Canmetcon
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Identification
YMDB IDYMDB00364
NameL-Tyrosine
SpeciesSaccharomyces cerevisiae
StrainBaker's yeast
DescriptionTyrosine (abbreviated as Tyr or Y) is an alpha-amino acid. The L-isomer is one of the 22 proteinogenic amino acids, i.e., the building blocks of proteins. It is classified as a nonpolar, aromatic amino acid, because of the hydrophobic nature of the phenol side chain. L-Tyrosine is an electrically neutral amino acid. The word 'tyrosine' is from the Greek tyri, meaning cheese, as it was first discovered in 1846 by German chemist Justus von Liebig in the protein casein from cheese. 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. Tyrosine is produced via prephenate, an intermediate on the shikimate pathway. Prephenate is oxidatively decarboxylated with retention of the hydroxyl group to give p-hydroxyphenylpyruvate, which is transaminated using glutamate as the nitrogen source to give tyrosine and alpha-ketoglutarate. In yeast, the biosynthesis of phenylalanine, tyrosine, and tryptophan proceeds via a common pathway to chorismate, at which point the pathway branches. One branch proceeds to phenylalanine and tyrosine, and the other to tryptophan. The phenylalanine and tyrosine branch has one reaction in common, rearrangement of chorismate to prephenate, at which point, the pathway branches again to either phenylalanine or tyrosine. S. cerevisiae, similar to E. coli, synthesizes phenylalanine and tyrosine via the intermediate 4-hydroxyphenylpyruvate and phenylpyruvate, respectively. Aromatic amino acid biosynthesis in S. cerevisiae is controlled by a combination of feedback inhibition, activation of enzyme activity, and regulation of enzyme synthesis. The carbon flow through the pathways is regulated primarily at the initial step and the branching points by the terminal end-products. The initial step of chorismate biosynthesis can be catalyzed by two isoenzymes Aro3p or Aro4p, whereby Aro3p is inhibited by phenylalanine, and Aro4p by tyrosine. The first step in the phenylalanine-tyrosine branch is feedback inhibited by tyrosine and activated by tryptophan. S. cerevisiae degrade the aromatic amino acids (tryptophan, phenylalanine, and tyrosine) via the Ehrlich pathway. This pathway consists of 3 steps: 1) deamination of the amino acid to the corresponding alpha-keto acid; 2) decarboxylation of the resulting alpha-keto acid to the respective aldehyde; and, 3) reduction of the aldehyde to form the corresponding long chain or complex alcohol, known as a fusel alcohol or fusel oil. Fusel alcohols are important flavor and aroma compounds in yeast-fermented food products and beverages. Aro10p appears to be the primary decarboxylase catalyzing the second step in phenylalanine degradation. Although Vulrahan et. al. (2003) found that THI3 does not encode an active phenylpyruvate decarboxylase, they found Thi3p was required in conjunction with one of the pyruvate decarboxylases Pdc1p, Pdc5p or Pdc6p for the ARO10-independent decarboxylase activity. The main uptake systems for utilizing aromatic amino acids appear to be Gap1p, a general amino acid permease, and Wap1p, an inducible amino acid permease with wide substrate specificity.
Structure
Thumb
Synonyms
  • (-)-a-Amino-p-hydroxyhydrocinnamate
  • (-)-a-Amino-p-hydroxyhydrocinnamic acid
  • (-)-alpha-Amino-p-hydroxyhydrocinnamate
  • (-)-alpha-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
  • 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
  • (2S)-2-Amino-3-(4-hydroxyphenyl)propanoic acid
  • L-Tyrosin
  • Y
  • (-)-Α-amino-p-hydroxyhydrocinnamate
  • (-)-Α-amino-p-hydroxyhydrocinnamic acid
  • (2S)-2-Amino-3-(4-hydroxyphenyl)propanoate
  • (S)-Α-amino-4-hydroxybenzenepropanoate
  • (S)-Α-amino-4-hydroxybenzenepropanoic acid
  • L Tyrosine
  • Tyrosine, L-isomer
  • Tyrosine, L isomer
  • Para tyrosine
  • Para-tyrosine
CAS number60-18-4
WeightAverage: 181.1885
Monoisotopic: 181.073893223
InChI KeyOUYCCCASQSFEME-QMMMGPOBSA-N
InChIInChI=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
IUPAC Name(2S)-2-amino-3-(4-hydroxyphenyl)propanoic acid
Traditional IUPAC NameL-tyrosine
Chemical FormulaC9H11NO3
SMILES[H]OC(=O)[C@@]([H])(N([H])[H])C([H])([H])C1=C([H])C([H])=C(O[H])C([H])=C1[H]
Chemical Taxonomy
Description belongs to the class of organic compounds known as tyrosine and derivatives. Tyrosine and derivatives are compounds containing tyrosine or a derivative thereof resulting from reaction of tyrosine at the amino group or the carboxy group, or from the replacement of any hydrogen of glycine by a heteroatom.
