2.02012-05-31 10:23:06 -06002015-09-13 12:56:06 -0600ECMDB00182M2MDB000075L-LysineL-lysine is an alpha-amino acid with the chemical formula HO2CCH(NH2)(CH2)4NH2. Lysine is a basic amino acid as are arginine and histidine. Lysine is a proteogenic amino acid, meaning that it is used in protein synthesis. Lysine typically constitutes about 7-8% of an average protein. The epsilon-amino group often participates in hydrogen bonding and as a general base in catalysis. Common posttranslational modifications include methylation of the epsilon-amino group, giving methyl-, dimethyl-, and trimethyllysine. In bacteria, lysine is synthesized from aspartic acid, which is first converted to aspartyl-semialdehyde. (+)-S-Lysine(S)-2,6-diamino-Hexanoate(S)-2,6-diamino-Hexanoic acid(S)-2,6-Diaminohexanoate(S)-2,6-Diaminohexanoic acid(S)-a,e-Diaminocaproate(S)-a,e-Diaminocaproic acid(S)-Lysine2,6-Diaminohexanoate2,6-Diaminohexanoic acid6-Amino-Aminutrin6-Amino-L-NorleucineA-LysineAlpha-LysineAminutrinH-Lys-ohKL-(+)-LysineL-2,6-DiainohexanoateL-2,6-Diainohexanoic acidL-2,6-DiaminocaproateL-2,6-Diaminocaproic acidL-LysLysLysineLysine acidα-LysineC6H14N2O2146.1876146.105527702(2S)-2,6-diaminohexanoic acidL-lysine56-87-1NCCCC[C@H](N)C(O)=OInChI=1S/C6H14N2O2/c7-4-2-1-3-5(8)6(9)10/h5H,1-4,7-8H2,(H,9,10)/t5-/m0/s1KDXKERNSBIXSRK-YFKPBYRVSA-NSolidCytosolExtra-organismPeriplasmlogp-3.76logs-0.14solubility1.05e+02 g/lmelting_point224.5 oClogp-3.2pka_strongest_acidic2.74pka_strongest_basic10.29iupac(2S)-2,6-diaminohexanoic acidaverage_mass146.1876mono_mass146.105527702smilesNCCCC[C@H](N)C(O)=OformulaC6H14N2O2inchiInChI=1S/C6H14N2O2/c7-4-2-1-3-5(8)6(9)10/h5H,1-4,7-8H2,(H,9,10)/t5-/m0/s1inchikeyKDXKERNSBIXSRK-YFKPBYRVSA-Npolar_surface_area89.34refractivity37.81polarizability15.84rotatable_bond_count5acceptor_count4donor_count3physiological_charge1formal_charge0Tropane, piperidine and pyridine alkaloid biosynthesisec00960Lysine biosynthesisLysine is biosynthesized from L-aspartic acid. L-aspartic acid can be incorporated into the cell through various methods: C4 dicarboxylate / orotate:H+ symporter ,
glutamate / aspartate : H+ symporter GltP, dicarboxylate transporter , C4 dicarboxylate / C4 monocarboxylate transporter DauA, glutamate / aspartate ABC transporter
L-aspartic acid is phosphorylated by an ATP-driven Aspartate kinase resulting in ADP and L-aspartyl-4-phosphate. L-aspartyl-4-phosphate is then dehydrogenated through an NADPH driven aspartate semialdehyde dehydrogenase resulting in a release of phosphate, NADP and L-aspartic 4-semialdehyde (involved in methionine biosynthesis).
L-aspartic 4-semialdehyde interacts with a pyruvic acid through a 4-hydroxy-tetrahydrodipicolinate synthase resulting in a release of hydrogen ion, water and
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate. The latter compound is then reduced by an NADPH driven 4-hydroxy-tetrahydrodipicolinate reductase resulting in a release of water, NADP and (S)-2,3,4,5-tetrahydrodipicolinate, This compound interacts with succinyl-CoA and water through a tetrahydrodipicolinate succinylase resulting in a release of coenzyme A and N-Succinyl-2-amino-6-ketopimelate. This compound interacts with L-glutamic acid through a N-succinyldiaminopimelate aminotransferase resulting in oxoglutaric acid, N-succinyl-L,L-2,6-diaminopimelate. The latter compound is then desuccinylated by reacting with water through a N-succinyl-L-diaminopimelate desuccinylase resulting in a succinic acid and L,L-diaminopimelate. This compound is then isomerized through a diaminopimelate epimerase resulting in a meso-diaminopimelate (involved in peptidoglyccan biosynthesis I). This compound is then decarboxylated by a diaminopimelate decarboxylase resulting in a release of carbon dioxide and L-lysine.
