{"ymdb_id":"YMDB00383","created_at":"2011-05-29T18:11:30.000Z","updated_at":"2016-09-08T18:35:25.000Z","name":"Gluconic acid","cas":"526-95-4","state":"Solid","melting_point":"113-118 oC","description":"Gluconic acid is one of the 16 stereoisomers of 2,3,4,5,6-pentahydroxyhexanoic acid. Gluconic acid, gluconate salts, and gluconate esters occur widely in nature because such species arise from the oxidation of glucose.","experimental_water_solubility":"316 mg/mL at 25 oC [MERCK INDEX (1996)]","experimental_logp_hydrophobicity":"","location":null,"synthesis_reference":"Anastassiadis, Savas; Morgunov, Igor G.  Gluconic acid production.    Recent Patents on Biotechnology  (2007),  1(2),  167-180.","chebi_id":"33198","hmdb_id":"HMDB00625","kegg_id":"C00257","pubchem_id":"10690","cs_id":"24534269","foodb_id":null,"wikipedia_link":"Gluconic_acid","biocyc_id":"GLUCONATE","iupac":"(2R,3S,4R,5R)-2,3,4,5,6-pentahydroxyhexanoic acid","traditional_iupac":"gluconate","logp":"-3.4097443106666665","pka":"12.593710458724516","alogps_solubility":"1.59e+02 g/l","alogps_logp":"-2.57","alogps_logs":"-0.09","acceptor_count":"7","donor_count":"6","rotatable_bond_count":"5","polar_surface_area":"138.45000000000002","refractivity":"38.27100000000001","polarizability":"17.148802962823897","formal_charge":"0","physiological_charge":"-1","pka_strongest_basic":"-2.974220927705365","pka_strongest_acidic":"3.388205574321856","bioavailability":"1","number_of_rings":"0","rule_of_five":"0","ghose_filter":"0","veber_rule":"0","mddr_like_rule":"0","synonyms":["2-Dehydro-3-deoxy-D-gluconate","2-Keto-3-deoxy-D-gluconate","2,3,4,5,6-pentahydroxy-hexanoate","2,3,4,5,6-pentahydroxy-hexanoic acid","2,3,4,5,6-Pentahydroxyhexanoate","2,3,4,5,6-Pentahydroxyhexanoic acid","D-gluco-hexonic acid","D-gluconate","D-gluconic acid","D-gluconsaeure","D-glukonsaeure","Dextronate","Dextronic acid","GCO","Glosanto","Gluconate","Gluconic acid","Glycogenate","Glycogenic acid","Glyconate","Glyconic acid","Hexonic acid","Magnesium D-gluconate dihydratae","Magnesium gluconate","Maltonate","Maltonic acid","Pentahydroxycaproate","Pentahydroxycaproic acid","Sodium stibogluconate"],"pathways":[{"name":"Pentose phosphate pathway","kegg_map_id":"00030"},{"name":"Pentose and glucuronate interconversions","kegg_map_id":"00040"}],"growth_conditions":[],"references":[{"pubmed_id":21051339,"citation":"UniProt Consortium (2011). \"Ongoing and future developments at the Universal Protein Resource.\" Nucleic Acids Res 39:D214-D219."},{"pubmed_id":21062828,"citation":"Scheer, M., Grote, A., Chang, A., Schomburg, I., Munaretto, C., Rother, M., Sohngen, C., Stelzer, M., Thiele, J., Schomburg, D. (2011). \"BRENDA, the enzyme information system in 2011.\" Nucleic Acids Res 39:D670-D676."},{"pubmed_id":12980980,"citation":"SABLE, H. Z., GUARINO, A. J. (1952). \"Phosphorylation of gluconate in yeast extracts.\" J Biol Chem 196:395-402."},{"pubmed_id":21300171,"citation":"Cadiere, A., Ortiz-Julien, A., Camarasa, C., Dequin, S. (2011). \"Evolutionary engineered Saccharomyces cerevisiae wine yeast strains with increased in vivo flux through the pentose phosphate pathway.\" Metab Eng 13:263-271."},{"pubmed_id":17439666,"citation":"Castrillo, J. I., Zeef, L. A., Hoyle, D. C., Zhang, N., Hayes, A., Gardner, D. C., Cornell, M. J., Petty, J., Hakes, L., Wardleworth, L., Rash, B., Brown, M., Dunn, W. B., Broadhurst, D., O'Donoghue, K., Hester, S. S., Dunkley, T. P., Hart, S. R., Swainston, N., Li, P., Gaskell, S. J., Paton, N. W., Lilley, K. S., Kell, D. B., Oliver, S. G. (2007). \"Growth control of the eukaryote cell: a systems biology study in yeast.