibitors.
Avilés et al., Barcelona, Spain. In Biochimie, 2010
Besides, the widespread use of carboxypeptidase A as a benchmark metalloprotease since the early days of Biochemistry has allowed the identification and design of an increasingly vast repertory of small molecular weight inhibitors.
Mast cell proteases: multifaceted regulators of inflammatory disease.
Wernersson et al., Uppsala, Sweden. In Blood, 2010
MCs express extraordinarily high levels of a number of proteases of chymase, tryptase, and carboxypeptidase A type, and these are stored in high amounts as active enzymes in the MC secretory granules.
Enabled and Capping protein play important roles in shaping cell behavior during Drosophila oogenesis.
Peifer et al., Chapel Hill, United States. In Dev Biol, 2009
Enabled and Capping actin regulator proteins shape oogenesis.
Novel insights into the biological function of mast cell carboxypeptidase A.
Wernersson et al., Uppsala, Sweden. In Trends Immunol, 2009
When mast cells are activated they can respond by releasing their secretory granule compounds, including mast cell-specific proteases of chymase, tryptase and carboxypeptidase A (MC-CPA) type.
Mast cells can enhance resistance to snake and honeybee venoms.
Galli et al., Stanford, United States. In Science, 2006
We show, in contrast, that mast cells can significantly reduce snake-venom-induced pathology in mice, at least in part by releasing carboxypeptidase A and possibly other proteases, which can degrade venom components.
Crystal structure of the human angiotensin-converting enzyme-lisinopril complex.
Acharya et al., Bath, United Kingdom. In Nature, 2003
Notably, these inhibitors were developed without knowledge of the structure of human ACE, but were instead designed on the basis of an assumed mechanistic homology with carboxypeptidase A.
Heparin is essential for the storage of specific granule proteases in mast cells.
Stevens et al., Boston, United States. In Nature, 1999
The mast cells in the skeletal muscle that normally contain heparin lacked metachromatic granules and failed to store appreciable amounts of mouse mast-cell protease (mMCP)-4, mMCP-5 and carboxypeptidase A (mMC-CPA), even though they contained substantial amounts of mMCP-7.
A potential catalytic site revealed by the 1.7-A crystal structure of the amino-terminal signalling domain of Sonic hedgehog.
Leahy et al., Baltimore, United States. In Nature, 1995
The structure revealed a tetrahedrally coordinated zinc ion that appears to be structurally analogous to the zinc coordination sites of zinc hydrolases, such as thermolysin and carboxypeptidase A. This previously unsuspected catalytic site represents a distinct activity from the autoprocessing activity that resides in the carboxy-terminal domain.
share on facebooktweetadd +1mail to friends