KingdomOrganic compounds
Super ClassOrganic acids and derivatives
ClassCarboxylic acids and derivatives
Sub ClassAmino acids, peptides, and analogues
Direct ParentTyrosine and derivatives
Alternative Parents
Substituents
  • Tyrosine or derivatives
  • Phenylalanine or derivatives
  • 3-phenylpropanoic-acid
  • Alpha-amino acid
  • Amphetamine or derivatives
  • L-alpha-amino acid
  • 1-hydroxy-2-unsubstituted benzenoid
  • Phenol
  • Aralkylamine
  • Monocyclic benzene moiety
  • Benzenoid
  • Amino acid
  • Carboxylic acid
  • Monocarboxylic acid or derivatives
  • Organic oxide
  • Organooxygen compound
  • Organonitrogen compound
  • Amine
  • Primary aliphatic amine
  • Organic nitrogen compound
  • Carbonyl group
  • Organopnictogen compound
  • Organic oxygen compound
  • Hydrocarbon derivative
  • Primary amine
  • Aromatic homomonocyclic compound
Molecular FrameworkAromatic homomonocyclic compounds
External Descriptors
Physical Properties
StateSolid
Charge0
Melting point343 °C
Experimental Properties
PropertyValueReference
Water Solubility0.479 mg/mL at 25 oC [SEIDELL,A (1941)]PhysProp
LogP-2.26 [HANSCH,C ET AL. (1995)]PhysProp
Predicted Properties
PropertyValueSource
Water Solubility7.67 g/LALOGPS
logP-2.4ALOGPS
logP-1.5ChemAxon
logS-1.4ALOGPS
pKa (Strongest Acidic)2ChemAxon
pKa (Strongest Basic)9.19ChemAxon
Physiological Charge0ChemAxon
Hydrogen Acceptor Count4ChemAxon
Hydrogen Donor Count3ChemAxon
Polar Surface Area83.55 ŲChemAxon
Rotatable Bond Count3ChemAxon
Refractivity47.1 m³·mol⁻¹ChemAxon
Polarizability18.01 ųChemAxon
Number of Rings1ChemAxon
Bioavailability1ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Biological Properties
Cellular Locations
  • extracellular
  • mitochondrion
  • peroxisome
  • vacuole
  • cytoplasm
Organoleptic Properties
Flavour/OdourSource
OdorlessFDB000446
SMPDB Pathways
Phenylalanine metabolismPW002437 ThumbThumb?image type=greyscaleThumb?image type=simple
Tyrosine metabolismPW002441 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Cyanoamino acid metabolismec00460 Map00460
Phenylalanine metabolismec00360 Map00360
Phenylalanine, tyrosine and tryptophan biosynthesisec00400 Map00400
Thiamine metabolismec00730 Map00730
Tyrosine metabolismec00350 Map00350
SMPDB Reactions
(4-hydroxyphenyl)pyruvic acid + L-AlaninePyruvic acid + L-Tyrosine
(4-hydroxyphenyl)pyruvic acid + L-Glutamic acidOxoglutaric acid + L-Tyrosine
KEGG Reactions
L-Tyrosine + N10-Formyl-THFN-Formyl-L-tyrosine + 5,6,7,8-Tetrahydrofolic acid + hydron
L-Glutamic acid + (4-hydroxyphenyl)pyruvic acidL-Tyrosine + Oxoglutaric acid
L-Tyrosine + Adenosine triphosphate + tRNA(Tyr) → Adenosine monophosphate + Pyrophosphate + Tyr-tRNA(Tyr)
Concentrations
Intracellular Concentrations
Intracellular ConcentrationSubstrateGrowth ConditionsStrainCitation
283 ± 6 µM YPD mediaaerobicBaker's yeastPMID: 7654310
170 ± 3 µM YPG mediaaerobicBaker's yeastPMID: 7654310
340 ± 7 µM SD mediaaerobicBaker's yeastPMID: 7654310
453 ± 9 µM SG mediaaerobicBaker's yeastPMID: 7654310
1019 ± 21 µM M (molasses)aerobicBaker's yeastPMID: 7654310
