2.02012-05-31 13:01:47 -06002015-09-13 12:56:09 -0600ECMDB00883M2MDB000196L-ValineValine is an alpha-amino acid with the chemical formula HO2CCH(NH2)CH(CH3)2. L-Valine is one of 20 proteinogenic amino acids. Its codons are GUU, GUC, GUA, and GUG. This amino acid is classified as nonpolar. Along with leucine and isoleucine, valine is a branched-chain amino acid. It is named after the plant valerian. (Wikipedia)(2S)-2-Amino-3-methylbutanoate(2S)-2-Amino-3-methylbutanoic acid(S)-2-amino-3-methyl-Butanoate(S)-2-amino-3-methyl-Butanoic acid(S)-2-Amino-3-methylbutanoate(S)-2-Amino-3-methylbutanoic acid(S)-2-Amino-3-methylbutyrate(S)-2-Amino-3-methylbutyric acid(S)-a-Amino-b-methylbutyrate(S)-a-Amino-b-methylbutyric acid(S)-alpha-Amino-beta-methylbutyrate(S)-alpha-Amino-beta-methylbutyric acid(S)-Valine(S)-α-amino-β-Methylbutyrate(S)-α-amino-β-Methylbutyric acid2-Amino-3-methylbutanoate2-Amino-3-methylbutanoic acid2-Amino-3-methylbutyrate2-Amino-3-methylbutyric acidL-(+)-a-AminoisovalerateL-(+)-a-Aminoisovaleric acidL-(+)-alpha-AminoisovalerateL-(+)-alpha-Aminoisovaleric acidL-(+)-α-AminoisovalerateL-(+)-α-Aminoisovaleric acidL-a-Amino-b-methylbutyrateL-a-Amino-b-methylbutyric acidL-alpha-Amino-beta-methylbutyrateL-alpha-Amino-beta-methylbutyric acidL-ValineL-α-amino-β-MethylbutyrateL-α-amino-β-Methylbutyric acidVValValineC5H11NO2117.1463117.078978601(2S)-2-amino-3-methylbutanoic acidL-valine72-18-4CC(C)[C@H](N)C(O)=OInChI=1S/C5H11NO2/c1-3(2)4(6)5(7)8/h3-4H,6H2,1-2H3,(H,7,8)/t4-/m0/s1KZSNJWFQEVHDMF-BYPYZUCNSA-NSolidCytosolExtra-organismPeriplasmlogp-2.29logs0.26solubility2.14e+02 g/lmelting_point295-300 oClogp-2pka_strongest_acidic2.72pka_strongest_basic9.6iupac(2S)-2-amino-3-methylbutanoic acidaverage_mass117.1463mono_mass117.078978601smilesCC(C)[C@H](N)C(O)=OformulaC5H11NO2inchiInChI=1S/C5H11NO2/c1-3(2)4(6)5(7)8/h3-4H,6H2,1-2H3,(H,7,8)/t4-/m0/s1inchikeyKZSNJWFQEVHDMF-BYPYZUCNSA-Npolar_surface_area63.32refractivity29.49polarizability12.19rotatable_bond_count2acceptor_count3donor_count2physiological_charge0formal_charge0Alanine, aspartate and glutamate metabolismec00250Valine, leucine and isoleucine biosynthesisec00290Pantothenate and CoA biosynthesisThe CoA biosynthesis requires compounds from two other pathways: aspartate metabolism and valine biosynthesis. It requires a Beta-Alanine and R-pantoate.
The compound (R)-pantoate is generated in two reactions, as shown by the interaction of alpha-ketoisovaleric acid, 5,10 methylene-THF and water through a 3-methyl-2-oxobutanoate hydroxymethyltransferase resulting in a tetrahydrofolic acid and a 2-dehydropantoate. This compound interacts with hydrogen through a NADPH driven acetohydroxy acid isomeroreductase resulting in the release of NADP and R-pantoate.
