2.02012-05-31 10:22:41 -06002015-09-13 12:56:06 -0600ECMDB00167M2MDB000068L-ThreonineThreonine is an amino acid. It is converted to pyruvate via threonine dehydrogenase. An intermediate in this pathway can undergo thiolysis with CoA to produce acetyl-CoA and glycine. (Wikipedia)(2S,3R)-(-)-Threonine(2S,3R)-2-Amino-3-hydroxybutyrate(2S,3R)-2-Amino-3-hydroxybutyric acid(R-(R*,S*))-2-Amino-3-hydroxybutanoate(R-(R*,S*))-2-Amino-3-hydroxybutanoic acid(S)-Threonine2-Amino-3-hydroxybutanoate2-Amino-3-hydroxybutanoic acid2-Amino-3-hydroxybutyrate2-Amino-3-hydroxybutyric acidL-(-)-ThreonineL-2-Amino-3-hydroxybutyrateL-2-Amino-3-hydroxybutyric acidL-a-amino-b-HydroxybutyrateL-a-amino-b-Hydroxybutyric acidL-alpha-Amino-beta-hydroxybutyrateL-alpha-Amino-beta-hydroxybutyric acidL-thrL-α-amino-β-HydroxybutyrateL-α-amino-β-Hydroxybutyric acidTThrThreThreoninThreonine[R-(R*,S*)]-2-amino-3-hydroxy-Butanoate[R-(R*,S*)]-2-amino-3-hydroxy-Butanoic acid[R-(R*,S*)]-2-Amino-3-hydroxybutanoate[R-(R*,S*)]-2-Amino-3-hydroxybutanoic acidC4H9NO3119.1192119.058243159(2S,3R)-2-amino-3-hydroxybutanoic acidL-threonine72-19-5C[C@@H](O)[C@H](N)C(O)=OInChI=1S/C4H9NO3/c1-2(6)3(5)4(7)8/h2-3,6H,5H2,1H3,(H,7,8)/t2-,3+/m1/s1AYFVYJQAPQTCCC-GBXIJSLDSA-NSolidCytosolExtra-organismPeriplasmlogp-3.01logs0.60solubility4.77e+02 g/lmelting_point256 oClogp-3.5pka_strongest_acidic2.21pka_strongest_basic9iupac(2S,3R)-2-amino-3-hydroxybutanoic acidaverage_mass119.1192mono_mass119.058243159smilesC[C@@H](O)[C@H](N)C(O)=OformulaC4H9NO3inchiInChI=1S/C4H9NO3/c1-2(6)3(5)4(7)8/h2-3,6H,5H2,1H3,(H,7,8)/t2-,3+/m1/s1inchikeyAYFVYJQAPQTCCC-GBXIJSLDSA-Npolar_surface_area83.55refractivity26.46polarizability11.08rotatable_bond_count2acceptor_count4donor_count3physiological_charge0formal_charge0Glycine, serine and threonine metabolismec00260Valine, leucine and isoleucine biosynthesisec00290Vitamin B6 metabolismec00750Aminoacyl-tRNA biosynthesisec00970Porphyrin and chlorophyll metabolismec00860Propanoate 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.PW000940ec00640MetabolicMicrobial metabolism in diverse environmentsec01120ABC transportersec02010Metabolic pathwayseco01100Secondary Metabolites: threonine biosynthesis from aspartateThe biosynthesis of threonine starts with L-aspartic acid being phosphorylated by an ATP driven Aspartate kinase resulting in an a release of an ADP and an L-aspartyl-4-phosphate. This compound interacts with a hydrogen ion through an NADPH driven aspartate semialdehyde dehydrogenase resulting in the release of a phosphate, an NADP and a L-aspartate-semialdehyde.The latter compound interacts with a hydrogen ion through a NADPH driven aspartate kinase / homoserine dehydrogenase resulting in the release of an NADP and a L-homoserine. L-homoserine is phosphorylated through an ATP driven homoserine kinase resulting in the release of an ADP, a hydrogen ion and a O-phosphohomoserine. The latter compound then interacts with a water molecule threonine synthase resulting in the release of a phosphate and an L-threonine. PW000976Metabolicinner 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 addedPW000786Metabolicisoleucine biosynthesisIsoleucine biosynthesis begins with L-threonine from the threonine biosynthesis pathway. L-threonine interacts with a threonine dehydratase biosynthetic releasing water, a hydrogen ion and (2Z)-2-aminobut-2-enoate. This compound is isomerized into a 2-iminobutanoate which interacts with water and a hydrogen ion spontaneously, resulting in the release of ammonium and 2-ketobutyric acid. This compound reacts with pyruvic acid and hydrogen ion through an acetohydroxybutanoate synthase / acetolactate synthase 2 resulting in carbon dioxide and (S)-2-Aceto-2-hydroxybutanoic acid. The latter compound is reduced by an NADPH driven acetohydroxy acid isomeroreductase releasing NADP and acetohydroxy acid isomeroreductase. The latter compound is dehydrated by a dihydroxy acid dehydratase resulting in 3-methyl-2-oxovaleric acid.This compound reacts in a reversible reaction with L-glutamic acid through a Branched-chain-amino-acid aminotransferase resulting in oxoglutaric acid and L-isoleucine.
