L-tyrosine biosynthesis I

MetaCyc:TYRSYN

L-tyrosine biosynthesis I converts chorismate to prephenate, oxidatively decarboxylates prephenate with NAD+ to 3-(4-hydroxyphenyl)pyruvate, and transaminates 3-(4-hydroxyphenyl)pyruvate with L-glutamate to form L-tyrosine.

Pathway type
amino acid biosynthesis
Organism scope

Read the source YAML

Pathway network

19 nodes · 22 asserted directed edges

Arrows show recorded subject → object relationships, not necessarily metabolic flow. Select a node for details or an arrow for evidence. Scroll, zoom or find a node to explore.

Pathway network: L-tyrosine biosynthesis I 19 nodes · 22 asserted directed edges. Every arrow links to its evidence table row; nodes link to their component details. Isolated declared components are retained. CHEBI:29748 — consumes → RHEA:13898; Evidence: RHEA:13898consumes RHEA:13898 — produces → CHEBI:29934; Evidence: RHEA:13898produces CHEBI:29934 — consumes → RHEA:13870; Evidence: RHEA:13870consumes CHEBI:57540 — consumes → RHEA:13870; Evidence: RHEA:13870consumes RHEA:13870 — produces → CHEBI:16526; Evidence: RHEA:13870produces RHEA:13870 — produces → CHEBI:36242; Evidence: RHEA:13870produces RHEA:13870 — produces → CHEBI:57945; Evidence: RHEA:13870produces CHEBI:29985 — consumes → RHEA:15095; Evidence: RHEA:15095consumes CHEBI:36242 — consumes → RHEA:15095; Evidence: RHEA:15095consumes RHEA:15095 — produces → CHEBI:16810; Evidence: RHEA:15095produces RHEA:15095 — produces → CHEBI:58315; Evidence: RHEA:15095produces EC:5.4.99.5 — catalyzes → RHEA:13898; Evidence: RHEA:13897, PMID:12581215catalyzes EC:1.3.1.12 — catalyzes → RHEA:13870; Evidence: RHEA:13869, PMID:12581215catalyzes EC:2.6.1.57 — catalyzes → RHEA:15095; Evidence: RHEA:15093, PMID:236311catalyzes RHEA:13870 — precedes → RHEA:15095; Evidence: MetaCyc:TYRSYNprecedes RHEA:13898 — precedes → RHEA:13870; Evidence: MetaCyc:TYRSYNprecedes UniProtKB:P07023 — enables → RHEA:13898; Evidence: UniProtKB:P07023enables UniProtKB:P07023 — enables → RHEA:13870; Evidence: UniProtKB:P07023enables UniProtKB:P07023 — located_in → GO:0005737; Evidence: UniProtKB:P07023located in UniProtKB:P0A9J8 — enables → RHEA:13898; Evidence: UniProtKB:P0A9J8enables CHEBI:58095 — inhibits → UniProtKB:P0A9J8; Evidence: UniProtKB:P0A9J8inhibits UniProtKB:P0A9J8 — located_in → GO:0005737; Evidence: UniProtKB:P0A9J8located in chorismate mutase; EC:5.4.99.5; Declared type: molecular_activity molecular activity chorismate mutase prephenate dehydrogenase; EC:1.3.1.12; Declared type: molecular_activity molecular activity prephenate dehydrogenase aromatic-amino-acid transaminase; EC:2.6.1.57; Declared type: molecular_activity molecular activity aromatic-amino-acid transaminase chorismate; CHEBI:29748; Declared type: small_molecule small molecule chorismate prephenate; CHEBI:29934; Declared type: small_molecule small molecule prephenate NAD+; CHEBI:57540; Declared type: small_molecule small molecule NAD+ 3-(4-hydroxyphenyl)pyruvate; CHEBI:36242; Declared type: small_molecule small molecule 3-(4-hydroxyphenyl)pyruvate CO2; CHEBI:16526; Declared type: small_molecule small molecule CO2 NADH; CHEBI:57945; Declared type: small_molecule small molecule NADH L-glutamate; CHEBI:29985; Declared type: small_molecule small molecule L-glutamate L-tyrosine; CHEBI:58315; Declared type: small_molecule small molecule L-tyrosine 2-oxoglutarate; CHEBI:16810; Declared type: small_molecule small molecule 2-oxoglutarate T-protein; UniProtKB:P07023; Declared type: protein protein T-protein cytoplasm; GO:0005737; Declared type: cellular_component cellular component cytoplasm Bifunctional chorismate mutase/prephenate dehydratase; UniProtKB:P0A9J8; Declared type: protein protein Bifunctional chorismate mutase/prephenate dehydratase L-phenylalanine zwitterion; CHEBI:58095; Declared type: small_molecule small molecule L-phenylalanine zwitterion chorismate mutase reaction; RHEA:13898; Declared type: reaction/activity; Source reaction direction: left_to_right reaction / activity chorismate mutase reaction prephenate dehydrogenase reaction; RHEA:13870; Declared type: reaction/activity; Source reaction direction: left_to_right reaction / activity prephenate dehydrogenase reaction L-tyrosine aminotransferase reaction; RHEA:15095; Declared type: reaction/activity; Source reaction direction: right_to_left reaction / activity L-tyrosine aminotransferase reaction