On the other hand L-aspartic acid interacts with a hydrogen ion and gets decarboxylated through an Aspartate 1- decarboxylase resulting in a carbon dioxide and a Beta-alanine.
Beta-alanine and R-pantoate interact with an ATP driven pantothenate synthetase resulting in pyrophosphate, AMP, hydrogen ion and pantothenic acid.
Pantothenic acid is phosphorylated through a ATP-driven pantothenate kinase resulting in a ADP, a hydrogen ion and D-4'-Phosphopantothenate. This compound interacts with a CTP and a L-cysteine resulting in a fused 4'-phosphopantothenoylcysteine decarboxylase and phosphopantothenoylcysteine synthetase resulting in a hydrogen ion, a pyrophosphate, a CMP and 4-phosphopantothenoylcysteine.
The latter compound interacts with a hydrogen ion through a fused 4'-phosphopantothenoylcysteine decarboxylase and phosphopantothenoylcysteine synthetase resulting in a carbon dioxide release and a 4-phosphopantetheine. This compound interacts with an ATP, hydrogen ion and an phosphopantetheine adenylyltransferase resulting in a release of pyrophosphate, and dephospho-CoA.
Dephospho-CoA reacts with an ATP driven dephospho-CoA kinase resulting in a ADP , a hydrogen ion and a Coenzyme A.
. The latter is converted into (R)-4'-phosphopantothenate is two steps, involving a β-alanine ligase and a kinase. In most organsims the ligase acts before the kinase (EC 6.3.2.1, pantoate—β-alanine ligase (AMP-forming) followed by EC 2.7.1.33, pantothenate kinase, as described in phosphopantothenate biosynthesis I and phosphopantothenate biosynthesis II. However, in archaea the order is reversed, and EC 2.7.1.169, pantoate kinase acts before EC 6.3.2.36, 4-phosphopantoate—β-alanine ligase, as described in phosphopantothenate biosynthesis III.
The kinases are feedback inhibited by CoA itself, accounting for the primary regulatory mechanism of CoA biosynthesis. The addition of L-cysteine to (R)-4'-phosphopantothenate, resulting in the formation of R-4'-phosphopantothenoyl-L-cysteine (PPC), is followed by decarboxylation of PPC to 4'-phosphopantetheine. The ultimate reaction is catalyzed by EC 2.7.1.24, dephospho-CoA kinase, which converts 4'-phosphopantetheine to CoA. All enzymes of this pathway are essential for growth.
The reactions in the biosynthetic route towards CoA are identical in most organisms, although there are differences in the functionality of the involved enzymes. In plants every step is catalyzed by single monofunctional enzymes, whereas in bacteria and mammals bifunctional enzymes are often employed [Rubio06].PW000828ec00770MetabolicAminoacyl-tRNA biosynthesisec00970Propanoate metabolism
Starting from L-threonine, this compound is deaminated through a threonine deaminase resulting in a hydrogen ion, a water molecule and a (2z)-2-aminobut-2-enoate. The latter compound then isomerizes to a 2-iminobutanoate, This compound then reacts spontaneously with hydrogen ion and a water molecule resulting in a ammonium and a 2-Ketobutyric acid. The latter compound interacts with CoA through a pyruvate formate-lyase / 2-ketobutyrate formate-lyase resulting in a formic acid and a propionyl-CoA.
Propionyl-CoA can then be processed either into a 2-methylcitric acid or into a propanoyl phosphate.
Propionyl-CoA interacts with oxalacetic acid and a water molecule through a 2-methylcitrate synthase resulting in a hydrogen ion, a CoA and a 2-Methylcitric acid.The latter compound is dehydrated through a 2-methylcitrate dehydratase resulting in a water molecule and cis-2-methylaconitate. The latter compound is then dehydrated by a
bifunctional aconitate hydratase 2 and 2-methylisocitrate dehydratase resulting in a water molecule and methylisocitric acid. The latter compound is then processed by 2-methylisocitrate lyase resulting in a release of succinic acid and pyruvic acid.