L-lysine is then incorporated into lysine degradation pathway. Lysine also regulate its own biosynthesis by repressing dihydrodipicolinate synthase and also repressing lysine-sensitive aspartokinase 3.
A metabolic connection joins synthesis of an amino acid, lysine, to synthesis of cell wall material. Diaminopimelate is a precursor both for lysine and for cell wall components. The synthesis of lysine, methionine and threonine share two reactions at the start of the three pathways, the reactions converting L-aspartate to L-aspartate semialdehyde. The reaction involving aspartate kinase is carried out by three isozymes, one specific for synthesis of each end product amino acid. Each of the three aspartate kinase isozymes is regulated by its corresponding end product amino acid.PW000771ec00300MetabolicAminoacyl-tRNA biosynthesisec00970Biotin metabolismBiotin (vitamin H or vitamin B7) is the essential cofactor of biotin-dependent carboxylases, such as pyruvate carboxylase and acetyl-CoA carboxylase.In E. coli and many organisms, pimelate thioester is derived from malonyl-ACP. The pathway starts with a malonyl-[acp] interacting with S-adenosylmethionine through a biotin synthesis protein BioC resulting in a S-adenosylhomocysteine and a malonyl-[acp] methyl ester. The latter compound is then involved in the synthesis of a 3-ketoglutaryl-[acp] methyl ester through a 3-oxoacyl-[acyl-carrier-protein] synthase. The compound 3-ketoglutaryl-[acp] methyl ester is reduced by a NADPH mediated 3-oxoacyl-[acyl-carrier-protein] reductase resulting in a 3R-hydroxyglutaryl-[acp] methyl ester. This compound is then dehydrated through ad (3R)-hydroxymyristoyl-[acp] dehydratase producing a enoylglutaryl-[acp] methyl ester. This compound is then reduced through a NADPH mediated enoyl-acp-reductase [NADH] resulting in a glutaryl-[acp] methyl ester. This compound interacts with a malonyl-[acp] through a 3-oxoacyl-[acp] synthase 2 resulting in a 3-ketopimeloyl [acp] methyl ester. This compound is then reduced through a NADPH 3-oxoacyl [acp] reductase producing a 3-hydroxypimeloyl-[acp] methyl ester and then dehydrated by (3R)-hydroxymyristoyl-[acp] dehydratase to produce a enoylpimeloyl-[acp] methyl ester. This compound is then reduced by a NADPH dependent enoyl-[acp]reductase resulting in a pimeloyl-[acp] methyl ester. This compound then reacts with water through a carboxylesterase resulting in a pimeloyl-[acp] and a methanol. The pimeloyl-acp reacts with L-alanine through a 8-amino-7-oxononanoate synthase resulting in 8-amino-7-oxononanoate which in turn reacts with S-adenosylmethionine through a 7,8 diaminonanoate transaminase resulting in a S-adenosyl-4-methylthio-2-oxobutanoate and 7,8 diaminononanoate. The latter compound is then dephosphorylated through a dethiobiotin synthetase resulting in a dethiobiotin. This compound interacts with a sulfurated[sulfur carrier), a hydrogen ion and a S-adenosylmethionine through a biotin synthase to produce Biotin and releasing l-methionine and a 5-deoxyadenosine.
Biotin is then metabolized by a bifunctional protein resulting in pyrophosphate and Biotinyl-5-AMP which in turn reacts with the same protein (bifunctional protein birA resulting ina biotin caroxyl carrying protein.This product then enters the fatty acid biosynthesis.
