{"database":"BioModels","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Pdf":["https://www.ebi.ac.uk/biomodels/model/download/MODEL4780441670?filename=MODEL4780441670.pdf"],"Svg":["https://www.ebi.ac.uk/biomodels/model/download/MODEL4780441670?filename=MODEL4780441670.svg"],"Owl":["https://www.ebi.ac.uk/biomodels/model/download/MODEL4780441670?filename=MODEL4780441670-biopax3.owl","https://www.ebi.ac.uk/biomodels/model/download/MODEL4780441670?filename=MODEL4780441670-biopax2.owl"],"Xml":["https://www.ebi.ac.uk/biomodels/model/download/MODEL4780441670?filename=MODEL4780441670_urn.xml","https://www.ebi.ac.uk/biomodels/model/download/MODEL4780441670?filename=MODEL4780441670_url.xml"],"Other":["https://www.ebi.ac.uk/biomodels/model/download/MODEL4780441670?filename=MODEL4780441670.xpp","https://www.ebi.ac.uk/biomodels/model/download/MODEL4780441670?filename=MODEL4780441670.sci","https://www.ebi.ac.uk/biomodels/model/download/MODEL4780441670?filename=MODEL4780441670.png","https://www.ebi.ac.uk/biomodels/model/download/MODEL4780441670?filename=MODEL4780441670.m","https://www.ebi.ac.uk/biomodels/model/download/MODEL4780441670?filename=MODEL4780441670.vcml"]},"type":"primary"},"statusCodeValue":200,"statusCode":"OK"}],"scores":null,"additional":{"submitter":["Sharat Vayttaden"],"curationStatus":["Non-curated"],"modellingApproach":["ordinary differential equation model"],"levelVersion":["L2V1"],"full_dataset_link":["https://www.ebi.ac.uk/biomodels/MODEL4780441670"],"publication_pubmed":["11325714"],"isPrivate":["false"],"repository":["BioModels"],"modelFormat":["SBML"],"omics_type":["Models"],"tokenised_name":["Condorelli2001 GuanylateCyclase"],"publication_year":["2001"],"submissionId":["MODEL4780441670"],"modelFlag":["Non Miriam"],"publication_authors":["P Condorelli, S C George"],"first_author":["P Condorelli"],"publication":["11325714,\n                            Free nitric oxide (NO) activates soluble guanylate cyclase (sGC), an enzyme, within both pulmonary and vascular smooth muscle. sGC catalyzes the cyclization of guanosine 5'-triphosphate to guanosine 3',5'-cyclic monophosphate (cGMP). Binding rates of NO to the ferrous heme(s) of sGC have been measured in vitro. However, a missing link in our understanding of the control mechanism of sGC by NO is a comprehensive in vivo kinetic analysis. Available literature data suggests that NO dissociation from the heme center of sGC is accelerated by its interaction with one or more cofactors in vivo. We present a working model for sGC activation and NO consumption in vivo. Our model predicts that NO influences the cGMP formation rate over a concentration range of approximately 5-100 nM (apparent Michaelis constant approximately 23 nM), with Hill coefficients between 1.1 and 1.5. The apparent reaction order for NO consumption by sGC is dependent on NO concentration, and varies between 0 and 1.5. Finally, the activation of sGC (half-life approximately 1-2 s) is much more rapid than deactivation (approximately 50 s). We conclude that control of sGC in vivo is most likely ultra-sensitive, and that activation in vivo occurs at lower NO concentrations than previously reported.. 5, 80.\n                            Department of Chemical and Biochemical Engineering and Materials Science, University of California, Irvine, Irvine, California 92697-2575, USA."],"submitter_mail":["doqcs@ncbs.res.in"],"submitter_affiliation":["DOQCS"],"pubmed_abstract":["Free nitric oxide (NO) activates soluble guanylate cyclase (sGC), an enzyme, within both pulmonary and vascular smooth muscle. sGC catalyzes the cyclization of guanosine 5'-triphosphate to guanosine 3',5'-cyclic monophosphate (cGMP). Binding rates of NO to the ferrous heme(s) of sGC have been measured in vitro. However, a missing link in our understanding of the control mechanism of sGC by NO is a comprehensive in vivo kinetic analysis. Available literature data suggests that NO dissociation from the heme center of sGC is accelerated by its interaction with one or more cofactors in vivo. We present a working model for sGC activation and NO consumption in vivo. Our model predicts that NO influences the cGMP formation rate over a concentration range of approximately 5-100 nM (apparent Michaelis constant approximately 23 nM), with Hill coefficients between 1.1 and 1.5. The apparent reaction order for NO consumption by sGC is dependent on NO concentration, and varies between 0 and 1.5. Finally, the activation of sGC (half-life approximately 1-2 s) is much more rapid than deactivation (approximately 50 s). We conclude that control of sGC in vivo is most likely ultra-sensitive, and that activation in vivo occurs at lower NO concentrations than previously reported."],"pubmed_title":["In vivo control of soluble guanylate cyclase activation by nitric oxide: a kinetic analysis."],"pubmed_authors":["Condorelli P P, George S C SC"],"additional_accession":[]},"is_claimable":false,"name":"Condorelli2001_GuanylateCyclase","description":"\n      \n    This model features the observations of Condorelli P, George SC. Biophys J. (2001) 80(5):2110-9. They propose a in vivo mechanism for the binding of free NO to sGC based on in vitro data within both pulmonary and vascular smooth muscle. All the parameters used have been obtained from reported results based on experiments. One important conclusion they make is that control of sGC in vivo is most likely to be ultra-sensitive and that activation in vivo occurs at lower NO concentrations than reported.    This model originates from BioModels Database: A Database of Annotated Published Models (http://www.ebi.ac.uk/biomodels/). It is copyright (c) 2005-2011 The BioModels.net Team.      \n          To the extent possible under law, all copyright and related or neighbouring rights to this encoded model have been dedicated to the public domain worldwide. Please refer to      CC0 Public Domain Dedication\n          for more information.      \n    In summary, you are entitled to use this encoded model in absolutely any manner you deem suitable, verbatim, or with modification, alone or embedded it in a larger context, redistribute it, commercially or not, in a restricted way or not..      \n    \n          To cite BioModels Database, please use:      Li C, Donizelli M, Rodriguez N, Dharuri H, Endler L, Chelliah V, Li L, He E, Henry A, Stefan MI, Snoep JL, Hucka M, Le Novère N, Laibe C (2010) BioModels Database: An enhanced, curated and annotated resource for published quantitative kinetic models. BMC Syst Biol., 4:92.\n\n\n","dates":{"last_modification":"2007-01-26","publication":"2005-01-01","submission":"2006-11-29"},"accession":"MODEL4780441670","cross_references":{"pubmed":["11325714"],"biomodels__db":["MODEL4780441670"],"go":["GO:0071731"],"taxonomy":["9606"]}}