Succinic acid can then interact with a propionyl-CoA through a propionyl-CoA:succinate CoA transferase resulting in a propionic acid and a succinyl CoA. Succinyl-CoA is then isomerized through a methylmalonyl-CoA mutase resulting in a methylmalonyl-CoA. This compound is then decarboxylated through a methylmalonyl-CoA decarboxylase resulting in a release of Carbon dioxide and Propionyl-CoA.
ropionyl-CoA interacts with a phosphate through a phosphate acetyltransferase / phosphate propionyltransferase resulting in a CoA and a propanoyl phosphate.
Propionyl-CoA can react with a phosphate through a phosphate acetyltransferase / phosphate propionyltransferase resulting in a CoA and a propanoyl phosphate. The latter compound is then dephosphorylated through a ADP driven acetate kinase/propionate kinase protein complex resulting in an ATP and Propionic acid.
Propionic acid can be processed by a reaction with CoA through a ATP-driven propionyl-CoA synthetase resulting in a pyrophosphate, an AMP and a propionyl-CoA.PW000940ec00640MetabolicValine, leucine and isoleucine degradationec00280ABC transportersec02010Metabolic pathwayseco01100L-alanine metabolismL-alanine is an essential component of proteins and peptidoglycan. The latter also contains about three molecules of D-alanine for every L-alanine. Only about 10 percent of the total alanine synthesized flows into peptidoglycan.
There are at least 3 ways to begin the biosynthesis of alanine.
The first method for alanine biosynthesis begins with L-cysteine produced from L-cysteine biosynthesis pathway. L-cysteine reacts with an [L-cysteine desulfurase] L-cysteine persulfide through a cysteine desulfurase resulting in a release of [L-cysteine desulfurase] l-cysteine persulfide and L-alanine.
The second method starts with pyruvic acid reacting with L-glutamic acid through a glutamate-pyruvate aminotransferase resulting in a oxoglutaric acid and L-alanine.
The third method starts with L-glutamic acid interacting with Alpha-ketoisovaleric acid through a valine transaminase resulting in an oxoglutaric acid and L-valine. L-valine reacts with pyruvic acid through a valine-pyruvate aminotransferase resulting Alpha-ketoisovaleric acid and L-alanine.
This first step of the pathway, which can be catalyzed by either of two racemases( biosynthetic or catabolic), also serves an essential role in biosynthesis because its product, D-alanine, is an essential component of cell wall peptidoglycan (murein). D-alanine is metabolized by an ATP driven D-alanine ligase A and B resulting in D-alanyl-D-alanine. This product is incorporated into the peptidoglycan biosynthesis.
L-alanine is metabolized with alanine racemase, either catabolic or metabolic resulting in a D-alanine. This compound reacts with water and a quinone through a
D-amino acid dehydrogenase resulting in Pyruvic acid, hydroquinone and ammonium, thus entering the central metabolism and thereby can serve as a total source of carbon and energy. This pathway is unique among those through which L-amino acids are degraded, in that the L form must first be converted to the D form.
D-alanine, is an essential component of cell wall peptidoglycan (murein). The role of the alr racemase is predominately biosynthetic: it is produced constitutively in small amounts. The role of the dadX racemase is degradative: it is induced to high levels by alanine and is subject to catabolite repression.
PW000788MetabolicSecondary Metabolites: Valine and I-leucine biosynthesis from pyruvateThe biosynthesis of Valine and L-leucine from pyruvic acid starts with pyruvic acid interacting with a hydrogen ion through a acetolactate synthase / acetohydroxybutanoate synthase resulting in a release of a carbon dioxide, a (S)-2-acetolactate. The latter compound then interacts with a hydrogen ion through a NADPH-driven acetohydroxy acid isomeroreductase resulting in the release of a NADP, a (R) 2,3-dihydroxy-3-methylvalerate. The latter compound is then dehydrated by a dihydroxy acid dehydratase resulting in the release of a water molecule an 3-methyl-2-oxovaleric acid.