\" J Biol 6:4."}],"proteins":[{"created_at":"2011-05-26T20:26:33.000Z","updated_at":"2011-05-26T20:26:33.000Z","name":"Probable gluconokinase","uniprot_id":"Q03786","uniprot_name":"GNTK_YEAST","enzyme":true,"transporter":false,"gene_name":null,"num_residues":193,"molecular_weight":"22174.5","theoretical_pi":"7.2","general_function":"Involved in ATP binding","specific_function":"ATP + D-gluconate = ADP + 6-phospho-D- gluconate","reactions":[{"id":2596,"direction":"\u003e","locations":"Cytoplasm","altext":"ATP + D-gluconate = ADP + 6-phospho-D-gluconate.","export":false,"pw_reaction_id":null,"source":null}],"signal_regions":"None","transmembrane_regions":"None","pdb_id":null,"cellular_location":"Cytoplasm","genbank_gene_id":"Z49701","genbank_protein_id":"817834","gene_card_id":null,"chromosome_location":null,"locus":"YDR248C","synonyms":["Gluconate kinase"],"enzyme_classes":["2.7.1.12"],"go_classes":[{"category":"Component","description":" Not Available"},{"category":"Function","description":" nucleoside binding"},{"category":"Function","description":" purine nucleoside binding"},{"category":"Function","description":" adenyl nucleotide binding"},{"category":"Function","description":" adenyl ribonucleotide binding"},{"category":"Function","description":" ATP binding"},{"category":"Function","description":" kinase activity"},{"category":"Function","description":" catalytic activity"},{"category":"Function","description":" transferase activity"},{"category":"Function","description":" transferase activity, transferring phosphorus-containing groups"},{"category":"Function","description":" binding"},{"category":"Process","description":" sulfur metabolic process"},{"category":"Process","description":" sulfate assimilation"},{"category":"Process","description":" metabolic process"},{"category":"Process","description":" cellular metabolic process"},{"category":"Process","description":" primary metabolic process"},{"category":"Process","description":" carbohydrate metabolic process"}],"pfams":[{"name":"APS_kinase","identifier":"PF01583"}],"pathways":[{"name":"Pentose phosphate pathway","kegg_map_id":"00030"}],"gene_sequence":"ATGACAGAGAAACACAAAACTATGGGGAAATTTAAGGTTATTGTATTGGCAGGTACTGCAGGTACAGGAAAATCAACCATTGCAGGTGAACTAATCCATGAATTTAAAGATATATACCCGGATTTGAAATTCATCGAAGGTGATGATTTACACCCGCCTGCCAACGTAGAAAAGATGACAAGAGGGATTCCATTAAATGACGACGACCGTTGGGACTGGTTGAAAAAAGTTGCCGTAGAATCTACAAAAGCTGCAGCAAGCACTAAGGAGCATTTGTCAATTGTTGCTTGCTCGAGCTTGAAGAAGAAATACAGAGATTTGATTAGGCACACATGCCCTGAATCGGAGTTCCATTTTATCTTTTTGTATGCAAGTAAAATAGAAGTTCTGAAAAGGCTCAAAACAAGGAAGGGTCATTTCATGAAAGCTGATATGATGGAGTCTCAATTCAGGGATCTGGAGTTACCAGACATCAACGACGAAACTGACTGTGACATTGTTCCCTTAGATTTCAAAACGTTTTATCAAATTGAAAAAGATGTTATACAGGTGGTAAAAAGTAAAGTTTTGAATATTGAGTAA","protein_sequence":"MTEKHKTMGKFKVIVLAGTAGTGKSTIAGELIHEFKDIYPDLKFIEGDDLHPPANVEKMTRGIPLNDDDRWDWLKKVAVESTKAAASTKEHLSIVACSSLKKKYRDLIRHTCPESEFHFIFLYASKIEVLKRLKTRKGHFMKADMMESQFRDLELPDINDETDCDIVPLDFKTFYQIEKDVIQVVKSKVLNIE"},{"created_at":"2011-05-26T23:22:53.000Z","updated_at":"2011-05-29T14:08:01.000Z","name":"NADPH-dependent methylglyoxal reductase GRE2","uniprot_id":"Q12068","uniprot_name":"GRE2_YEAST","enzyme":true,"transporter":false,"gene_name":"GRE2","num_residues":342,"molecular_weight":"38169.19922","theoretical_pi":"6.06","general_function":"Involved