4019 ± 80 µM MA (molasses)aerobicBaker's yeastPMID: 7654310
283 ± 6 µM MB (molasses)aerobicBaker's yeastPMID: 7654310
2604 ± 52 µM MAB (molasses)aerobicBaker's yeastPMID: 7654310
883 ± 44 µM YEB media with 0.5 mM glucoseaerobicBaker's yeastExperimentally Determined
Not Available
250 ± 33 µM Synthetic medium with 20 g/L glucoseaerobicBaker's yeastPMID: 12584756
Conversion Details Here
Extracellular Concentrations
Intracellular ConcentrationSubstrateGrowth ConditionsStrainCitation
1297 ± 143 µM hops, malted barleyanaerobicBaker's yeastPMID: 16448171
Conversion Details Here
Spectra
Spectra
References
References:
  • Martinez-Force, E., Benitez, T. (1995). "Effects of varying media, temperature, and growth rates on the intracellular concentrations of yeast amino acids." Biotechnol Prog 11:386-392.7654310
  • UniProt Consortium (2011). "Ongoing and future developments at the Universal Protein Resource." Nucleic Acids Res 39:D214-D219.21051339
  • Scheer, M., Grote, A., Chang, A., Schomburg, I., Munaretto, C., Rother, M., Sohngen, C., Stelzer, M., Thiele, J., Schomburg, D. (2011). "BRENDA, the enzyme information system in 2011." Nucleic Acids Res 39:D670-D676.21062828
  • Herrgard, M. J., Swainston, N., Dobson, P., Dunn, W. B., Arga, K. Y., Arvas, M., Bluthgen, N., Borger, S., Costenoble, R., Heinemann, M., Hucka, M., Le Novere, N., Li, P., Liebermeister, W., Mo, M. L., Oliveira, A. P., Petranovic, D., Pettifer, S., Simeonidis, E., Smallbone, K., Spasic, I., Weichart, D., Brent, R., Broomhead, D. S., Westerhoff, H. V., Kirdar, B., Penttila, M., Klipp, E., Palsson, B. O., Sauer, U., Oliver, S. G., Mendes, P., Nielsen, J., Kell, D. B. (2008). "A consensus yeast metabolic network reconstruction obtained from a community approach to systems biology." Nat Biotechnol 26:1155-1160.18846089
  • Vaseghi, S., Baumeister, A., Rizzi, M., Reuss, M. (1999). "In vivo dynamics of the pentose phosphate pathway in Saccharomyces cerevisiae." Metab Eng 1:128-140.10935926
  • Almeida, C., Duarte, I. F., Barros, A., Rodrigues, J., Spraul, M., Gil, A. M. (2006). "Composition of beer by 1H NMR spectroscopy: effects of brewing site and date of production." J Agric Food Chem 54:700-706.16448171
  • Hans, M. A., Heinzle, E., Wittmann, C. (2003). "Free intracellular amino acid pools during autonomous oscillations in Saccharomyces cerevisiae." Biotechnol Bioeng 82:143-151.12584756
  • Nookaew, I., Jewett, M. C., Meechai, A., Thammarongtham, C., Laoteng, K., Cheevadhanarak, S., Nielsen, J., Bhumiratana, S. (2008). "The genome-scale metabolic model iIN800 of Saccharomyces cerevisiae and its validation: a scaffold to query lipid metabolism." BMC Syst Biol 2:71.18687109
  • Yang, Z., Huang, J., Geng, J., Nair, U., Klionsky, D. J. (2006). "Atg22 recycles amino acids to link the degradative and recycling functions of autophagy." Mol Biol Cell 17:5094-5104.17021250
  • Shimazu, M., Sekito, T., Akiyama, K., Ohsumi, Y., Kakinuma, Y. (2005). "A family of basic amino acid transporters of the vacuolar membrane from Saccharomyces cerevisiae." J Biol Chem 280:4851-4857.15572352
