2.0 2012-05-31 10:22:12 -0600 2015-09-13 12:56:06 -0600 ECMDB00158 M2MDB000060 L-Tyrosine Tyrosine (Tyr, Y) or 4-hydroxyphenylalanine is a non-essential amino acid with a polar side group. Its codons are UAC and UAU. Aside from being a proteogenic amino acid, tyrosine has a special role by virtue of the phenol functionality. It occurs in proteins that are part of signal transduction processes. It functions as a receiver of phosphate groups that are transferred by way of protein kinases (so-called receptor tyrosine kinases). Phosphorylation of the hydroxyl group changes the activity of the target protein. (Wikipedia) L-Tyrosine is the enantiomer of tyrosine (the other being D-tyrosine) that is used in building proteins. (-)-a-Amino-p-hydroxyhydrocinnamate (-)-a-Amino-p-hydroxyhydrocinnamic acid (-)-alpha-Amino-p-hydroxyhydrocinnamate (-)-alpha-Amino-p-hydroxyhydrocinnamic acid (-)-α-amino-P-Hydroxyhydrocinnamate (-)-α-amino-P-Hydroxyhydrocinnamic acid (S)-(-)-Tyrosine (S)-2-Amino-3-(p-hydroxyphenyl)propionate (S)-2-Amino-3-(p-hydroxyphenyl)propionic acid (S)-3-(p-Hydroxyphenyl)alanine (S)-a-amino-4-hydroxy-Benzenepropanoate (S)-a-amino-4-hydroxy-Benzenepropanoic acid (S)-a-Amino-4-hydroxybenzenepropanoate (S)-a-Amino-4-hydroxybenzenepropanoic acid (S)-alpha-amino-4-hydroxy-Benzenepropanoate (S)-alpha-amino-4-hydroxy-Benzenepropanoic acid (S)-alpha-Amino-4-hydroxybenzenepropanoate (S)-alpha-Amino-4-hydroxybenzenepropanoic acid (S)-Tyrosine (S)-α-amino-4-Hydroxy-benzenepropanoate (S)-α-amino-4-Hydroxy-benzenepropanoic acid (S)-α-amino-4-Hydroxybenzenepropanoate (S)-α-amino-4-Hydroxybenzenepropanoic acid 2-Amino-3-(4-hydroxyphen yl)-2-amino-3-(4-hydroxyphenyl)-Propanoate 2-Amino-3-(4-hydroxyphen yl)-2-amino-3-(4-hydroxyphenyl)-Propanoic acid 3-(4-Hydroxyphenyl)-L-alanine 4-Hydroxy-L-Phenylalanine Benzenepropanoate Benzenepropanoic acid L-p-Tyrosine L-Tyrosine P-Tyrosine Tyr Tyrosine Y C9H11NO3 181.1885 181.073893223 (2S)-2-amino-3-(4-hydroxyphenyl)propanoic acid L-tyrosine 60-18-4 N[C@@H](CC1=CC=C(O)C=C1)C(O)=O InChI=1S/C9H11NO3/c10-8(9(12)13)5-6-1-3-7(11)4-2-6/h1-4,8,11H,5,10H2,(H,12,13)/t8-/m0/s1 OUYCCCASQSFEME-QMMMGPOBSA-N Solid Cytosol Extra-organism Periplasm logp -2.39 ALOGPS logs -1.37 ALOGPS solubility 7.67e+00 g/l ALOGPS melting_point 343 oC logp -1.5 ChemAxon pka_strongest_acidic 2 ChemAxon pka_strongest_basic 9.19 ChemAxon iupac (2S)-2-amino-3-(4-hydroxyphenyl)propanoic acid ChemAxon average_mass 181.1885 ChemAxon mono_mass 181.073893223 ChemAxon smiles N[C@@H](CC1=CC=C(O)C=C1)C(O)=O ChemAxon formula C9H11NO3 ChemAxon inchi InChI=1S/C9H11NO3/c10-8(9(12)13)5-6-1-3-7(11)4-2-6/h1-4,8,11H,5,10H2,(H,12,13)/t8-/m0/s1 ChemAxon inchikey OUYCCCASQSFEME-QMMMGPOBSA-N ChemAxon polar_surface_area 83.55 ChemAxon refractivity 47.1 ChemAxon polarizability 18.01 ChemAxon rotatable_bond_count 3 ChemAxon acceptor_count 4 ChemAxon donor_count 3 ChemAxon physiological_charge 0 ChemAxon formal_charge 0 ChemAxon Tyrosine metabolism ec00350 Phenylalanine metabolism