2.02012-05-31 10:23:03 -06002015-09-13 12:56:06 -0600ECMDB00177M2MDB000074L-HistidineHistidine is an amino acid. It is a precursor for histamine and carnosine biosynthesis. The enzyme histidine ammonia-lyase converts histidine into ammonia and urocanic acid. (Wikipedia)α-amino-4-imidazoleproprionateα-amino-4-imidazoleproprionic acid(S)-α-amino-1H-imidazole-4-propanoate(S)-α-amino-1H-imidazole-4-propanoic acid(S)-1H-Imidazole-4-alanine(S)-2-Amino-3-(4-imidazolyl)propionsaeure(S)-4-(2-Amino-2-carboxyethyl)imidazole(S)-a-Amino-1H-imidazole-4-propanoate(S)-a-Amino-1H-imidazole-4-propanoic acid(S)-a-amino-1H-Imidazole-4-propionate(S)-a-amino-1H-Imidazole-4-propionic acid(S)-alpha-Amino-1H-imidazole-4-propanoate(S)-alpha-Amino-1H-imidazole-4-propanoic acid(S)-alpha-Amino-1H-imidazole-4-propionate(S)-alpha-Amino-1H-imidazole-4-propionic acid(S)-Histidine(S)-α-amino-1H-Imidazole-4-propanoate(S)-α-amino-1H-Imidazole-4-propanoic acid(S)-α-amino-1H-Imidazole-4-propionate(S)-α-amino-1H-Imidazole-4-propionic acid(S)1H-Imidazole-4-alanine3-(1H-Imidazol-4-yl)-L-Alaninea-amino-4-Imidazoleproprionatea-amino-4-Imidazoleproprionic acidAlpha-Amino-4-imidazoleproprionateAlpha-Amino-4-imidazoleproprionic acidAmino-1H-imidazole-4-propanoateAmino-1H-imidazole-4-propanoic acidAmino-4-imidazoleproprionateAmino-4-imidazoleproprionic acidGlyoxaline-5-alanineHHisHistidineL-(-)-Histidineα-amino-4-Imidazoleproprionateα-amino-4-Imidazoleproprionic acidC6H9N3O2155.1546155.069476547(2S)-2-amino-3-(1H-imidazol-5-yl)propanoic acidL-histidine71-00-1N[C@@H](CC1=CN=CN1)C(O)=OInChI=1S/C6H9N3O2/c7-5(6(10)11)1-4-2-8-3-9-4/h2-3,5H,1,7H2,(H,8,9)(H,10,11)/t5-/m0/s1HNDVDQJCIGZPNO-YFKPBYRVSA-NSolidCytosolExtra-organismPeriplasmlogp-2.67logs-0.34solubility7.13e+01 g/lmelting_point287 oClogp-3.6pka_strongest_acidic1.85pka_strongest_basic9.44iupac(2S)-2-amino-3-(1H-imidazol-5-yl)propanoic acidaverage_mass155.1546mono_mass155.069476547smilesN[C@@H](CC1=CN=CN1)C(O)=OformulaC6H9N3O2inchiInChI=1S/C6H9N3O2/c7-5(6(10)11)1-4-2-8-3-9-4/h2-3,5H,1,7H2,(H,8,9)(H,10,11)/t5-/m0/s1inchikeyHNDVDQJCIGZPNO-YFKPBYRVSA-Npolar_surface_area92refractivity38.06polarizability14.67rotatable_bond_count3acceptor_count4donor_count3physiological_charge0formal_charge0Aminoacyl-tRNA biosynthesisec00970Histidine metabolismec00340beta-Alanine metabolismThe Beta-Alanine Metabolism starts with a product of Aspartate metabolism. Aspartate is decarboxylated by aspartate 1-decarboxylase, releasing carbon dioxide and Beta-alanine. Beta alanine is then metabolized through a pantothenate synthetase resulting in Pantothenic acid undergoes phosphorylation through a ATP driven pantothenate kinase, resulting in D-4-phosphopantothenate.
Pantothenate (vitamin B5) is the universal precursor for the synthesis of the 4'-phosphopantetheine moiety of coenzyme A and acyl carrier protein. Only plants and microorganismscan synthesize pantothenate de novo - animals require a dietary supplement. The enzymes of this pathway are therefore considered to be antimicrobial drug targets.PW000896ec00410MetabolicABC transportersec02010Metabolic pathwayseco01100Secondary Metabolites: Histidine biosynthesisHistidine biosynthesis