Components and activities

Declared biological components and source reaction directions
NodeKind or roleSource direction
Escherichia coli
NCBITaxon:562
taxon
chorismate mutase
EC:5.4.99.5
molecular activity
prephenate dehydrogenase
EC:1.3.1.12
molecular activity
aromatic-amino-acid transaminase
EC:2.6.1.57
molecular activity
chorismate
CHEBI:29748
small molecule
prephenate
CHEBI:29934
small molecule
NAD+
CHEBI:57540
small molecule
3-(4-hydroxyphenyl)pyruvate
CHEBI:36242
small molecule
CO2
CHEBI:16526
small molecule
NADH
CHEBI:57945
small molecule
L-glutamate
CHEBI:29985
small molecule
L-tyrosine
CHEBI:58315
small molecule
2-oxoglutarate
CHEBI:16810
small molecule
T-protein
UniProtKB:P07023
protein
cytoplasm
GO:0005737
cellular component
Bifunctional chorismate mutase/prephenate dehydratase
UniProtKB:P0A9J8
protein
L-phenylalanine zwitterion
CHEBI:58095
small molecule
chorismate mutase reaction
RHEA:13898
reactionleft to right
prephenate dehydrogenase reaction
RHEA:13870
reactionleft to right
L-tyrosine aminotransferase reaction
RHEA:15095
reactionright to left

Mechanistic edges

Mechanistic edges and their cited evidence
SubjectPredicate and descriptionObjectEvidence
chorismate
CHEBI:29748
consumes

chorismate mutase reaction
RHEA:13898
  • RHEA:13898

    Source assertion: Rhea lists CHEBI:29748 on the substrates side of RHEA:13898 in this directed reaction.

    Source locationrdf:Description[@rdf:about='http://rdf.rhea-db.org/13898']/rh:substrates; rh:contains/rh:compound/rh:accession
chorismate mutase reaction
RHEA:13898
produces

prephenate
CHEBI:29934
  • RHEA:13898

    Source assertion: Rhea lists CHEBI:29934 on the products side of RHEA:13898 in this directed reaction.

    Source locationrdf:Description[@rdf:about='http://rdf.rhea-db.org/13898']/rh:products; rh:contains/rh:compound/rh:accession
prephenate
CHEBI:29934
consumes

prephenate dehydrogenase reaction
RHEA:13870
  • RHEA:13870

    Source assertion: Rhea lists CHEBI:29934 on the substrates side of RHEA:13870 in this directed reaction.

    Source locationrdf:Description[@rdf:about='http://rdf.rhea-db.org/13870']/rh:substrates; rh:contains/rh:compound/rh:accession
NAD+
CHEBI:57540
consumes

prephenate dehydrogenase reaction
RHEA:13870
  • RHEA:13870

    Source assertion: Rhea lists CHEBI:57540 on the substrates side of RHEA:13870 in this directed reaction.