The pathways of the metabolism of phenylalaline begins with the conversion of chorismate to prephenate through a P-protein (chorismate mutase:pheA). Prephenate then interacts with a hydrogen ion through the same previous enzyme resulting in a release of carbon dioxide, water and a phenolpyruvic acid. Three enzymes those enconde by tyrB, aspC and ilvE are involved in catalyzing the third step of these pathways, all three can contribute to the synthesis of phenylalanine: only tyrB and aspC contribute to biosynthesis of tyrosine. Phenolpyruvic acid can also be obtained from a reversivle reaction with ammonia, a reduced acceptor and a D-amino acid dehydrogenase, resulting in a water, an acceptor and a D-phenylalanine, which can be then transported into the periplasmic space by aromatic amino acid exporter. L-phenylalanine also interacts in two reversible reactions, one involved with oxygen through a catalase peroxidase resulting in a carbon dioxide and 2-phenylacetamide. The other reaction involved an interaction with oxygen through a phenylalanine aminotransferase resulting in a oxoglutaric acid and phenylpyruvic acid. L-phenylalanine can be imported into the cytoplasm through an aromatic amino acid:H+ symporter AroP. The compound can also be imported into the periplasmic space through a transporter: L-amino acid efflux transporter. PW000921 ec00360 Metabolic Phenylalanine, tyrosine and tryptophan biosynthesis ec00400 Novobiocin biosynthesis ec00401 Cyanoamino acid metabolism ec00460 Aminoacyl-tRNA biosynthesis ec00970 Thiamine metabolism ec00730 Ubiquinone and other terpenoid-quinone biosynthesis ec00130 Metabolic pathways eco01100 inner membrane transport list 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 added PW000786 Metabolic tRNA Charging 2 This pathway groups together all E. coli tRNA charging reactions. PW000803 Metabolic tRNA charging This pathway groups together all E. coli tRNA charging reactions. PW000799 Metabolic tyrosine biosynthesis The pathways of biosynthesis of phenylalaline and tyrosine are intimately connected. First step of both pathways is the conversion of chorismate to prephenate, the third step of both is the conversion of a ketoacid to the aminoacid through transamination. The two pathways differ only in the second step of their three-step reaction sequences: In the case of phenylalanine biosynthesi a dehydratase converts prephenate to phenylpyruvate(reaction occurs slowly in the absence of enzymic activity); in the case of tyrosine biosynthesis, a dehydrogenase converts prephenate to p-hydroxyphenylpyruvate. Also in both pathways the first two steps are catalyzed by two distinc active sites on a single protein. Thus the first step of each pathway can be catalyzed by two enzyme: those associated with both the phenylalanine specific dehydratase and the tyrosine specific dehydrogenase. Three enzymes those enconde by tyrB, aspC and ilvE are involved in catalyzing the third step of these pathways, all three can contribute