starts with a product of PRPP biosynthesis pathway, phosphoribosyl pyrophosphate which interacts with a hydrogen ion through an ATP phosphoribosyltransferase resulting in an pyrophosphate and a phosphoribosyl-ATP. This compound interacts with water through a phosphoribosyl-AMP cyclohydrolase / phosphoribosyl-ATP pyrophosphatase resulting in the release of pyrophosphate, hydrogen ion and a phosphoribosyl-AMP. This enzyme proceeds to interact with phosphoribosyl-AMP and water resulting in a 1-(5'-Phosphoribosyl)-5-amino-4-imidazolecarboxamide. This compound is then isomerized by a N-(5'-phospho-L-ribosyl-formimino)-5-amino-1-(5'-phosphoribosyl)-4-imidazolecarboxamide isomerase resulting in a PhosphoribosylformiminoAICAR-phosphate. This compound reacts with L-glutamine through an imidazole glycerol phosphate synthase resulting in a L-glutamic acid, hydrogen ion, 5-aminoimidazole-4-carboxamide and a D-erythro-imidazole-glycerol-phosphate. This compound reacts with a imidazoleglycerol-phosphate dehydratase / histidinol-phosphatase, dehydrating the compound and resulting in a imidazole acetol-phosphate.
This compound interacts with L-glutamic acid through a histidinol-phosphate aminotransferase, releasing oxoglutaric acid and L-histidinol-phosphate. The latter compound interacts with water and a imidazoleglycerol-phosphate dehydratase / histidinol-phosphatase resulting in L-histidinol and phosphate. L-histidinol interacts with a NAD-driven histidinol dehydrogenase resulting in a Histidinal. This in turn reacts with water in a NAD driven histidinal dehydrogenase resulting in L-Histidine.
L-Histidine then represses ATP phosphoribosyltransferase, regulation its own biosynthesis.PW000984Metabolichistidine biosynthesisHistidine biosynthesis starts with a product of PRPP biosynthesis pathway, phosphoribosyl pyrophosphate which interacts with a hydrogen ion through an ATP phosphoribosyltransferase resulting in an pyrophosphate and a phosphoribosyl-ATP. This compound interacts with water through a phosphoribosyl-AMP cyclohydrolase / phosphoribosyl-ATP pyrophosphatase resulting in the release of pyrophosphate, hydrogen ion and a phosphoribosyl-AMP. This enzyme proceeds to interact with phosphoribosyl-AMP and water resulting in a 1-(5'-Phosphoribosyl)-5-amino-4-imidazolecarboxamide. This compound is then isomerized by a N-(5'-phospho-L-ribosyl-formimino)-5-amino-1-(5'-phosphoribosyl)-4-imidazolecarboxamide isomerase resulting in a PhosphoribosylformiminoAICAR-phosphate. This compound reacts with L-glutamine through an imidazole glycerol phosphate synthase resulting in a L-glutamic acid, hydrogen ion, 5-aminoimidazole-4-carboxamide and a D-erythro-imidazole-glycerol-phosphate. This compound reacts with a imidazoleglycerol-phosphate dehydratase / histidinol-phosphatase, dehydrating the compound and resulting in a imidazole acetol-phosphate.
This compound interacts with L-glutamic acid through a histidinol-phosphate aminotransferase, releasing oxoglutaric acid and L-histidinol-phosphate. The latter compound interacts with water and a imidazoleglycerol-phosphate dehydratase / histidinol-phosphatase resulting in L-histidinol and phosphate. L-histidinol interacts with a NAD-driven histidinol dehydrogenase resulting in a Histidinal. This in turn reacts with water in a NAD driven histidinal dehydrogenase resulting in L-Histidine.