L-isoleucine can also be transported into the cytoplasm through two different methods: a branched chain amino acid ABC transporter or a
branched chain amino acid transporter BrnQ
y.
PW000818MetabolictRNA Charging 2This pathway groups together all E. coli tRNA charging reactions.PW000803MetabolictRNA chargingThis pathway groups together all E. coli tRNA charging reactions.PW000799Metabolicthreonine biosynthesisThe biosynthesis of threonine starts with oxalacetic acid interacting with an L-glutamic acid through an aspartate aminotransferase resulting in a oxoglutaric acid and an L-aspartic acid. The latter compound is then phosphorylated by an ATP driven Aspartate kinase resulting in an a release of an ADP and an L-aspartyl-4-phosphate. This compound interacts with a hydrogen ion through an NADPH driven aspartate semialdehyde dehydrogenase resulting in the release of a phosphate, an NADP and a L-aspartate-semialdehyde.The latter compound interacts with a hydrogen ion through a NADPH driven aspartate kinase / homoserine dehydrogenase resulting in the release of an NADP and a L-homoserine. L-homoserine is phosphorylated through an ATP driven homoserine kinase resulting in the release of an ADP, a hydrogen ion and a O-phosphohomoserine. The latter compound then interacts with a water molecule threonine synthase resulting in the release of a phosphate and an L-threonine. PW000817MetabolicL-threonine degradation to methylglyoxalL-threonine is degrade into methylglyoxal (pyruvaldehyde) by first reacting with a NDA dependent threonine dehydrogenase resulting in the release of a hydrogen ion, an NADH and a 2-amino-3-oxobutanoate. The latter compound reacts spontaneously with a hydrogen ion resulting in the release of a carbon dioxide and a aminoacetone. The aminoacetone in turn reacts with an oxygen and a water molecule through an aminoacetone oxidase resulting in the release of a hydrogen peroxide, ammonium and a methylglyoxal which can then be incorporated in the methylglyoxal degradation pathways.PW002106Metabolicisoleucine biosynthesis I (from threonine)ILEUSYN-PWYthreonine degradation IPWY-5437tRNA chargingTRNA-CHARGING-PWYthreonine degradation III (to methylglyoxal)THRDLCTCAT-PWYthreonine degradation IITHREONINE-DEG2-PWYthreonine degradation IVPWY-5436threonine biosynthesis from homoserineHOMOSER-THRESYN-PWYSpecdb::CMs399Specdb::CMs400Specdb::CMs1025Specdb::CMs1090Specdb::CMs2588Specdb::CMs30052Specdb::CMs30053Specdb::CMs30382Specdb::CMs30613Specdb::CMs30728Specdb::CMs31038Specdb::CMs31039Specdb::CMs37333Specdb::CMs170648Specdb::CMs1052537Specdb::CMs1052539Specdb::CMs1052541Specdb::CMs1052542Specdb::CMs1052544Specdb::CMs1052546Specdb::CMs1052548Specdb::CMs1052550Specdb::CMs1052552Specdb::CMs1052553Specdb::CMs1052555Specdb::NmrOneD1129Specdb::NmrOneD1184Specdb::NmrOneD4794Specdb::NmrOneD142650Specdb::NmrOneD142651Specdb::NmrOneD142652Specdb::NmrOneD142653Specdb::NmrOneD142654Specdb::NmrOneD142655Specdb::NmrOneD142656Specdb::NmrOneD142657Specdb::NmrOneD142658Specdb::NmrOneD142659Specdb::NmrOneD142660Specdb::NmrOneD142661Specdb::NmrOneD142662Specdb::NmrOneD142663Specdb::NmrOneD142664Specdb::NmrOneD142665Specdb::NmrOneD142666Specdb::NmrOneD142667Specdb::NmrOneD142668Specdb::NmrOneD142669Specdb::NmrOneD166491Specdb::MsMs263Specdb::MsMs264Specdb::MsMs265Specdb::MsMs3258Specdb::MsMs3259Specdb::MsMs3260Specdb::MsMs3261Specdb::MsMs3262Specdb::MsMs3263Specdb::MsMs3264Specdb::MsMs3265Specdb::MsMs3266Specdb::MsMs3267Specdb::MsMs3268Specdb::MsMs3269Specdb::MsMs3270Specdb::MsMs3271Specdb::MsMs3272Specdb::MsMs3273Specdb::MsMs3274Specdb::MsMs3275Specdb::MsMs3276Specdb::MsMs3277Specdb::MsMs3278Specdb::MsMs178482Specdb::NmrTwoD979Specdb::NmrTwoD1182HMDB0016762886051C0018816857THRTHR_LFZW_DHG1L-ThreonineKeseler, 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). 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Nippon Nogei Kagaku Kaishi (1965), 39(6), 2http://hmdb.ca/system/metabolites/msds/000/000/117/original/HMDB00167.pdf?1358894693Threonine synthaseP00934THRC_ECOLIthrChttp://ecmdb.ca/proteins/P00934.xmlThreonine dehydratase biosyntheticP04968THD1_ECOLIilvAhttp://ecmdb.ca/proteins/P04968.xmlL-threonine 3-dehydrogenaseP07913TDH_ECOLItdhhttp://ecmdb.ca/proteins/P07913.xmlSerine hydroxymethyltransferaseP0A825GLYA_ECOLIglyAhttp://ecmdb.ca/proteins/P0A825.xmlThreonyl-tRNA synthetaseP0A8M3SYT_ECOLIthrShttp://ecmdb.ca/proteins/P0A8M3.xmlClass B acid phosphataseP0AE22APHA_ECOLIaphAhttp://ecmdb.ca/proteins/P0AE22.xmlThreonine dehydratase catabolicP0AGF6THD2_ECOLItdcBhttp://ecmdb.ca/proteins/P0AGF6.xmlLow specificity L-threonine aldolaseP75823LTAE_ECOLIltaEhttp://ecmdb.ca/proteins/P75823.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.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.xmlThreonylcarbamoyl-AMP synthaseP45748TSAC_ECOLItsaChttp://ecmdb.ca/proteins/P45748.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.xmlThreonine/serine transporter tdcCB1XGT1TDCC_ECODHtdcChttp://ecmdb.ca/proteins/B1XGT1.xmlThreonine/serine transporter tdcCC4ZR30TDCC_ECOBWtdcChttp://ecmdb.ca/proteins/C4ZR30.xmlInner membrane transporter rhtAP0AA67RHTA_ECOLIrhtAhttp://ecmdb.ca/proteins/P0AA67.xmlThreonine/serine transporter tdcCP0AAD8TDCC_ECOLItdcChttp://ecmdb.ca/proteins/P0AAD8.xmlHigh-affinity branched-chain amino acid transport system permease protein livHP0AEX7LIVH_ECOLIlivHhttp://ecmdb.ca/proteins/P0AEX7.xmlSerine/threonine transporter sstTP0AGE4SSTT_ECOLIsstThttp://ecmdb.ca/proteins/P0AGE4.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.xmlThreonine efflux proteinP0AG38RHTC_ECOLIrhtChttp://ecmdb.ca/proteins/P0AG38.