The 3-methyl-2-oxovaleric acid can produce an L-valine by interacting with a L-glutamic acid through a Valine Transaminase resulting in the release of a Oxoglutaric acid and a L-valine.
The 3-methyl-2-oxovaleric acid then interacts with an acetyl-CoA and a water molecule through a 2-isopropylmalate synthase resulting in the release of a hydrogen ion, a Coenzyme A and a 2-Isopropylmalic acid. The isopropylimalic acid is then hydrated by interacting with a isopropylmalate isomerase resulting in a 3-isopropylmalate. This compound then interacts with an NAD driven 3-isopropylmalate dehydrogenase resulting in a NADH, a hydrogen ion and a 2-isopropyl-3-oxosuccinate. The latter compound then interacts with hydrogen ion spontaneously resulting in a carbon dioxide and a ketoleucine. The ketoleucine then interacts with a L-glutamic acid through a branched-chain amino-acid aminotransferase resulting in the oxoglutaric acid and L-leucine.PW000978MetabolicValine Biosynthesis
The pathway of valine biosynthesis starts with pyruvic acid interacting with a hydrogen ion through a acetolactate synthase / acetohydroxybutanoate synthase or a acetohydroxybutanoate synthase / acetolactate synthase resulting in the release of carbon dioxide and (S)-2-acetolactate. The latter compound then interacts with a hydrogen ion through an NADPH driven
acetohydroxy acid isomeroreductase resulting in the release of a NADP and an (R) 2,3-dihydroxy-3-methylvalerate. The latter compound is then dehydrated by a
dihydroxy acid dehydratase resulting in the release of water and isovaleric acid. Isovaleric acid interacts with an L-glutamic acid through a Valine Transaminase resulting in a oxoglutaric acid and an L-valine.
L-valine is then transported into the periplasmic space through a L-valine efflux transporter.PW000812MetabolictRNA 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-PWYalanine biosynthesis IALANINE-VALINESYN-PWYvaline biosynthesisVALSYN-PWYSpecdb::CMs662Specdb::CMs663Specdb::CMs664Specdb::CMs665Specdb::CMs666Specdb::CMs912Specdb::CMs967Specdb::CMs2760Specdb::CMs30029Specdb::CMs30030Specdb::CMs30383Specdb::CMs30384Specdb::CMs30615Specdb::CMs30616Specdb::CMs30725Specdb::CMs30802Specdb::CMs31254Specdb::CMs31255Specdb::CMs37823Specdb::CMs134289Specdb::CMs142023Specdb::CMs1080931Specdb::CMs1080933Specdb::CMs1080935Specdb::EiMs1986Specdb::NmrOneD1279Specdb::NmrOneD1582Specdb::NmrOneD4778Specdb::NmrOneD7862Specdb::NmrOneD7863Specdb::NmrOneD7864Specdb::NmrOneD7865Specdb::NmrOneD7866Specdb::NmrOneD7867Specdb::NmrOneD7868Specdb::NmrOneD7869Specdb::NmrOneD7870Specdb::NmrOneD7871Specdb::NmrOneD7872Specdb::NmrOneD7873Specdb::NmrOneD7874Specdb::NmrOneD7875Specdb::NmrOneD7876Specdb::NmrOneD7877Specdb::NmrOneD7878Specdb::NmrOneD7879Specdb::NmrOneD7880Specdb::NmrOneD7881Specdb::NmrOneD166439Specdb::MsMs1244Specdb::MsMs1245Specdb::MsMs1246Specdb::MsMs4762Specdb::MsMs4763Specdb::MsMs4764Specdb::MsMs4765Specdb::MsMs4766Specdb::MsMs4767Specdb::MsMs4768Specdb::MsMs4769Specdb::MsMs4770Specdb::MsMs4771Specdb::MsMs4772Specdb::MsMs4773Specdb::MsMs4774Specdb::MsMs4775Specdb::MsMs4776Specdb::MsMs4777Specdb::MsMs4783Specdb::MsMs4784Specdb::MsMs4785Specdb::MsMs178806Specdb::MsMs178807Specdb::MsMs178808Specdb::NmrTwoD1041Specdb::NmrTwoD1524HMDB0088311826050C0018316414VALVAL_LFZWvalineKeseler, I. 