PW000762ec00780MetabolicLysine degradationec00310Microbial metabolism in diverse environmentsec01120ABC transportersec02010Metabolic pathwayseco01100Lysine Degradation I
Under conditions of anaerobiosis and phosphate starvation (believed to reflect conditions in the gut), E. coli converts glucose to weak organic acids which, though they are excreted, can reenter the cell and cause bactericidal acid stress even at only moderately acidic pH. Acid resistance system 4 (AR4) is the lysine-dependent acid resistance system which allows for the survival of E. coli under these conditions when lysine is available. AR4 couples the transport activity of a lysine:cadaverine antiporter, CadB, with lysine decarboxylase, CadA. CadB functions by exchanging external lysine for internal cadaverine.
Lysine is imported into the cell through CadB or generated in the cell from aspartic acid. Within the cell, lysine is decarboxylated by CadA to cadaverine, releasing CO2 and replacing it with a proton. Cadaverine is then exported through CadB. This effectively consumes protons within the cytoplasm, raising the pH. The glutamate-dependent acid resistance system (AR2) is also able to provide acid resistance to E. coli growing under conditions of anaerobiosis and phosphate starvation, but to a slightly lesser degree than AR4 possibly due to the different pH optimums of their respective decarboxylase enzymes. AR2 is more efficient than AR3 or AR4 as a mediator of acid resistance at low pH.PW000772Metabolicinner membrane transportlist of inner membrane transport complexes, transporting compounds from the periplasmic space to the cytosol
This pathway should be updated regularly with the new inner membrae transports addedPW000786MetabolictRNA Charging 2This pathway groups together all E. coli tRNA charging reactions.PW000803MetabolictRNA chargingThis pathway groups together all E. coli tRNA charging reactions.PW000799MetabolicFructoselysine and Psicoselysine DegradationFructosamines are generated non-enzymatically by a condensation of glucose with primary amines, followed by an Amadori rearrangement. Fructoselysine appears to be metabolized by bacteria in the human hind gut. E. coli can grow on fructoselysine or psicoselysine as the sole carbon source. Growth on fructoselysine induces the production of the enzymes of the fructoselysine degradation pathway. (EcoCyc)PW002049Metabolicaminopropylcadaverine biosynthesisPolyamines are important for cell growth and are believed to be involved in many processes including DNA, RNA, and protein synthesis, as well as membrane integrity and resistance to stress, to name a few. Cadaverine and aminopropylcadaverine are alternative polyamines that can at least partially substitute for purtrescine and spermidine, the primary polyamines found in E. coli. Lysine is decarboxylated to form cadaverine which is then converted to aminopropylcadaverine by the aminopropyltransferase, SpeE. (EcoCyc)PW002039MetabolictRNA chargingTRNA-CHARGING-PWYlysine biosynthesis IDAPLYSINESYN-PWYfructoselysine and psicoselysine degradationPWY0-521aminopropylcadaverine biosynthesisPWY0-1303lysine degradation