• Guanylate cyclase C (GUCY2C, commonly known as GC-C, or STa receptor, STaR) is an enzyme encoded by the GUCY2C gene in humans and belongs to the receptor guanylate cyclase family. (adcreviews.com)
  • Field M, Graf LH Jr, Laird WJ, Smith PL (1978) Heat-stable enterotoxin of Escherichia coli: In vitro effects on guanylate cyclase activity, cyclic GMP concentration, and ion transport in small intestine. (springer.com)
  • Ozaki H, Sato T, Kubota H, Hata Y, Katsube Y, Shimonishi Y (1991) Molecular structure of the toxic domain of heat-stable enterotoxin produced by enterotoxigenic Escherichia coli . (springer.com)
  • Soluble guanylyl cyclases are typically obligate heterodimers, composed of a single alpha and a single beta subunit. (biologists.com)
  • Two recent reports, however, show that there is likely to be an additional class of soluble guanylyl cyclases that do not need a second subunit for activity. (biologists.com)
  • The sequence of MsGC-I contains no regions that show similarity to the regulatory domain of soluble guanylyl cyclases. (elsevierpure.com)
  • Each subunit consists of four domains: an N-terminal HNOX domain, a PAS-like domain, a coiled-coil domain, and a C-terminal catalytic domain. (wikipedia.org)
  • The mammalian enzyme contains one heme per dimer, with a proximal histidine ligand located in the HNOX domain of the beta 1 subunit. (wikipedia.org)
  • The HNOX (Heme Nitric oxide/OXygen binding) domain of the beta subunit of sGC contains the prosthetic heme group, and is part of a family of related sensor proteins found throughout a wide range of organisms. (wikipedia.org)
  • In late 2009, the crystal structure of a human guanylate cyclase catalytic domain, that of the beta subunit, was reported (pdb code 2WZ1). (wikipedia.org)
  • The guanylyl cyclase structure is presumed to be in an inactive conformation: in the active state of the nucleotide cyclases, it is expected that helix α1 (labeled in the right-hand panel) moves into the active site and toward helix α4 of the other subunit of the dimer. (biomedcentral.com)
  • Depending on which family the G protein is, it goes on to activate (G αs protein subunit) or inhibit (G αi protein subunit) the membrane-bound cyclase. (pancreapedia.org)
  • Carboxyl-terminal domain III of the delta' subunit of the DNA polymerase III holoenzyme binds delta. (colorado.edu)
  • While the membrane bound forms are monomers and stimulated by the natriuretic peptides, the soluble guanylate cyclases (sGC) exist as heterodimers consisting of an α 1 - and a β 1 -subunit and containing heme as a prosthetic group [ 1 ]. (biomedcentral.com)
  • This enzyme also activates the transcription factor NF-KAPPA B and is composed of alpha and beta catalytic subunits, which are protein kinases and gamma, a regulatory subunit. (uchicago.edu)
  • When expressed in COS-7 cells, MsGC-I appears to exist as a soluble homodimer with high levels of basal guanylyl cyclase activity that is insensitive to stimulation by nitric oxide. (elsevierpure.com)
  • The 250-residue guanylate cyclase domain at the C-terminus of sGC is highly conserved in soluble and membrane bound guanylyl cyclases, and shares significant homology with the catalytic domains of many adenylyl cyclases. (wikipedia.org)
  • In mammalian adenylyl cyclases, the catalytic core is composed of homologous domains (C1 and C2) that form only one functional active site. (biomedcentral.com)
  • Most mammalian adenylyl cyclases are large transmembrane proteins and subject to complex regulation, most importantly through direct interactions with heterotrimeric GTP-binding (G) proteins (Figure 2 , left-hand side). (biomedcentral.com)
  • Mammalian adenylyl cyclases (left-hand side) are typically transmembrane proteins activated by heterotrimeric G proteins. (biomedcentral.com)
  • cAMP, which was originally identified by its ability to cause breakdown of glycogen in response to adrenaline, is produced by adenylyl cyclase, an enzyme first characterized in 1958. (biomedcentral.com)
  • It took another decade to establish that cGMP and the enzyme responsible for its synthesis, guanylyl cyclase, are also present in mammalian tissues. (biomedcentral.com)
  • Like other membrane guanylyl cyclases, this enzyme has a hydrophobic amino-terminal signal sequence followed by a large extracellular domain, a single membrane spanning domain, a kinase homology domain, and a guanylyl cyclase catalytic domain. (utsouthwestern.edu)
  • In contrast to other membrane guanylyl cyclases, this enzyme is not activated by natriuretic peptides. (utsouthwestern.edu)
  • A cyclase enzyme (lyase) catalyzes the formation of the cyclic nucleotide from its nucleotide triphosphate precursor ( Figure 1 ). (pancreapedia.org)