    Source locationrdf:Description[@rdf:about='http://rdf.rhea-db.org/13870']/rh:substrates; rh:contains/rh:compound/rh:accession
prephenate dehydrogenase reaction
RHEA:13870
produces

CO2
CHEBI:16526
  • RHEA:13870

    Source assertion: Rhea lists CHEBI:16526 on the products side of RHEA:13870 in this directed reaction.

    Source locationrdf:Description[@rdf:about='http://rdf.rhea-db.org/13870']/rh:products; rh:contains/rh:compound/rh:accession
prephenate dehydrogenase reaction
RHEA:13870
produces

3-(4-hydroxyphenyl)pyruvate
CHEBI:36242
  • RHEA:13870

    Source assertion: Rhea lists CHEBI:36242 on the products side of RHEA:13870 in this directed reaction.

    Source locationrdf:Description[@rdf:about='http://rdf.rhea-db.org/13870']/rh:products; rh:contains/rh:compound/rh:accession
prephenate dehydrogenase reaction
RHEA:13870
produces

NADH
CHEBI:57945
  • RHEA:13870

    Source assertion: Rhea lists CHEBI:57945 on the products side of RHEA:13870 in this directed reaction.

    Source locationrdf:Description[@rdf:about='http://rdf.rhea-db.org/13870']/rh:products; rh:contains/rh:compound/rh:accession
L-glutamate
CHEBI:29985
consumes

L-tyrosine aminotransferase reaction
RHEA:15095
  • RHEA:15095

    Source assertion: Rhea lists CHEBI:29985 on the substrates side of RHEA:15095 in this directed reaction.

    Source locationrdf:Description[@rdf:about='http://rdf.rhea-db.org/15095']/rh:substrates; rh:contains/rh:compound/rh:accession
3-(4-hydroxyphenyl)pyruvate
CHEBI:36242
consumes

L-tyrosine aminotransferase reaction
RHEA:15095
  • RHEA:15095

    Source assertion: Rhea lists CHEBI:36242 on the substrates side of RHEA:15095 in this directed reaction.

    Source locationrdf:Description[@rdf:about='http://rdf.rhea-db.org/15095']/rh:substrates; rh:contains/rh:compound/rh:accession
L-tyrosine aminotransferase reaction
RHEA:15095
produces

2-oxoglutarate
CHEBI:16810
  • RHEA:15095

    Source assertion: Rhea lists CHEBI:16810 on the products side of RHEA:15095 in this directed reaction.

    Source locationrdf:Description[@rdf:about='http://rdf.rhea-db.org/15095']/rh:products; rh:contains/rh:compound/rh:accession
L-tyrosine aminotransferase reaction
RHEA:15095
produces

L-tyrosine
CHEBI:58315
  • RHEA:15095

    Source assertion: Rhea lists CHEBI:58315 on the products side of RHEA:15095 in this directed reaction.

    Source locationrdf:Description[@rdf:about='http://rdf.rhea-db.org/15095']/rh:products; rh:contains/rh:compound/rh:accession
chorismate mutase
EC:5.4.99.5
catalyzes

chorismate mutase reaction
RHEA:13898
  • RHEA:13897

    Source assertion: Rhea associates EC:5.4.99.5 with the reaction family containing RHEA:13898.

    Source locationrh:ec
  • PMID:12581215
    Mapping of chorismate mutase and prephenate dehydrogenase domains in the Escherichia coli T-protein.
    Source locationPubMed ArticleTitle
prephenate dehydrogenase
EC:1.3.1.12
catalyzes

prephenate dehydrogenase reaction
RHEA:13870
  • RHEA:13869

    Source assertion: Rhea associates EC:1.3.1.12 with the reaction family containing RHEA:13870.