L-Histidine then represses ATP phosphoribosyltransferase, regulation its own biosynthesis.PW000810MetabolictRNA Charging 2This pathway groups together all E. coli tRNA charging reactions.PW000803MetabolictRNA chargingThis pathway groups together all E. coli tRNA charging reactions.PW000799MetabolictRNA chargingTRNA-CHARGING-PWYhistidine biosynthesisHISTSYN-PWYSpecdb::CMs416Specdb::CMs417Specdb::CMs418Specdb::CMs419Specdb::CMs1646Specdb::CMs1833Specdb::CMs3063Specdb::CMs30203Specdb::CMs30309Specdb::CMs30596Specdb::CMs30739Specdb::CMs30768Specdb::CMs31051Specdb::CMs31052Specdb::CMs31961Specdb::CMs31962Specdb::CMs37340Specdb::CMs157409Specdb::CMs1052791Specdb::CMs1052793Specdb::CMs1052795Specdb::CMs1052797Specdb::CMs1052799Specdb::EiMs1976Specdb::NmrOneD1146Specdb::NmrOneD1193Specdb::NmrOneD142730Specdb::NmrOneD142731Specdb::NmrOneD142732Specdb::NmrOneD142733Specdb::NmrOneD142734Specdb::NmrOneD142735Specdb::NmrOneD142736Specdb::NmrOneD142737Specdb::NmrOneD142738Specdb::NmrOneD142739Specdb::NmrOneD142740Specdb::NmrOneD142741Specdb::NmrOneD142742Specdb::NmrOneD142743Specdb::NmrOneD142744Specdb::NmrOneD142745Specdb::NmrOneD142746Specdb::NmrOneD142747Specdb::NmrOneD142748Specdb::NmrOneD142749Specdb::NmrOneD166370Specdb::NmrOneD166434Specdb::NmrOneD166541Specdb::MsMs283Specdb::MsMs284Specdb::MsMs285Specdb::MsMs3351Specdb::MsMs3352Specdb::MsMs3353Specdb::MsMs3354Specdb::MsMs3355Specdb::MsMs3356Specdb::MsMs3357Specdb::MsMs3358Specdb::MsMs3359Specdb::MsMs3360Specdb::MsMs3361Specdb::MsMs3362Specdb::MsMs3363Specdb::MsMs3364Specdb::MsMs3365Specdb::MsMs3366Specdb::MsMs3367Specdb::MsMs3368Specdb::MsMs3369Specdb::MsMs3370Specdb::MsMs3371Specdb::MsMs3372Specdb::NmrTwoD1189HMDB0017762746038C0013515971HISHIS_LFZW_DHE2L-HistidineKeseler, I. M., Collado-Vides, J., Santos-Zavaleta, A., Peralta-Gil, M., Gama-Castro, S., Muniz-Rascado, L., Bonavides-Martinez, C., Paley, S., Krummenacker, M., Altman, T., Kaipa, P., Spaulding, A., Pacheco, J., Latendresse, M., Fulcher, C., Sarker, M., Shearer, A. G., Mackie, A., Paulsen, I., Gunsalus, R. P., Karp, P. D. (2011). "EcoCyc: a comprehensive database of Escherichia coli biology." Nucleic Acids Res 39:D583-D590.21097882Kanehisa, M., Goto, S., Sato, Y., Furumichi, M., Tanabe, M. (2012). "KEGG for integration and interpretation of large-scale molecular data sets." Nucleic Acids Res 40:D109-D114.22080510van der Werf, M. J., Overkamp, K. M., Muilwijk, B., Coulier, L., Hankemeier, T. (2007). "Microbial metabolomics: toward a platform with full metabolome coverage." Anal Biochem 370:17-25.17765195Winder, C. L., Dunn, W. B., Schuler, S., Broadhurst, D., Jarvis, R., Stephens, G. M., Goodacre, R. (2008). "Global metabolic profiling of Escherichia coli cultures: an evaluation of methods for quenching and extraction of intracellular metabolites." Anal Chem 80:2939-2948.18331064Bennett, B. D., Kimball, E. H., Gao, M., Osterhout, R., Van Dien, S. J., Rabinowitz, J. D. (2009). "Absolute metabolite concentrations