IPWY0-461Specdb::CMs423Specdb::CMs424Specdb::CMs425Specdb::CMs1365Specdb::CMs1547Specdb::CMs1644Specdb::CMs2495Specdb::CMs30111Specdb::CMs30112Specdb::CMs30377Specdb::CMs30602Specdb::CMs30737Specdb::CMs30794Specdb::CMs31054Specdb::CMs31055Specdb::CMs31056Specdb::CMs32353Specdb::CMs37342Specdb::CMs148423Specdb::CMs1052863Specdb::CMs1052865Specdb::CMs1052867Specdb::CMs1052869Specdb::CMs1052871Specdb::NmrOneD1151Specdb::NmrOneD1194Specdb::NmrOneD4846Specdb::NmrOneD142750Specdb::NmrOneD142751Specdb::NmrOneD142752Specdb::NmrOneD142753Specdb::NmrOneD142754Specdb::NmrOneD142755Specdb::NmrOneD142756Specdb::NmrOneD142757Specdb::NmrOneD142758Specdb::NmrOneD142759Specdb::NmrOneD142760Specdb::NmrOneD142761Specdb::NmrOneD142762Specdb::NmrOneD142763Specdb::NmrOneD142764Specdb::NmrOneD142765Specdb::NmrOneD142766Specdb::NmrOneD142767Specdb::NmrOneD142768Specdb::NmrOneD142769Specdb::NmrOneD166351Specdb::NmrOneD166447Specdb::MsMs289Specdb::MsMs290Specdb::MsMs291Specdb::MsMs3408Specdb::MsMs3409Specdb::MsMs3410Specdb::MsMs3411Specdb::MsMs3412Specdb::MsMs3413Specdb::MsMs3414Specdb::MsMs3415Specdb::MsMs3416Specdb::MsMs3417Specdb::MsMs3418Specdb::MsMs3419Specdb::MsMs3420Specdb::MsMs3421Specdb::MsMs3422Specdb::MsMs3423Specdb::MsMs3424Specdb::MsMs3425Specdb::MsMs3429Specdb::MsMs3430Specdb::MsMs3431Specdb::MsMs3432Specdb::NmrTwoD985Specdb::NmrTwoD1191HMDB0018259625747C0004718019LYSLYS_LFZW_DHZ3L-LysineKeseler, 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-D114.22080510Vijayendran, C., Barsch, A., Friehs, K., Niehaus, K., Becker, A., Flaschel, E. (2008). "Perceiving molecular evolution processes in Escherichia coli by comprehensive metabolite and gene expression profiling." Genome Biol 9:R72.18402659van 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). 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Biochemical Preparations (1961), 8 85-8.http://hmdb.ca/system/metabolites/msds/000/000/128/original/HMDB00182.pdf?1358461504Diaminopimelate decarboxylaseP00861DCDA_ECOLIlysAhttp://ecmdb.ca/proteins/P00861.xmlHistidine transport ATP-binding protein hisPP07109HISP_ECOLIhisPhttp://ecmdb.ca/proteins/P07109.xmlLysyl-tRNA synthetaseP0A8N3SYK1_ECOLIlysShttp://ecmdb.ca/proteins/P0A8N3.xmlLysyl-tRNA synthetase, heat inducibleP0A8N5SYK2_ECOLIlysUhttp://ecmdb.ca/proteins/P0A8N5.xmlUncharacterized protein YjeAP0A8N7YJEA_ECOLIpoxAhttp://ecmdb.ca/proteins/P0A8N7.xmlLysine decarboxylase, inducibleP0A9H3LDCI_ECOLIcadAhttp://ecmdb.ca/proteins/P0A9H3.xmlFructoselysine 6-phosphate deglycaseP0AC00FRLB_ECOLIfrlBhttp://ecmdb.ca/proteins/P0AC00.xmlLysine decarboxylase, constitutiveP52095DCLZ_ECOLIldcChttp://ecmdb.ca/proteins/P52095.xmlHistidine transport system permease protein hisMP0AEU3HISM_ECOLIhisMhttp://ecmdb.ca/proteins/P0AEU3.xmlHistidine transport system permease protein hisQP52094HISQ_ECOLIhisQhttp://ecmdb.ca/proteins/P52094.xmlLysine-arginine-ornithine-binding periplasmic proteinP09551ARGT_ECOLIargThttp://ecmdb.ca/proteins/P09551.xmltRNA(Ile)-lysidine synthetase (EC:6.1.1.5)P52097tilShttp://ecmdb.ca/proteins/P52097.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.xmlLysine-specific permeaseP25737LYSP_ECOLIlysPhttp://ecmdb.ca/proteins/P25737.xmlHistidine transport system permease protein hisQP52094HISQ_ECOLIhisQhttp://ecmdb.ca/proteins/P52094.xmlLysine-arginine-ornithine-binding periplasmic proteinP09551ARGT_ECOLIargThttp://ecmdb.ca/proteins/P09551.xmlOuter membrane protein NP77747OMPN_ECOLIompNhttp://ecmdb.ca/proteins/P77747.xmlOuter membrane pore protein EP02932PHOE_ECOLIphoEhttp://ecmdb.ca/proteins/P02932.xmlOuter membrane protein FP02931OMPF_ECOLIompFhttp://ecmdb.ca/proteins/P02931.xmlProbable cadaverine/lysine antiporterP0AAE8CADB_ECOLIcadBhttp://ecmdb.ca/proteins/P0AAE8.xmlArginine