  • Briza, P., Kalchhauser, H., Pittenauer, E., Allmaier, G., Breitenbach, M. (1996). "N,N'-Bisformyl dityrosine is an in vivo precursor of the yeast ascospore wall." Eur J Biochem 239:124-131.8706696
  • Iraqui, I., Vissers, S., Cartiaux, M., Urrestarazu, A. (1998). "Characterisation of Saccharomyces cerevisiae ARO8 and ARO9 genes encoding aromatic aminotransferases I and II reveals a new aminotransferase subfamily." Mol Gen Genet 257:238-248.9491083
  • Castrillo, J. I., Zeef, L. A., Hoyle, D. C., Zhang, N., Hayes, A., Gardner, D. C., Cornell, M. J., Petty, J., Hakes, L., Wardleworth, L., Rash, B., Brown, M., Dunn, W. B., Broadhurst, D., O'Donoghue, K., Hester, S. S., Dunkley, T. P., Hart, S. R., Swainston, N., Li, P., Gaskell, S. J., Paton, N. W., Lilley, K. S., Kell, D. B., Oliver, S. G. (2007). "Growth control of the eukaryote cell: a systems biology study in yeast." J Biol 6:4.17439666
Synthesis Reference:Enei, Hitoshi; Matsui, Hiroshi; Yamashita, Koichi; Okumura, Shinji; Yamada, Hideaki. Microbiological synthesis of L-tyrosine and 3,4-dihydroxyphenyl-L-alanine. I. Distribution of tyrosine phenol lyase in microorganisms. Agricultural and Biological Chemist
External Links:
ResourceLink
CHEBI ID17895
HMDB IDHMDB00158
Pubchem Compound ID6057
Kegg IDC00082
ChemSpider ID5833
FOODB IDFDB000446
WikipediaTyrosine
BioCyc IDTYR

Enzymes

General function:
Involved in nucleotide binding
Specific function:
Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction:tyrosine is first activated by ATP to form Tyr- AMP and then transferred to the acceptor end of tRNA(Tyr)
Gene Name:
MSY1
Uniprot ID:
P48527
Molecular weight:
55286.89844
Reactions
ATP + L-tyrosine + tRNA(Tyr) → AMP + diphosphate + L-tyrosyl-tRNA(Tyr).
General function:
Involved in nucleotide binding
Specific function:
Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction:tyrosine is first activated by ATP to form Tyr- AMP and then transferred to the acceptor end of tRNA(Tyr). The specificity determinants on tRNA(Tyr) are the base pair C1-G72, the discriminator residue A73, and the three anticodon bases G34, U35 and A36. Also involved in nuclear tRNA export
Gene Name:
TYS1
Uniprot ID:
P36421
Molecular weight:
44019.60156
Reactions
ATP + L-tyrosine + tRNA(Tyr) → AMP + diphosphate + L-tyrosyl-tRNA(Tyr).
General function:
Involved in transferase activity, transferring nitrogenous groups
Specific function:
Has aromatic amino acid transaminase activity and kynurenine aminotransferase activity
Gene Name:
ARO9
Uniprot ID:
P38840
Molecular weight:
58527.0
Reactions
An aromatic amino acid + 2-oxoglutarate → an aromatic oxo acid + L-glutamate.
General function:
Involved in transferase activity, transferring nitrogenous groups
Specific function:
Has aromatic amino acid transaminase activity. Also active with methionine, alpha-aminoadipate and leucine when phenylpyruvate is the amino acceptor
Gene Name:
ARO8
Uniprot ID:
P53090
Molecular weight:
56177.30078
Reactions
An aromatic amino acid + 2-oxoglutarate → an aromatic oxo acid + L-glutamate.