and implied enzyme active site occupancy in Escherichia coli." Nat Chem Biol 5:593-599.19561621Ishii, N., Nakahigashi, K., Baba, T., Robert, M., Soga, T., Kanai, A., Hirasawa, T., Naba, M., Hirai, K., Hoque, A., Ho, P. Y., Kakazu, Y., Sugawara, K., Igarashi, S., Harada, S., Masuda, T., Sugiyama, N., Togashi, T., Hasegawa, M., Takai, Y., Yugi, K., Arakawa, K., Iwata, N., Toya, Y., Nakayama, Y., Nishioka, T., Shimizu, K., Mori, H., Tomita, M. (2007). "Multiple high-throughput analyses monitor the response of E. coli to perturbations." Science 316:593-597.17379776Sreekumar A, Poisson LM, Rajendiran TM, Khan AP, Cao Q, Yu J, Laxman B, Mehra R, Lonigro RJ, Li Y, Nyati MK, Ahsan A, Kalyana-Sundaram S, Han B, Cao X, Byun J, Omenn GS, Ghosh D, Pennathur S, Alexander DC, Berger A, Shuster JR, Wei JT, Varambally S, Beecher C, Chinnaiyan AM: Metabolomic profiles delineate potential role for sarcosine in prostate cancer progression. Nature. 2009 Feb 12;457(7231):910-4.19212411Shoemaker JD, Elliott WH: Automated screening of urine samples for carbohydrates, organic and amino acids after treatment with urease. J Chromatogr. 1991 Jan 2;562(1-2):125-38.2026685Silwood CJ, Lynch E, Claxson AW, Grootveld MC: 1H and (13)C NMR spectroscopic analysis of human saliva. J Dent Res. 2002 Jun;81(6):422-7.12097436Nicholson JK, O'Flynn MP, Sadler PJ, Macleod AF, Juul SM, Sonksen PH: Proton-nuclear-magnetic-resonance studies of serum, plasma and urine from fasting normal and diabetic subjects. Biochem J. 1984 Jan 15;217(2):365-75.6696735Wevers RA, Engelke U, Wendel U, de Jong JG, Gabreels FJ, Heerschap A: Standardized method for high-resolution 1H-NMR of cerebrospinal fluid. Clin Chem. 1995 May;41(5):744-51.7729054Hagenfeldt L, Bjerkenstedt L, Edman G, Sedvall G, Wiesel FA: Amino acids in plasma and CSF and monoamine metabolites in CSF: interrelationship in healthy subjects. J Neurochem. 1984 Mar;42(3):833-7.6198473Peng CT, Wu KH, Lan SJ, Tsai JJ, Tsai FJ, Tsai CH: Amino acid concentrations in cerebrospinal fluid in children with acute lymphoblastic leukemia undergoing chemotherapy. Eur J Cancer. 2005 May;41(8):1158-63. Epub 2005 Apr 14.15911239Cynober LA: Plasma amino acid levels with a note on membrane transport: characteristics, regulation, and metabolic significance. Nutrition. 2002 Sep;18(9):761-6.12297216Rainesalo S, Keranen T, Palmio J, Peltola J, Oja SS, Saransaari P: Plasma and cerebrospinal fluid amino acids in epileptic patients. Neurochem Res. 2004 Jan;29(1):319-24.14992292Klassen P, Furst P, Schulz C, Mazariegos M, Solomons NW: Plasma free amino acid concentrations in healthy Guatemalan adults and in patients with classic dengue. Am J Clin Nutr. 2001 Mar;73(3):647-52.11237944Xiao B, Jing C, Kelly G, Walker PA, Muskett FW, Frenkiel TA, Martin SR, Sarma K, Reinberg D, Gamblin SJ, Wilson JR: Specificity and mechanism of the histone methyltransferase Pr-Set7. Genes Dev. 2005 Jun 15;19(12):1444-54. Epub 2005 Jun 2.15933069Mukerji SK, Pimstone NR, Gandhi SN, Tan KT: Biochemical diagnosis and monitoring therapeutic modulation of disease activity in an unusual case of congenital erythropoietic porphyria. Clin Chem. 1985 Dec;31(12):1946-51.4064282Churchill D, Yacoub JM, Siu KP, Symes A, Gault MH: Toxic nephropathy after low-dose methoxyflurane anesthesia: drug interaction with secobarbital? Can Med Assoc J. 1976 Feb 21;114(4):326-8, 333.1253070Sieja K, Stanosz S, von Mach-Szczypinski J, Olewniczak S, Stanosz M: Concentration of histamine in serum and tissues of the primary ductal breast cancers in women. Breast. 