exporter protein ArgOP11667ARGO_ECOLIargOhttp://ecmdb.ca/proteins/P11667.xmlOuter membrane protein CP06996OMPC_ECOLIompChttp://ecmdb.ca/proteins/P06996.xmlHydrogen ion + L-Lysine <> Cadaverine + Carbon dioxideR00462LYSDECARBOX-RXNAdenosine triphosphate + Water + L-Lysine > ADP + Hydrogen ion + L-Lysine + PhosphateABC-3-RXNAdenosine triphosphate + Water + L-Lysine > ADP + Hydrogen ion + L-Lysine + PhosphateABC-3-RXNAdenosine triphosphate + L-Lysine + tRNA(Lys) > Adenosine monophosphate + L-Lysine-tRNA (Lys) + PyrophosphateDiaminopimelic acid + Hydrogen ion > Carbon dioxide + L-LysineFructoselysine-6-phosphate + Water <> Glucose 6-phosphate + L-LysineRXN0-963Meso-2,6-Diaminoheptanedioate <> L-Lysine + Carbon dioxideR00451L-Lysine <> Cadaverine + Carbon dioxideR00462Adenosine triphosphate + L-Lysine + tRNA(Lys) + tRNA(Lys) <> Adenosine monophosphate + Pyrophosphate + L-Lysyl-tRNA + L-Lysyl-tRNAR03658[tRNA(Ile2)]-cytidine34 + L-Lysine + Adenosine triphosphate <> [tRNA(Ile2)]-lysidine34 + Adenosine monophosphate + Pyrophosphate + WaterR09597L-Lysine + Adenosine triphosphate + Water > L-Lysine + ADP + Phosphate + Hydrogen ionABC-3-RXNL-Lysine + Adenosine triphosphate + Water > L-Lysine + ADP + Phosphate + Hydrogen ionABC-3-RXNHydrogen ion + <i>meso</i>-diaminopimelate > L-Lysine + Carbon dioxideDIAMINOPIMDECARB-RXNHydrogen ion + L-Lysine > Carbon dioxide + CadaverineLYSDECARBOX-RXNL-Lysine (R)-beta-lysineRXN0-5192Meso-2,6-Diaminoheptanedioate > L-Lysine + Carbon dioxideL-Lysine > Cadaverine + Carbon dioxideL-Lysine > (R)-beta-lysineFructoselysine-6-phosphate + Water > Glucose 6-phosphate + L-LysineAdenosine triphosphate + L-Lysine + tRNA(Lys) > Adenosine monophosphate + Pyrophosphate + L-lysyl-tRNA(Lys)(tRNA(Ile2))-cytidine(34) + L-Lysine + Adenosine triphosphate > (tRNA(Ile2))-lysidine(34) + Adenosine monophosphate + Pyrophosphate + WaterBiocytin + Water > Biotin + L-Lysine + L-LysinePW_R002492Meso-2,6-Diaminoheptanedioate + Hydrogen ion > L-Lysine + Carbon dioxide + L-LysinePW_R002533L-Lysine + Hydrogen ion + L-Lysine > Cadaverine + Carbon dioxidePW_R002534L-Lysine + L-Lysine > CadaverinePW_R002535L-Lysine + Adenosine triphosphate + Hydrogen ion + tRNA(Lys) + L-Lysine > Adenosine monophosphate + Pyrophosphate + L-Lysyl-tRNAPW_R002840L-Lysine + Adenosine triphosphate + Water + L-Lysine > Adenosine diphosphate + Phosphate + Hydrogen ion + L-Lysine + ADPPW_RCT000110Fructoselysine-6-phosphate + Water <> β-D-glucose 6-phosphate + L-LysinePW_R005985Adenosine triphosphate + L-Lysine + tRNA(Lys) <> Adenosine monophosphate + Pyrophosphate + L-Lysyl-tRNAMeso-2,6-Diaminoheptanedioate <> L-Lysine + Carbon dioxideAdenosine triphosphate + L-Lysine + tRNA(Lys) <> Adenosine monophosphate + Pyrophosphate + L-Lysyl-tRNAGutnick 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 culture401.0uM0.037 oCK12 NCM3722Mid-Log Phase16040000Bennett, 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 culture762.0uM0.037 oCK12 NCM3722Mid-Log Phase30480000Bennett, 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 culture554.0uM0.037 oCK12 NCM3722Mid-Log Phase22160000Bennett, 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/h361.0uM0.037 oCBW25113Stationary Phase, glucose limited14440000Ishii, 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 flask567.33uMtrue31.537 oCBL21 DE3Stationary phase cultures (overnight culture)2269333126005Lin, 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