to the synthesis of phenylalanine: only tyrB and aspC contribute to biosynthesis of tyrosine PW000806 Metabolic Thiazole Biosynthesis I This pathway describes only the synthesis of the thiazole moiety of thiamin. Different variations of this pathway exist, this particular pathway describes the pathway that occurs in Escherichia coli K-12 and Salmonella enterica enterica serovar Typhimurium. The biosynthesis of the thiazole moiety is complex. In Escherichia coli it involves six proteins, the products of the thiS, thiF, thiG, thiH, thiI, and iscS genes. The process begins when IscS, a protein that is also involved in the biosynthesis of iron-sulfur clusters, catalyzes the transfer of a sulfur atom from cysteine to a ThiI sulfur-carrier protein, generating a an S-sulfanyl-[ThiI sulfur-carrier protein]. In a parallel route, the ThiF protein activates a ThiS sulfur-carrier protein by adenylation of its carboxy terminus, generating a carboxy-adenylated-[ThiS sulfur-carrier protein]. In a second reaction, which may also be catalyzed by ThiF, the sulfur from an S-sulfanyl-[ThiI sulfur-carrier protein] is transferred to ThiS, generating a thiocarboxy-[ThiS-Protein]. The final reaction of this pathway, which is catalyzed by the ThiG protein, requires three inputs: a thiocarboxy-[ThiS-Protein], 1-deoxy-D-xylulose 5-phosphate and 2-iminoacetate. 2-iminoacetate is formed in Escherichia coli from L-tyrosine by tyrosine lyase (ThiH), which forms a complex with ThiG. For many years the products of this reaction was assumed to be 4-methyl-5-(β-hydroxyethyl)thiazole (thiazole). However, recent work performed with the thiazole synthase from Bacillus subtilis has shown that the actual product is the thiazole tautomer 2-[(2R,5Z)-(2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate. While in Bacillus a dedicated thiazole tautomerase converts this product into a different tautomer (2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate), most of the proteobacteria lack the tautomerase. (EcoCyc) PW002041 Metabolic thiazole biosynthesis I (E. coli) PWY-6892 tRNA charging TRNA-CHARGING-PWY tyrosine biosynthesis I TYRSYN Specdb::CMs 383 Specdb::CMs 384 Specdb::CMs 385 Specdb::CMs 386 Specdb::CMs 387 Specdb::CMs 388 Specdb::CMs 1602 Specdb::CMs 1669 Specdb::CMs 2619 Specdb::CMs 30212 Specdb::CMs 30317 Specdb::CMs 30318 Specdb::CMs 30319 Specdb::CMs 30614 Specdb::CMs 30740 Specdb::CMs 30773 Specdb::CMs 31030 Specdb::CMs 31031 Specdb::CMs 37328 Specdb::CMs 173009 Specdb::CMs 1051730 Specdb::CMs 1051732 Specdb::CMs 1051734 Specdb::CMs 1051736 Specdb::CMs 1051738 Specdb::EiMs 1974 Specdb::NmrOneD 1117 Specdb::NmrOneD 1175 Specdb::NmrOneD 4862 Specdb::NmrOneD 4863 Specdb::NmrOneD 4864 Specdb::NmrOneD 4865 Specdb::NmrOneD 5912 Specdb::NmrOneD 5913 Specdb::NmrOneD 5914 Specdb::NmrOneD 5915 Specdb::NmrOneD 5916 Specdb::NmrOneD 5917 Specdb::NmrOneD 5918 Specdb::NmrOneD 5919 Specdb::NmrOneD 5920 Specdb::NmrOneD 5921 Specdb::NmrOneD 5922 Specdb::NmrOneD 5923 Specdb::NmrOneD 5924 