    Source locationrh:ec
  • PMID:12581215
    Mapping of chorismate mutase and prephenate dehydrogenase domains in the Escherichia coli T-protein.
    Source locationPubMed ArticleTitle
aromatic-amino-acid transaminase
EC:2.6.1.57
catalyzes

L-tyrosine aminotransferase reaction
RHEA:15095
  • RHEA:15093

    Source assertion: Rhea associates EC:2.6.1.57 with the reaction family containing RHEA:15095.

    Source locationrh:ec
  • PMID:236311
    Multispecific aspartate and aromatic amino acid aminotransferases in Escherichia coli.
    Source locationPubMed ArticleTitle
prephenate dehydrogenase reaction
RHEA:13870
precedes

L-tyrosine aminotransferase reaction
RHEA:15095
  • MetaCyc:TYRSYN

    Source assertion: MetaCyc pathway ordering places RHEA:13870 before RHEA:15095 in this pathway. Shared intermediate: CHEBI:36242.

    Source locationPathway/reaction-ordering and reaction-layout; Rhea-to-MetaCyc cross-references
chorismate mutase reaction
RHEA:13898
precedes

prephenate dehydrogenase reaction
RHEA:13870
  • MetaCyc:TYRSYN

    Source assertion: MetaCyc pathway ordering places RHEA:13898 before RHEA:13870 in this pathway. Shared intermediate: CHEBI:29934.

    Source locationPathway/reaction-ordering and reaction-layout; Rhea-to-MetaCyc cross-references
T-protein
UniProtKB:P07023
enables

chorismate mutase reaction
RHEA:13898
  • UniProtKB:P07023

    Source assertion: UniProt annotates UniProtKB:P07023 with catalytic activity for the reaction family of RHEA:13898. Annotation evidence: curated source annotation; organism taxon: NCBITaxon:83333.

    Source locationcomments[commentType='CATALYTIC ACTIVITY'].reaction.reactionCrossReferences
T-protein
UniProtKB:P07023
enables

prephenate dehydrogenase reaction
RHEA:13870
  • UniProtKB:P07023

    Source assertion: UniProt annotates UniProtKB:P07023 with catalytic activity for the reaction family of RHEA:13870. Annotation evidence: curated source annotation; organism taxon: NCBITaxon:83333.

    Source locationcomments[commentType='CATALYTIC ACTIVITY'].reaction.reactionCrossReferences
T-protein
UniProtKB:P07023
located_in

cytoplasm
GO:0005737
  • UniProtKB:P07023

    Source assertion: UniProt locates UniProtKB:P07023 in Cytoplasm (SL-0086, mapped by UniProt to GO:0005737). Annotation evidence: curated source annotation.

    Source locationcomments[commentType='SUBCELLULAR LOCATION'].subcellularLocations; UniProt location vocabulary GO mapping
Bifunctional chorismate mutase/prephenate dehydratase
UniProtKB:P0A9J8
enables

chorismate mutase reaction
RHEA:13898
  • UniProtKB:P0A9J8

    Source assertion: UniProt annotates UniProtKB:P0A9J8 with catalytic activity for the reaction family of RHEA:13898. Annotation evidence: ECO:0000269; organism taxon: NCBITaxon:83333.

    Source locationcomments[commentType='CATALYTIC ACTIVITY'].reaction.reactionCrossReferences
L-phenylalanine zwitterion
CHEBI:58095
inhibits

Bifunctional chorismate mutase/prephenate dehydratase
UniProtKB:P0A9J8
  • UniProtKB:P0A9J8

    Source assertion: UniProt activity-regulation annotation: Both activities are inhibited by L-phenylalanine

    Source locationcomments[commentType='ACTIVITY REGULATION'].texts
Bifunctional chorismate mutase/prephenate dehydratase
UniProtKB:P0A9J8
located_in

cytoplasm
GO:0005737
  • UniProtKB:P0A9J8

    Source assertion: UniProt locates UniProtKB:P0A9J8 in Cytoplasm (SL-0086, mapped by UniProt to GO:0005737). Annotation evidence: ECO:0000305.

    Source locationcomments[commentType='SUBCELLULAR LOCATION'].subcellularLocations; UniProt location vocabulary GO mapping

References

Curation history