2005 Jun;14(3):236-41. Epub 2005 Jan 21.15927833Masini E, Fabbroni V, Giannini L, Vannacci A, Messerini L, Perna F, Cortesini C, Cianchi F: Histamine and histidine decarboxylase up-regulation in colorectal cancer: correlation with tumor stage. Inflamm Res. 2005 Apr;54 Suppl 1:S80-1.15928846Xiao YP, Han CB, Mao XY, Li JY, Xu L, Ren CS, Xin Y: Relationship between abnormality of FHIT gene and EBV infection in gastric cancer. World J Gastroenterol. 2005 Jun 7;11(21):3212-6.15929169Mason AB, Halbrooks PJ, James NG, Connolly SA, Larouche JR, Smith VC, MacGillivray RT, Chasteen ND: Mutational analysis of C-lobe ligands of human serum transferrin: insights into the mechanism of iron release. Biochemistry. 2005 Jun 7;44(22):8013-21.15924420Janknecht R, Hipskind RA, Houthaeve T, Nordheim A, Stunnenberg HG: Identification of multiple SRF N-terminal phosphorylation sites affecting DNA binding properties. EMBO J. 1992 Mar;11(3):1045-54.1547771Peterson JW, Boldogh I, Popov VL, Saini SS, Chopra AK: Anti-inflammatory and antisecretory potential of histidine in Salmonella-challenged mouse small intestine. Lab Invest. 1998 May;78(5):523-34.9605177Gerber DA: Low free serum histidine concentration in rheumatoid arthritis. A measure of disease activity. J Clin Invest. 1975 Jun;55(6):1164-73.1079527Hemler RJ, Hoogeveen JH, Kraaier V, Van Huffelen AC, Wieneke GH, Hijman R, Glerum JH: A pharmacological model of cerebral ischemia. The effects of indomethacin on cerebral blood flow velocity, quantitative EEG and cognitive functions. Methods Find Exp Clin Pharmacol. 1990 Nov;12(9):641-3.2084459Feng RN, Niu YC, Sun XW, Li Q, Zhao C, Wang C, Guo FC, Sun CH, Li Y: Histidine supplementation improves insulin resistance through suppressed inflammation in obese women with the metabolic syndrome: a randomised controlled trial. Diabetologia. 2013 May;56(5):985-94. doi: 10.1007/s00125-013-2839-7. Epub 2013 Jan 30.23361591Watanabe M, Suliman ME, Qureshi AR, Garcia-Lopez E, Barany P, Heimburger O, Stenvinkel P, Lindholm B: Consequences of low plasma histidine in chronic kidney disease patients: associations with inflammation, oxidative stress, and mortality. Am J Clin Nutr. 2008 Jun;87(6):1860-6.18541578Jung J, Kim SH, Lee HS, Choi GS, Jung YS, Ryu DH, Park HS, Hwang GS: Serum metabolomics reveals pathways and biomarkers associated with asthma pathogenesis. Clin Exp Allergy. 