Specdb::NmrOneD 5925 Specdb::NmrOneD 5926 Specdb::NmrOneD 5927 Specdb::NmrOneD 5928 Specdb::NmrOneD 5929 Specdb::NmrOneD 5930 Specdb::MsMs 245 Specdb::MsMs 246 Specdb::MsMs 247 Specdb::MsMs 3155 Specdb::MsMs 3156 Specdb::MsMs 3157 Specdb::MsMs 3158 Specdb::MsMs 3159 Specdb::MsMs 3160 Specdb::MsMs 3161 Specdb::MsMs 3162 Specdb::MsMs 3163 Specdb::MsMs 3164 Specdb::MsMs 3165 Specdb::MsMs 3166 Specdb::MsMs 3167 Specdb::MsMs 3168 Specdb::MsMs 3169 Specdb::MsMs 3170 Specdb::MsMs 3171 Specdb::MsMs 3172 Specdb::MsMs 3173 Specdb::MsMs 3174 Specdb::MsMs 3175 Specdb::MsMs 3176 Specdb::NmrTwoD 974 Specdb::NmrTwoD 1176 HMDB00158 6057 5833 C00082 17895 TYR TYR_LFZW_DHH Tyrosine Keseler, I. 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Microbiological synthesis of L-tyrosine and 3,4-dihydroxyphenyl-L-alanine. I. Distribution of tyrosine phenol lyase in microorganisms. Agricultural and Biological Chemist http://hmdb.ca/system/metabolites/msds/000/000/109/original/HMDB00158.pdf?1358894696 Aspartate aminotransferase P00509 AAT_ECOLI aspC http://ecmdb.ca/proteins/P00509.xml Aromatic-amino-acid aminotransferase P04693 TYRB_ECOLI tyrB http://ecmdb.ca/proteins/P04693.xml Histidinol-phosphate aminotransferase P06986 HIS8_ECOLI hisC http://ecmdb.ca/proteins/P06986.xml Periplasmic AppA protein P07102 PPA_ECOLI appA http://ecmdb.ca/proteins/P07102.xml Class B acid phosphatase P0AE22 APHA_ECOLI aphA http://ecmdb.ca/proteins/P0AE22.xml Tyrosyl-tRNA synthetase P0AGJ9 SYY_ECOLI tyrS http://ecmdb.ca/proteins/P0AGJ9.xml Thiazole synthase P30139 THIG_ECOLI thiG http://ecmdb.ca/proteins/P30139.xml Dehydroglycine synthase P30140 THIH_ECOLI thiH http://ecmdb.ca/proteins/P30140.xml Uncharacterized amino-acid ABC transporter ATP-binding protein yecC P37774 YECC_ECOLI yecC http://ecmdb.ca/proteins/P37774.xml Inner membrane amino-acid ABC transporter permease protein yecS P0AFT2 YECS_ECOLI yecS http://ecmdb.ca/proteins/P0AFT2.xml Tyrosine-specific transport protein P0AAD4 TYRP_ECOLI tyrP http://ecmdb.ca/proteins/P0AAD4.xml Aromatic amino acid transport protein AroP P15993 AROP_ECOLI aroP http://ecmdb.ca/proteins/P15993.xml Phenylalanine-specific permease P24207 PHEP_ECOLI pheP http://ecmdb.ca/proteins/P24207.xml Outer membrane protein N P77747 OMPN_ECOLI ompN http://ecmdb.ca/proteins/P77747.xml Inner membrane protein yddG P46136 YDDG_ECOLI yddG http://ecmdb.ca/proteins/P46136.xml Outer membrane pore protein E P02932 PHOE_ECOLI phoE http://ecmdb.ca/proteins/P02932.xml Outer membrane protein F P02931 OMPF_ECOLI ompF http://ecmdb.ca/proteins/P02931.xml Outer membrane protein C P06996 OMPC_ECOLI ompC http://ecmdb.ca/proteins/P06996.xml alpha-Ketoglutarate + L-Tyrosine <> 4-Hydroxyphenylpyruvic acid + L-Glutamate R00734 Adenosine triphosphate + tRNA(Tyr) + L-Tyrosine + tRNA(Tyr) <> Adenosine monophosphate + Pyrophosphate + L-Tyrosyl-tRNA(Tyr) + L-Tyrosyl-tRNA(Tyr) R02918 S-Adenosylmethionine + NADPH + L-Tyrosine > p-Cresol + 5'-Deoxyadenosine + Dehydroglycine + Hydrogen ion + L-Methionine + NADP Water + Phosphotyrosine > Phosphate + L-Tyrosine Adenosine triphosphate + L-Tyrosine + tRNA(Tyr) <> Adenosine monophosphate + Pyrophosphate + L-Tyrosyl-tRNA(Tyr) R02918 C15815 + L-Tyrosine + Iminoglycine <> 4-Methyl-5-(2-phosphoethyl)-thiazole R07465 L-Tyrosine + S-Adenosylmethionine + a reduced electron acceptor > Dehydroglycine + p-Cresol + 5'-Deoxyadenosine + L-Methionine + an oxidized electron acceptor + Hydrogen ion RXN-11319 L-Tyrosine + Oxoglutaric acid <> 4-Hydroxyphenylpyruvic acid + L-Glutamate TYRAMINOTRANS-RXN Adenosine triphosphate + L-Tyrosine + tRNA(Tyr) > Adenosine monophosphate + Pyrophosphate + L-tyrosyl-tRNA(Tyr) L-Tyrosine + S-adenosyl-L-methionine + reduced acceptor > 2-iminoacetate + p-Cresol + 5'-Deoxyadenosine + L-Methionine + acceptor +2 Hydrogen ion L-Tyrosine + S-Adenosylmethionine + NADPH <> 2-iminoacetate + p-Cresol + 5'-Deoxyadenosine + L-Methionine + NADP + Hydrogen ion R10246 L-Tyrosine + Adenosine triphosphate + Hydrogen ion + tRNA(Tyr) + L-Tyrosine > Adenosine monophosphate + Pyrophosphate + L-tyrosyl-tRNA(Tyr) PW_R002835 4-hydroxyphenylpyruvate + L-Glutamic acid + L-Glutamate > Oxoglutaric acid + L-Tyrosine + L-Tyrosine PW_R002858 L-Tyrosine + NADPH + S-adenosyl-L-methionine + L-Tyrosine + NADPH > Hydrogen ion + NADP + L-Methionine + 5'-Deoxyadenosine + p-Cresol + 2-iminoacetate PW_R005174 L-Tyrosine + S-adenosyl-L-methionine + NADPH > Dehydroglycine + 4-Methylcatechol + 5'-Deoxyadenosine + L-Methionine + NADP + Hydrogen ion PW_R005962 C15815 + L-Tyrosine + 2-iminoacetate <>4 4-Methyl-5-(2-phosphoethyl)-thiazole Adenosine triphosphate + tRNA(Tyr) + L-Tyrosine <> Adenosine monophosphate + Pyrophosphate + L-Tyrosyl-tRNA(Tyr) C15815 + L-Tyrosine + 2-iminoacetate <>4 4-Methyl-5-(2-phosphoethyl)-thiazole Adenosine triphosphate + tRNA(Tyr) + L-Tyrosine <> Adenosine monophosphate + Pyrophosphate + L-Tyrosyl-tRNA(Tyr) 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 glucose Shake flask and filter culture 28.9 uM 0.0 37 oC K12 NCM3722 Mid-Log Phase 115600 0 Bennett, 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. 19561621 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 glycerol Shake flask and filter culture 87.4 uM 0.0 37 oC K12 NCM3722 Mid-Log Phase 349600 0 Bennett, 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. 19561621 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 acetate Shake flask and filter culture 52.2 uM 0.0 37 oC K12 NCM3722 Mid-Log Phase 208800 0 Bennett, 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. 19561621 48 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 Gluco Bioreactor, pH controlled, O2 and CO2 controlled, dilution rate: 0.2/h 37.8 uM 0.0 37 oC BW25113 Stationary Phase, glucose limited 151200 0 Ishii, 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. 17379776 Luria-Bertani (LB) media Shake flask 76.8 uM true 6.24 37 oC BL21 DE3 Stationary phase cultures (overnight culture) 307200 24954 Lin, 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