in catalytic activity","specific_function":"Catalyzes the irreversible reduction of the cytotoxic compound methylglyoxal (MG) to (R)-lactaldehyde as an alternative to detoxification of MG by glyoxalase I GLO1. MG is synthesized via a bypath of glycolysis from dihydroxyacetone phosphate and is believed to play a role in cell cycle regulation and stress adaptation","reactions":[{"id":1702,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null},{"id":2615,"direction":"\u003e","locations":"Cytoplasm. Nucleus","altext":"Lactaldehyde + NADP(+) = methylglyoxal + NADPH.","export":false,"pw_reaction_id":null,"source":null},{"id":2616,"direction":"\u003e","locations":"Cytoplasm. Nucleus","altext":"3-methylbutanol + NAD(P)+ = 3-methylbutanal + NAD(P)H + H+","export":false,"pw_reaction_id":null,"source":null},{"id":14116,"direction":"\u003c\u003e","locations":null,"altext":null,"export":true,"pw_reaction_id":"PW_R006547","source":"Smpdb"}],"signal_regions":"None","transmembrane_regions":"None","pdb_id":null,"cellular_location":"Cytoplasm. Nucleus","genbank_gene_id":"AY558040","genbank_protein_id":"45269970","gene_card_id":"GRE2","chromosome_location":"chromosome 15","locus":"YOL151W","synonyms":["Genes de respuesta a estres protein 2"],"enzyme_classes":["1.1.1.283","1.1.1.265"],"go_classes":[{"category":"Component","description":" Not Available"},{"category":"Function","description":" catalytic activity"},{"category":"Function","description":" binding"},{"category":"Function","description":" cofactor binding"},{"category":"Function","description":" coenzyme binding"},{"category":"Process","description":" metabolic process"},{"category":"Process","description":" cellular metabolic process"}],"pfams":[{"name":"Epimerase","identifier":"PF01370"}],"pathways":[{"name":"Pyruvate metabolism","kegg_map_id":"00620"},{"name":"Stress-activated signalling pathways: high osmolarity test 1","kegg_map_id":null}],"gene_sequence":"ATGTCAGTTTTCGTTTCAGGTGCTAACGGGTTCATTGCCCAACACATTGTCGATCTCCTGTTGAAGGAAGACTATAAGGTCATCGGTTCTGCCAGAAGTCAAGAAAAGGCCGAGAATTTAACGGAGGCCTTTGGTAACAACCCAAAATTCTCCATGGAAGTTGTCCCAGACATATCTAAGCTGGACGCATTTGACCATGTTTTCCAAAAGCACGGCAAGGATATCAAGATAGTTCTACATACGGCCTCTCCATTCTGCTTTGATATCACTGACAGTGAACGCGATTTATTAATTCCTGCTGTGAACGGTGTTAAGGGAATTCTCCACTCAATTAAAAAATACGCCGCTGATTCTGTAGAACGTGTAGTTCTCACCTCTTCTTATGCAGCTGTGTTCGATATGGCAAAAGAAAACGATAAGTCTTTAACATTTAACGAAGAATCCTGGAACCCAGCTACCTGGGAGAGTTGCCAAAGTGACCCAGTTAACGCCTACTGTGGTTCTAAGAAGTTTGCTGAAAAAGCAGCTTGGGAATTTCTAGAGGAGAATAGAGACTCTGTAAAATTCGAATTAACTGCCGTTAACCCAGTTTACGTTTTTGGTCCGCAAATGTTTGACAAAGATGTGAAAAAACACTTGAACACATCTTGCGAACTCGTCAACAGCTTGATGCATTTATCACCAGAGGACAAGATACCGGAACTATTTGGTGGATACATTGATGTTCGTGATGTTGCAAAGGCTCATTTAGTTGCCTTCCAAAAGAGGGAAACAATTGGTCAAAGACTAATCGTATCGGAGGCCAGATTTACTATGCAGGATGTTCTCGATATCCTTAACGAAGACTTCCCTGTTCTAAAAGGCAATATTCCAGTGGGGAAACCAGGTTCTGGTGCTACCCATAACACCCTTGGTGCTACTCTTGATAATAAAAAGAGTAAGAAATTGTTAGGTTTCAAGTTCAGGAACTTGAAAGAGACCATTGACGACACTGCCTCCCAAATTTTAAAATTTGAGGGCAGAATATAA","protein_sequence":"MSVFVSGANGFIAQHIVDLLLKEDYKVIGSARSQEKAENLTEAFGNNPKFSMEVVPDISKLDAFDHVFQKHGKDIKIVLHTASPFCFDITDSERDLLIPAVNGVKGILHSIKKYAADSVERVVLTSSYAAVFDMAKENDKSLTFNEESWNPATWESCQSDPVNAYCGSKKFAEKAAWEFLEENRDSVKFELTAVNPVYVFGPQMFDKDVKKHLNTSCELVNSLMHLSPEDKIPELFGGYIDVRDVAKAHLVAFQKRETIGQRLIVSEARFTMQDVLDILNEDFPVLKGNIPVGKPGSGATHNTLGATLDNKKSKKLLGFKFRNLKETIDDTASQILKFEGRI"}]}