2013 Apr;43(4):425-33. doi: 10.1111/cea.12089.23517038Effective method for the amelioration and prevention of tissue and cellular damage: http://www.google.com/patents/US6150392Aurelio Luigi; Brownlee Robert T C; Hughes Andrew B A novel synthesis of N-methyl asparagine, arginine, histidine, and tryptophan. Organic letters (2002), 4(21), 3767-9.http://hmdb.ca/system/metabolites/msds/000/000/126/original/HMDB00177.pdf?1358894676Histidinol dehydrogenaseP06988HISX_ECOLIhisDhttp://ecmdb.ca/proteins/P06988.xmlHistidine transport ATP-binding protein hisPP07109HISP_ECOLIhisPhttp://ecmdb.ca/proteins/P07109.xmlHistidyl-tRNA synthetaseP60906SYH_ECOLIhisShttp://ecmdb.ca/proteins/P60906.xmlHistidine transport system permease protein hisMP0AEU3HISM_ECOLIhisMhttp://ecmdb.ca/proteins/P0AEU3.xmlHistidine transport system permease protein hisQP52094HISQ_ECOLIhisQhttp://ecmdb.ca/proteins/P52094.xmlHistidine-binding periplasmic proteinP0AEU0HISJ_ECOLIhisJhttp://ecmdb.ca/proteins/P0AEU0.xmlHistidine transport ATP-binding protein hisPP07109HISP_ECOLIhisPhttp://ecmdb.ca/proteins/P07109.xmlUncharacterized amino-acid ABC transporter ATP-binding protein yecCP37774YECC_ECOLIyecChttp://ecmdb.ca/proteins/P37774.xmlInner membrane amino-acid ABC transporter permease protein yecSP0AFT2YECS_ECOLIyecShttp://ecmdb.ca/proteins/P0AFT2.xmlHistidine transport system permease protein hisMP0AEU3HISM_ECOLIhisMhttp://ecmdb.ca/proteins/P0AEU3.xmlAromatic amino acid transport protein AroPP15993AROP_ECOLIaroPhttp://ecmdb.ca/proteins/P15993.xmlHistidine transport system permease protein hisQP52094HISQ_ECOLIhisQhttp://ecmdb.ca/proteins/P52094.xmlOuter membrane protein NP77747OMPN_ECOLIompNhttp://ecmdb.ca/proteins/P77747.xmlOuter membrane pore protein EP02932PHOE_ECOLIphoEhttp://ecmdb.ca/proteins/P02932.xmlHistidine-binding periplasmic proteinP0AEU0HISJ_ECOLIhisJhttp://ecmdb.ca/proteins/P0AEU0.xmlOuter membrane protein FP02931OMPF_ECOLIompFhttp://ecmdb.ca/proteins/P02931.xmlOuter membrane protein CP06996OMPC_ECOLIompChttp://ecmdb.ca/proteins/P06996.xmlAdenosine triphosphate + Water + L-Histidine > ADP + Hydrogen ion + L-Histidine + PhosphateABC-14-RXNAdenosine triphosphate + Water + L-Histidine > ADP + Hydrogen ion + L-Histidine + PhosphateABC-14-RXNWater + L-Histidinol + 2 NAD >3 Hydrogen ion + L-Histidine +2 NADHAdenosine triphosphate + L-Histidine + tRNA(His) + tRNA(His) <> Adenosine monophosphate + L-Histidyl-tRNA(His) + Pyrophosphate + L-Histidyl-tRNA(His)R03655L-Histidinal + Water + NAD <> L-Histidine + NADH + Hydrogen ionR01163Adenosine triphosphate + L-Histidine + tRNA(His) <> Adenosine monophosphate + Pyrophosphate + L-Histidyl-tRNA(His)R03655Adenosine triphosphate + L-Histidine + Water > ADP + Phosphate + L-Histidine + Hydrogen ionABC-14-RXNAdenosine triphosphate + L-Histidine + Water > ADP + Phosphate + L-Histidine + Hydrogen ionABC-14-RXNhistidinal + NAD + Water > Hydrogen ion + L-Histidine + NADHHISTALDEHYD-RXNala-his + Water > L-Alanine + L-HistidineRXN0-6978L-Histidinol + Water + 2 NAD > L-Histidine +2 NADHAdenosine triphosphate + L-Histidine + tRNA(His) > Adenosine monophosphate + Pyrophosphate + L-histidyl-tRNA(His)L-Histidinol + 2 NAD + Water <> L-Histidine +2 NADH +3 Hydrogen ionR01158 L-Histidine + Adenosine triphosphate + Hydrogen ion + tRNA(His) + L-Histidine > Adenosine monophosphate + Pyrophosphate + L-histidyl-tRNA(His)PW_R002839Water + NAD + Histidinal >2 Hydrogen ion + NADH + L-Histidine + L-HistidinePW_R002874L-Histidine + Adenosine triphosphate + Water + L-Histidine > Adenosine diphosphate + Phosphate + Hydrogen ion + L-Histidine + ADPPW_RCT000109Adenosine triphosphate + L-Histidine + tRNA(His) <> Adenosine monophosphate + L-Histidyl-tRNA(His) + PyrophosphateL-Histidinal + Water + NAD <> L-Histidine + NADH + Hydrogen ionAdenosine triphosphate + L-Histidine + tRNA(His) <> Adenosine monophosphate + L-Histidyl-tRNA(His) + PyrophosphateGutnick minimal complete medium (4.7 g/L KH2PO4; 13.5 g/L K2HPO4; 1 g/L K2SO4; 0.1 g/L MgSO4-7H2O; 10 mM NH4Cl) with 4 g/L glucoseShake flask and filter culture67.6uM0.037 oCK12 NCM3722Mid-Log Phase2704000Bennett, B. D., Kimball, E. H., Gao, M., Osterhout, R., Van Dien, S. J., Rabinowitz, J. D. (2009). "Absolute metabolite concentrations and implied enzyme active site occupancy in Escherichia coli." Nat Chem Biol 5:593-599.19561621Gutnick minimal complete medium (4.7 g/L KH2PO4; 13.5 g/L K2HPO4; 1 g/L K2SO4; 0.1 g/L MgSO4-7H2O; 10 mM NH4Cl) with 4 g/L glycerolShake flask and filter culture175.0uM0.037 oCK12 NCM3722Mid-Log Phase7000000Bennett, B. D., Kimball, E. H., Gao, M., Osterhout, R., Van Dien, S. J., Rabinowitz, J. D. (2009). "Absolute metabolite concentrations and implied enzyme active site occupancy in Escherichia coli." Nat Chem Biol 5:593-599.19561621Gutnick minimal complete medium (4.7 g/L KH2PO4; 13.5 g/L K2HPO4; 1 g/L K2SO4; 0.1 g/L MgSO4-7H2O; 10 mM NH4Cl) with 4 g/L acetateShake flask and filter culture97.5uM0.037 oCK12 NCM3722Mid-Log Phase3900000Bennett, B. D., Kimball, E. H., Gao, M., Osterhout, R., Van Dien, S. J., Rabinowitz, J. D. (2009). "Absolute metabolite concentrations and implied enzyme active site occupancy in Escherichia coli." Nat Chem Biol 5:593-599.1956162148 mM Na2HPO4, 22 mM KH2PO4, 10 mM NaCl, 45 mM (NH4)2SO4, supplemented with 1 mM MgSO4, 1 mg/l thiamine·HCl, 5.6 mg/l CaCl2, 8 mg/l FeCl3, 1 mg/l MnCl2·4H2O, 1.7 mg/l ZnCl2, 0.43 mg/l CuCl2·2H2O, 0.6 mg/l CoCl2·2H2O and 0.6 mg/l Na2MoO4·2H2O. 4 g/L GlucoBioreactor, pH controlled, O2 and CO2 controlled, dilution rate: 0.2/h52.4uM0.037 oCBW25113Stationary Phase, glucose limited2096000Ishii, N., Nakahigashi, K., Baba, T., Robert, M., Soga, T., Kanai, A., Hirasawa, T., Naba, M., Hirai, K., Hoque, A., Ho, P. Y., Kakazu, Y., Sugawara, K., Igarashi, S., Harada, S., Masuda, T., Sugiyama, N., Togashi, T., Hasegawa, M., Takai, Y., Yugi, K., Arakawa, K., Iwata, N., Toya, Y., Nakayama, Y., Nishioka, T., Shimizu, K., Mori, H., Tomita, M. (2007). "Multiple high-throughput analyses monitor the response of E. coli to perturbations." Science 316:593-597.17379776Luria-Bertani (LB) mediaShake flask235.33uMtrue25.737 oCBL21 DE3Stationary phase cultures (overnight culture)941333102788Lin, Z., Johnson, L. C., Weissbach, H., Brot, N., Lively, M. O., Lowther, W. T. (2007). "Free methionine-(R)-sulfoxide reductase from Escherichia coli reveals a new GAF domain function." Proc Natl Acad Sci U S A 104:9597-9602.17535911Luria-Bertani (LB) mediaShake flask0.22uMtrue0.0137 oCBL21 DE3Stationary phase cultures (overnight culture)87134Lin, Z., Johnson, L. C., Weissbach, H., Brot, N., Lively, M. O., Lowther, W. T. (2007). "Free methionine-(R)-sulfoxide reductase from Escherichia coli reveals a new GAF domain function." Proc Natl Acad Sci U S A 104:9597-9602.17535911