{"ymdb_id":"YMDB00664","created_at":"2011-05-29T18:41:35.000Z","updated_at":"2016-09-08T18:35:45.000Z","name":"3'-Dephospho-CoA","cas":"3633-59-8","state":"Solid","melting_point":null,"description":"3'-Dephospho-CoA is the coenzyme A (CoA) precursor in the last step of coenzyme A biosynthesis pathway. Coenzyme A is a cofactor of ubiquitous occurrence in plants, bacteria, and animals. It is needed in a large number of enzymatic reactions central to intermediary metabolism, including the oxidation of fatty acids, carbohydrates, and amino acids. [Biocyc COA-PWY]","experimental_water_solubility":null,"experimental_logp_hydrophobicity":null,"location":null,"synthesis_reference":null,"chebi_id":"15468","hmdb_id":"HMDB01373","kegg_id":"C00882","pubchem_id":"444485","cs_id":"24785028","foodb_id":null,"wikipedia_link":null,"biocyc_id":"DEPHOSPHO-COA","iupac":"[({[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy}(hydroxy)phosphoryl)oxy][(3R)-3-hydroxy-2,2-dimethyl-3-({2-[(2-sulfanylethyl)carbamoyl]ethyl}carbamoyl)propoxy]phosphinic acid","traditional_iupac":"3'-dephospho-coa","logp":"-5.293668356465593","pka":"3.194041950179442","alogps_solubility":"2.56e+00 g/l","alogps_logp":"-0.98","alogps_logs":"-2.43","acceptor_count":"14","donor_count":"9","rotatable_bond_count":"16","polar_surface_area":"300.0299999999999","refractivity":"151.86729999999997","polarizability":"63.63833857739969","formal_charge":"0","physiological_charge":"-2","pka_strongest_basic":"4.010528179913593","pka_strongest_acidic":"1.8606698172470169","bioavailability":"0","number_of_rings":"3","rule_of_five":"0","ghose_filter":"0","veber_rule":"0","mddr_like_rule":"1","synonyms":["3'-dephospho-Coenzyme A","3'-O-dephosphono-CoA","3'-O-dephosphono-Coenzyme A","Coenzyme A, 3'-O-dephosphono-","Dephospho coa","Dephospho-CoA","Dephospho-Coenzyme A","dephosphocoenzyme a"],"pathways":[{"name":"Pantothenate and CoA biosynthesis","kegg_map_id":"00770"},{"name":"beta-Alanine metabolism","kegg_map_id":"00410"}],"growth_conditions":[],"references":[{"pubmed_id":18846089,"citation":"Herrgard, M. J., Swainston, N., Dobson, P., Dunn, W. B., Arga, K. Y., Arvas, M., Bluthgen, N., Borger, S., Costenoble, R., Heinemann, M., Hucka, M., Le Novere, N., Li, P., Liebermeister, W., Mo, M. L., Oliveira, A. P., Petranovic, D., Pettifer, S., Simeonidis, E., Smallbone, K., Spasic, I., Weichart, D., Brent, R., Broomhead, D. S., Westerhoff, H. V., Kirdar, B., Penttila, M., Klipp, E., Palsson, B. O., Sauer, U., Oliver, S. G., Mendes, P., Nielsen, J., Kell, D. B. (2008). \"A consensus yeast metabolic network reconstruction obtained from a community approach to systems biology.\" Nat Biotechnol 26:1155-1160."},{"pubmed_id":10922370,"citation":"Cartwright, J. L., Gasmi, L., Spiller, D. G., McLennan, A. G. (2000). \"The Saccharomyces cerevisiae PCD1 gene encodes a peroxisomal nudix hydrolase active toward coenzyme A and its derivatives.\" J Biol Chem 275:32925-32930."},{"pubmed_id":7012143,"citation":"Hampsey, D. M., Kohlhaw, G. B. (1981). \"Inactivation of yeast alpha-isopropylmalate synthase by CoA. Antagonism between CoA and adenylates and the mechanism of CoA inactivation.\" J Biol Chem 256:3791-3796."}],"proteins":[]}