  • The regulatory influence of the rhodopsin domain on the enzyme activity is only partially understood and holds the key for a deeper understanding of intra-molecular signaling pathways. (elifesciences.org)
  • MsGC-β3, identified in the tobacco hornworm Manduca sexta , was the first example of a soluble guanylyl cyclase that exhibited enzyme activity without the need for coexpression with additional subunits. (biologists.com)
  • These heterodimers, however, show no enzyme activity and, like mammalian β2 subunits, act in a dominant negative manner when combined with the NO-sensitive subunits to disrupt their activation by NO. In addition,we show that the unique C-terminal domain of MsGC-β3 is not necessary for enzyme activity and might act as an auto-inhibitory domain. (biologists.com)
  • Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human C-Type Lectin Domain Family 2, Member C (CLEC2C) in serum, plasma, tissue homogenates, cell lysates and other biological fluids. (allelisakits.com)
  • Description: Enzyme-linked immunosorbent assay based on the Double-antibody Sandwich method for detection of Human C-Type Lectin Domain Family 2, Member C (CLEC2C) in samples from serum, plasma, tissue homogenates, cell lysates and other biological fluids with no significant corss-reactivity with analogues from other species. (allelisakits.com)
  • Soluble guanylyl cyclase (sGC) is the only known receptor for nitric oxide, NO. It is soluble, i.e. completely intracellular. (wikipedia.org)
  • Binding of nitric oxide to the heme results in activation of the C-terminal catalytic domain, which produces cGMP from GTP. (wikipedia.org)
  • The HNOX domain uses the bound heme to sense gaseous ligands such as nitric oxide, oxygen, and/or possibly carbon monoxide. (wikipedia.org)
  • Mammalian guanylyl cyclases (right-hand side) are receptor enzymes directly activated by hormones, such as nitric oxide (NO), or other factors that bind to its regulatory domains (for simplicity, the regulatory domains are not shown). (biomedcentral.com)
  • We also demonstrate that MsGC-β3 is capable of forming heterodimers with the nitric oxide (NO)-sensitive guanylyl cyclase subunits MsGC-α1 and MsGC-β1. (biologists.com)
  • Most of the effects of the signaling molecule nitric oxide (NO) are mediated by cGMP, which is synthesized by soluble guanylyl cyclase and degraded by phosphodiesterases. (rupress.org)
  • In contrast, mammalian guanylyl cyclases are modular receptor enzymes: they exist as homo- or heterodimers with one catalytic domain in each polypeptide chain, and their activity can be modulated directly by hormones or other factors that bind to their accessory domains (Figure 2 , right-hand side) [ 9 ]. (biomedcentral.com)
  • Structure of the catalytic domain of human phosphodiesterase 5 with bound drug molecule'' america Firs' making it work better or faster than usual. (sexedstore.com)
  • In these photoreceptors, the C-terminus of the rhodopsin is directly linked to either a histidine kinase (histidine kinase rhodopsin), a phosphodiesterase (rhodopsin phosphodiesterase, RPDE), or a guanylyl cyclase (rhodopsin guanylyl cyclase, RGC). (elifesciences.org)
  • Here we show that in platelets and aortic tissue, NO led to a biphasic response characterized by a tremendous increase in cGMP (up to 100-fold) in less than 30 s and a rapid decline, reflecting the tightly controlled balance of guanylyl cyclase and phosphodiesterase activities. (rupress.org)
  • Two recent papers, including one in BMC Structural Biology , have revealed atomic structures of the enzymes that catalyze the synthesis of cGMP providing new clues about the molecular basis of substrate specificity and allosteric regulation in nucleotide cyclases. (biomedcentral.com)
  • The nucleotide cyclase wreath-like structure and active-site conformation. (biomedcentral.com)
  • The nucleotide analog marks the position of the single functional adenylyl cyclase active site. (biomedcentral.com)
  • GCC19CART is a CAR-T cell therapy based on ICT's unique technology platform, CoupledCAR®, which targets guanylate cyclase C (GUCY2C) in the treatment of refractory metastatic colorectal cancer (R/R mCRC) [1]. (adcreviews.com)
  • While the PAS domain of sGC has no available structure, the PAS domain of a protein with high sequence homology to sGC has been crystallized (pdb code 2P04). (wikipedia.org)
  • It inhibits the catalytic activity of proteasome-associated Usp14 in vitro (IC50 (adooq.com)
  • The two active sites of the guanylyl cyclase are found in a cleft formed at the interface of two identical subunits (top left). (biomedcentral.com)