L-2-aminoadipate + 2-oxoglutarate → 2-oxoadipate + L-glutamate
General function:
Involved in transferase activity, transferring nitrogenous groups
Specific function:
Plays a key role in amino acid metabolism. Important for metabolite exchange between mitochondria and cytosol
Gene Name:
AAT1
Uniprot ID:
Q01802
Molecular weight:
51795.10156
Reactions
L-aspartate + 2-oxoglutarate → oxaloacetate + L-glutamate.
General function:
Involved in transferase activity, transferring nitrogenous groups
Specific function:
Plays a key role in amino acid metabolism
Gene Name:
AAT2
Uniprot ID:
P23542
Molecular weight:
46057.30078
Reactions
L-aspartate + 2-oxoglutarate → oxaloacetate + L-glutamate.
General function:
Secondary metabolites biosynthesis, transport and catabolism
Specific function:
Involved in spore wall maturation. Catalyzes a two step reaction that leads to the LL-dityrosine containing precursor of the spore wall
Gene Name:
DIT1
Uniprot ID:
P21623
Molecular weight:
61390.10156
Reactions

Transporters

General function:
Amino acid transport and metabolism
Specific function:
Involved in amino acid efflux from the vacuole to the cytoplasm. Capable of transporting large neutral amino acids including tyrosine, glutamine, asparagine, isoleucine and leucine
Gene Name:
AVT3
Uniprot ID:
P36062
Molecular weight:
75458.70313
General function:
Amino acid transport and metabolism
Specific function:
Required for the vacuolar uptake of large neutral amino acids including tyrosine, glutamine, asparagine, isoleucine and leucine. Requires ATP for function
Gene Name:
AVT1
Uniprot ID:
P47082
Molecular weight:
65345.30078
General function:
Involved in transport
Specific function:
Permease for various amino acids as well as for GABA. Can also transport L-cysteine and beta-alanine
Gene Name:
GAP1
Uniprot ID:
P19145
Molecular weight:
65654.89844
General function:
Amino acid transport and metabolism
Specific function:
Involved in amino acid efflux from the vacuole to the cytoplasm. Capable of transporting large neutral amino acids including tyrosine, glutamine, asparagine, isoleucine and leucine
Gene Name:
AVT4
Uniprot ID:
P50944
Molecular weight:
80025.0
General function:
Involved in transport
Specific function:
Required for high-affinity tryptophan transport. Also transports cysteine, phenyalanine and tyrosine
Gene Name:
TAT2
Uniprot ID:
P38967
Molecular weight:
65403.80078
General function:
Involved in transport
Specific function:
Permease for leucine, valine and isoleucine. Also transports cysteine, methionine, phenyalanine, tyrosine and tryptophan
Gene Name:
BAP2
Uniprot ID:
P38084
Molecular weight:
67669.60156
General function:
Involved in transport
Specific function:
High-affinity transport of valine and tyrosine. Low- affinity transport of tryptophan. Can also transport L-cysteine
Gene Name:
TAT1
Uniprot ID:
P38085
Molecular weight:
68756.89844
General function:
Involved in transport
Specific function:
Involved in transport of isoleucine, leucine, valine, cysteine, methionine, phenylalanine, tyrosine and tryptophan
Gene Name:
BAP3
Uniprot ID:
P41815
Molecular weight:
67364.39844
General function:
Involved in amino acid export from vacuole
Specific function:
Required for lysis of autophagic vesicles after delivery to the vacuole
Gene Name:
ATG22
Uniprot ID:
P25568
Molecular weight:
58843.10156
General function:
Involved in transport
Specific function:
Broad substrate range permease which transports asparagine and glutamine with intermediate specificity. Also transports Ala, Cys, Gly, Ile, Leu, Met, Phe, Ser, Thr, Tyr and Val. Important for the utilization of amino acids as a nitrogen source
Gene Name:
AGP1
Uniprot ID:
P25376
Molecular weight:
69670.70313
General function:
Involved in transmembrane transport
Specific function:
Transporter required for vacuolar uptake of histidine, arginine and lysine and to a lesser extent tyrosine
Gene Name:
VBA2
Uniprot ID:
P38358
Molecular weight:
51676.39844