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.xmlOuter membrane protein FP02931OMPF_ECOLIompFhttp://ecmdb.ca/proteins/P02931.xmlOuter membrane protein CP06996OMPC_ECOLIompChttp://ecmdb.ca/proteins/P06996.xmlL-Threonine <> Acetaldehyde + GlycineR00751THREONINE-ALDOLASE-RXNL-Threonine > 2-Ketobutyric acid + AmmoniumAdenosine triphosphate + Water + L-Threonine > ADP + Hydrogen ion + Phosphate + L-ThreonineAdenosine triphosphate + Water + L-Threonine > ADP + Hydrogen ion + Phosphate + L-ThreonineWater + O-Phosphohomoserine <> Phosphate + L-ThreonineR01466THRESYN-RXNAdenosine triphosphate + L-Threonine + tRNA(Thr) + tRNA(Thr) <> Adenosine monophosphate + Pyrophosphate + L-Threonyl-tRNA(Thr) + L-Threonyl-tRNA(Thr)R03663NAD + L-Threonine <> L-2-Amino-3-oxobutanoic acid + Hydrogen ion + NADHR01465THREODEHYD-RXNWater + L-Threonine O-3-phosphate > Phosphate + L-ThreonineL-Threonine <> 2-Ketobutyric acid + AmmoniaR00996Adenosine triphosphate + L-Threonine + tRNA(Thr) <> Adenosine monophosphate + Pyrophosphate + L-Threonyl-tRNA(Thr)R03663ala-thr + Water > L-Alanine + L-ThreonineRXN0-6980L-Threonine > Hydrogen ion + 2-Ketobutyric acid + AmmoniaR00996THREDEHYD-RXNL-Threonine + NAD > Hydrogen ion + L-2-Amino-3-oxobutanoic acid + NADHTHREODEHYD-RXNL-Threonine > Acetaldehyde + GlycineTHREONINE-ALDOLASE-RXNO-Phosphohomoserine + Water > Phosphate + L-ThreonineR01466THRESYN-RXNL-Threonine > 2-Ketobutyric acid + AmmoniaR00996THREDEHYD-RXNAdenosine triphosphate + L-Threonine + tRNA(Thr) > Adenosine monophosphate + Pyrophosphate + L-threonyl-tRNA(Thr)L-Threonine + NAD > L-2-Amino-3-oxobutanoic acid + NADHO-Phosphohomoserine + Water > L-Threonine + Inorganic phosphateL-Threonine + 2-Aminobut-2-enoate + 2-Iminobutanoate + Water <> 2-Ketobutyric acid + AmmoniaR00996 L-Threonine + Adenosine triphosphate + Hydrogen carbonate <> L-Threonylcarbamoyladenylate + Pyrophosphate + WaterR10463 L-Threonine + Adenosine triphosphate + Hydrogen ion + tRNA(Thr) + L-Threonine > Pyrophosphate + Adenosine monophosphate + L-Threonyl-tRNA(Thr)PW_R002829O-Phosphohomoserine + Water > Phosphate + L-Threonine + L-ThreoninePW_R002921L-Threonine + L-Threonine > Hydrogen ion + Water + (2Z)-2-aminobut-2-enoatePW_R002922L-Threonine + NAD + L-Threonine > Hydrogen ion + NADH + L-2-Amino-3-oxobutanoic acidPW_R005168L-Threonine + Adenosine triphosphate + Hydrogen carbonate <> L-Threonylcarbamoyladenylate + Pyrophosphate + WaterL-Threonine <> Acetaldehyde + GlycineAdenosine triphosphate + L-Threonine + tRNA(Thr) <> Adenosine monophosphate + Pyrophosphate + L-Threonyl-tRNA(Thr)Water + O-Phosphohomoserine <> Phosphate + L-ThreonineGutnick 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 culture179.0uM0.037 oCK12 NCM3722Mid-Log Phase7160000Bennett, 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/h147.0uM0.037 oCBW25113Stationary Phase, glucose limited5880000Ishii, 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 flask125.67uMtrue1.2137 oCBL21 DE3Stationary phase cultures (overnight culture)5026674839Lin, 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