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J Invest Dermatol. 2005 Aug;125(2):256-63.16098035Jensen PK, Jacobsen NO: Studies of D-amino acid oxidase activity in human epidermis and cultured human epidermal cells. Arch Dermatol Res. 1984;276(1):57-64.6142701Kurpad AV, Regan MM, Raj TD, Gnanou JV, Rao VN, Young VR: The daily valine requirement of healthy adult Indians determined by the 24-h indicator amino acid balance approach. Am J Clin Nutr. 2005 Aug;82(2):373-9.16087981Kinoshita, Shukuo; Udaka, Shigezo. L-Valine production by fermentation. (1962), 2 pp.http://hmdb.ca/system/metabolites/msds/000/000/797/original/HMDB00883.pdf?1358894699Valyl-tRNA synthetaseP07118SYV_ECOLIvalShttp://ecmdb.ca/proteins/P07118.xmlValine--pyruvate aminotransferaseP09053AVTA_ECOLIavtAhttp://ecmdb.ca/proteins/P09053.xmlHigh-affinity branched-chain amino acid transport system permease protein livHP0AEX7LIVH_ECOLIlivHhttp://ecmdb.ca/proteins/P0AEX7.xmlHigh-affinity branched-chain amino acid transport system permease protein livMP22729LIVM_ECOLIlivMhttp://ecmdb.ca/proteins/P22729.xmlUncharacterized aminotransferase yfbQP0A959YFBQ_ECOLIyfbQhttp://ecmdb.ca/proteins/P0A959.xmlBranched-chain-amino-acid aminotransferaseP0AB80ILVE_ECOLIilvEhttp://ecmdb.ca/proteins/P0AB80.xmlHigh-affinity branched-chain amino acid transport ATP-binding protein livGP0A9S7LIVG_ECOLIlivGhttp://ecmdb.ca/proteins/P0A9S7.xmlLeu/Ile/Val-binding proteinP0AD96LIVJ_ECOLIlivJhttp://ecmdb.ca/proteins/P0AD96.xmlHigh-affinity branched-chain amino acid transport ATP-binding protein livFP22731LIVF_ECOLIlivFhttp://ecmdb.ca/proteins/P22731.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.xmlHigh-affinity branched-chain amino acid transport system permease protein livHP0AEX7LIVH_ECOLIlivHhttp://ecmdb.ca/proteins/P0AEX7.xmlHigh-affinity branched-chain amino acid transport system permease protein livMP22729LIVM_ECOLIlivMhttp://ecmdb.ca/proteins/P22729.xmlOuter membrane protein NP77747OMPN_ECOLIompNhttp://ecmdb.ca/proteins/P77747.xmlOuter membrane pore protein EP02932PHOE_ECOLIphoEhttp://ecmdb.ca/proteins/P02932.xmlHigh-affinity branched-chain amino acid transport ATP-binding protein livGP0A9S7LIVG_ECOLIlivGhttp://ecmdb.ca/proteins/P0A9S7.xmlLeu/Ile/Val-binding proteinP0AD96LIVJ_ECOLIlivJhttp://ecmdb.ca/proteins/P0AD96.xmlHigh-affinity branched-chain amino acid transport ATP-binding protein livFP22731LIVF_ECOLIlivFhttp://ecmdb.ca/proteins/P22731.xmlUncharacterized protein ygaHP43667YGAH_ECOLIygaHhttp://ecmdb.ca/proteins/P43667.xmlOuter membrane protein FP02931OMPF_ECOLIompFhttp://ecmdb.ca/proteins/P02931.xmlBranched-chain amino acid transport system 2 carrier proteinP0AD99BRNQ_ECOLIbrnQhttp://ecmdb.ca/proteins/P0AD99.xmlInner membrane protein