  • MsGC-I shows highest sequence identity with receptor guanylyl cyclases throughout its catalytic and dimerization domains but does not contain the ligand-binding, transmembrane, or kinase-like domains characteristic of receptor guanylyl cyclases. (elsevierpure.com)
  • Conduritol B epoxide is a mechanism-based inhibitor which binds covalently to the catalytic site of acid β-glucosidase. (xcessbio.com)
  • Murthy, K.S. Modulation of soluble guanylate cyclase activity by phosphorylation. (enzyme-database.org)
  • Recently, a pyrazolopyridine derivative BAY 41-2272, structurally related to YC-1, was identified stimulating soluble guanylate cyclase in an NO-independent manner, which results in vasodilatation and antiplatelet activity. (biomedcentral.com)
  • Family members have conserved ligand-binding, catalytic (guanylyl cyclase) and regulatory domains with the exception of NPR-C which has an extracellular binding domain homologous to that of other NPRs, but with a truncated intracellular domain which appears to couple, via the G i/o family of G proteins, to activation of phospholipase C, inwardly-rectifying potassium channels and inhibition of adenylyl cyclase activity [ 19 ]. (guidetopharmacology.org)
  • With the biochemical and structural characterization of SiaA, initial data on the catalytic inhibition of SiaA, and the interaction between SiaA and SiaC, our study identifies promising targets for the development of biofilm-interference drugs to combat infections of this aggressive opportunistic pathogen. (uni-konstanz.de)
  • The B domain includes two functional domains: a receptor-binding domain, which defines the tropism of a toxin for a cell and a translocation domain that delivers the A domain across a lipid bilayer, either on the plasma membrane or the endosome. (springer.com)
  • Enzymerhodopsins represent a recently discovered class of rhodopsins which includes histidine kinase rhodopsin, rhodopsin phosphodiesterases, and rhodopsin guanylyl cyclases (RGCs). (elifesciences.org)
  • The ligand-binding site is in the extracellular domain and the cytosolic domain has a heterotrimeric G protein-binding site (127). (pancreapedia.org)
  • The classification is based on sequence similarity within the kinase domain, the presence of additional domains, known biological functions, and conservation across divergent genomes. (wormbook.org)
  • We tracked the catalytic reaction of RGC and the free GC domain independently by UV-light induced release of GTP from the photolabile NPE-GTP substrate. (elifesciences.org)
  • The second signaling mechanism involves the binding of a small signaling molecule to a soluble cyclase. (pancreapedia.org)
  • Now, more than a decade after the first reported adenylyl cyclase structures, two atomic structures of a guanylyl cyclase catalytic core have been reported. (biomedcentral.com)
  • Protein kinase domain [Interproscan]. (ntu.edu.sg)
  • Mur ligase family, Mur ligase middle domain [Interproscan]. (ntu.edu.sg)
  • Description: A sandwich ELISA kit for detection of C-Type Lectin Domain Family 2, Member C from Human in samples from blood, serum, plasma, cell culture fluid and other biological fluids. (allelisakits.com)
  • In the case of sGC, the PAS domain mediates heterodimer formation and may play a role in signal propagation from the HNOX domain to the catalytic guanylate cyclase domain. (wikipedia.org)
  • tRNA synthetases class I (I, Anticodon-binding domain of tRNA, Zinc finger found in FPG and IleRS [Interproscan]. (ntu.edu.sg)
  • ApaG domain [Interproscan]. (ntu.edu.sg)
  • SurA N-terminal domain, PPIC-type PPIASE domain [Interproscan]. (ntu.edu.sg)
  • SEC-C motif, SecA DEAD-like domain, SecA Wing and Scaffold domain, SecA preprotein cross-linking domain [Interproscan]. (ntu.edu.sg)
  • TonB dependent receptor, TonB-dependent Receptor Plug Domain [Interproscan]. (ntu.edu.sg)
  • We demonstrated previously that in the opportunistic, human pathogen P. aeruginosa, the PP2C-like protein phosphatase SiaA and the di-guanylate cyclase SiaD control the formation of macroscopic cellular aggregates, a type of suspended biofilms, in response to surfactant stress. (uni-konstanz.de)
  • Thus, MsGC-I appears to represent a member of a new class of guanylyl cyclases. (elsevierpure.com)
  • Named after the first three proteins in which it was found (Period clock protein, ARNT protein, and Single minded protein) the PAS domain is a sensor domain that has been found in a large variety of proteins, and can work in conjunction with a variety of prosthetic groups as a sensor for a variety of conditions, including light, oxidative stress, or diatomic gases. (wikipedia.org)
  • The PAS domain of sGC is followed by an extended coiled-coil region, which contains a segment called a Signaling helix, which is found in a variety of signaling proteins. (wikipedia.org)