ygaZP76630YGAZ_ECOLIygaZhttp://ecmdb.ca/proteins/P76630.xmlOuter membrane protein CP06996OMPC_ECOLIompChttp://ecmdb.ca/proteins/P06996.xmlAdenosine triphosphate + Water + L-Valine > ADP + Hydrogen ion + Phosphate + L-ValineABC-36-RXNAdenosine triphosphate + Water + L-Valine > ADP + Hydrogen ion + Phosphate + L-ValineABC-36-RXNalpha-Ketoisovaleric acid + L-Alanine <> Pyruvic acid + L-Valine + a-Ketoisovaleric acidR01215VALINE-PYRUVATE-AMINOTRANSFER-RXNalpha-Ketoglutarate + L-Valine <> alpha-Ketoisovaleric acid + L-GlutamateR01214Adenosine triphosphate + tRNA(Val) + L-Valine + tRNA(Val) <> Adenosine monophosphate + Pyrophosphate + L-Valyl-tRNA(Val) + L-Valyl-tRNA(Val)R03665L-Valine + Pyruvic acid <> alpha-Ketoisovaleric acid + L-AlanineR01215Adenosine triphosphate + L-Valine + tRNA(Val) <> Adenosine monophosphate + Pyrophosphate + L-Valyl-tRNA(Val)R03665Adenosine triphosphate + L-Valine + Water > ADP + Phosphate + L-Valine + Hydrogen ionABC-36-RXNAdenosine triphosphate + L-Valine + Water > ADP + Phosphate + L-Valine + Hydrogen ionABC-36-RXNL-Valine + Oxoglutaric acid <> alpha-Ketoisovaleric acid + L-GlutamateBRANCHED-CHAINAMINOTRANSFERVAL-RXNL-Valine + Pyruvic acid > a-Ketoisovaleric acid + L-AlanineL-Valine + Oxoglutaric acid > a-Ketoisovaleric acid + L-GlutamateAdenosine triphosphate + L-Valine + tRNA(Val) > Adenosine monophosphate + Pyrophosphate + L-valyl-tRNA(Val)L-Valine + Pyruvic acid + L-Valine > L-Alanine + a-Ketoisovaleric acid + L-AlaninePW_R002662a-Ketoisovaleric acid + L-Glutamic acid + L-Glutamate > Oxoglutaric acid + L-Valine + L-ValinePW_R002663Isovaleric acid + L-Glutamic acid + L-Glutamate > Oxoglutaric acid + L-Valine + L-ValinePW_R0028863-Methyl-2-oxovaleric acid + L-Glutamic acid + 3-Methyl-2-oxovaleric acid + L-Glutamate > Oxoglutaric acid + L-Valine + L-ValinePW_R003714L-Valine + Adenosine triphosphate + Hydrogen ion + tRNA(Val) + L-Valine > Adenosine monophosphate + Pyrophosphate + L-Valyl-tRNA(Val)PW_R002831L-Valine + Adenosine triphosphate + Water + L-Valine > L-Valine + Adenosine diphosphate + Pyrophosphate + Hydrogen ion + ADPPW_RCT000104Adenosine triphosphate + tRNA(Val) + L-Valine <> Adenosine monophosphate + Pyrophosphate + L-Valyl-tRNA(Val)Gutnick 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 culture4020.0uM0.037 oCK12 NCM3722Mid-Log Phase160800000Bennett, 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 culture2290.0uM0.037 oCK12 NCM3722Mid-Log Phase91600000Bennett, 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 culture1070.0uM0.037 oCK12 NCM3722Mid-Log Phase42800000Bennett, 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/h181.0uM0.037 oCBW25113Stationary Phase, glucose limited7240000Ishii, 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 flask1645.0uMtrue134.037 oCBL21 DE3Stationary phase cultures (overnight culture)6580000536000Lin, 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 flask1623.33uMtrue107.8637 oCBL21 DE3Stationary phase cultures (overnight culture)6493333431432Lin, 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