D00845
type: Enzyme
active site residues resources: Crystal structure of shikimate 5-dehydrogenase (SDH) bound to NADP: insights into function and evolution.
active site residues resources: Crystal structure of a novel shikimate dehydrogenase from Haemophilus influenzae.
active site residues resources: Structural analysis of a set of proteins resulting from a bacterial genomics project.
active site residues resources: Structural and biochemical analyses of shikimate dehydrogenase AroE from Aquifex aeolicus: implications for the catalytic mechanism.
active site residues resources: Crystal structures of shikimate dehydrogenase AroE from Thermus thermophilus HB8 and its cofactor and substrate complexes: insights into the enzymatic mechanism.
active site residues resources: 1.6 angstroms structure of an NAD+-dependent quinate dehydrogenase from Corynebacterium glutamicum.
active site residues resources: X-ray crystallographic and enzymatic analyses of shikimate dehydrogenase from Staphylococcus epidermidis.
cath: Leucine Dehydrogenase; Chain A, domain 1
cath: Rossmann fold
csa: 1nvt
ec: https://purl.uniprot.org/enzyme/1.1.1.25
kegg enzyme: Shikimate dehydrogenase
kegg pathway: Phenylalanine, tyrosine and tryptophan biosynthesis
kegg product: 3-dehydroshikimate
kegg product: NADPH
kegg product: H+
kegg substrate: shikimate
kegg substrate: NADP+
pdb: 1nvtA01
pdb: 1nvtB01
pdb: 2hk7A01
pdb: 2hk7B01
pdb: 2hk8A01
pdb: 2hk8B01
pdb: 2hk8C01
pdb: 2hk8D01
pdb: 2hk8E01
pdb: 2hk8F01
pdb: 2hk8G01
pdb: 2hk8H01
pdb: 2hk9A01
pdb: 2hk9B01
pdb: 2hk9C01
pdb: 2hk9D01
pdb: 1nytA01
pdb: 1nytB01
pdb: 1nytC01
pdb: 1nytD01
pdb: 1p74A01
pdb: 1p74B01
pdb: 1p77A01
pdb: 3donA01
pdb: 3dooA01
pdb: 2eggA01
pdb: 2eggB01
pdb: 1wxdA01
pdb: 1wxdB01
pdb: 2cy0A01
pdb: 2cy0B01
pdb: 2d5cA01
pdb: 2d5cB01
pdb: 2ev9A01
pdb: 2ev9B01
pdb: 1nvtA02
pdb: 1nvtB02
pdb: 2hk7A02
pdb: 2hk7B02
pdb: 2hk8A02
pdb: 2hk8B02
pdb: 2hk8C02
pdb: 2hk8D02
pdb: 2hk8E02
pdb: 2hk8F02
pdb: 2hk8G02
pdb: 2hk8H02
pdb: 2hk9A02
pdb: 2hk9B02
pdb: 2hk9C02
pdb: 2hk9D02
pdb: 1nytA02
pdb: 1nytB02
pdb: 1nytC02
pdb: 1nytD02
pdb: 1p74A02
pdb: 1p74B02
pdb: 1p77A02
pdb: 3donA02
pdb: 3dooA02
pdb: 2eggA02

Analogue
compound: shikimate
ligand het code: DTV
pdb: 1nytA01

Analogue
compound: NADP+
ligand het code: ATR
pdb: 2hk9A02

Analogue
compound: NADP+
ligand het code: ATR
pdb: 1p77A02

ReferenceForCatalyticMechanism
reference index: 3
reference section: p.19470-19471

ReferenceForCatalyticMechanism
reference index: 5
reference section: Fig.5, p.7168-7169

ReferenceForCatalyticMechanism
reference index: 6
reference section: p.17105-17107

ReferenceForCatalyticMechanism
reference index: 8
reference section: p.7791-7794

ReferenceForCatalyticMechanism
reference index: 9
reference section: Fig.4, p.9519-9521

ReferenceForCatalyticMechanism
reference index: 10
reference section: Fig.8, p.432-435

ReferenceForCatalyticMechanism
reference index: 13
reference section: p.4-6

ReferenceForCatalyticMechanism
reference index: 14
reference section: Fig.4, p.1130-1132, p.1136

Leucine Dehydrogenase; Chain A, domain 1
type: Cath
catalytic domain: index.html
references: http://www.cathdb.info/version/latest/superfamily/3.40.192.10

Rossmann fold
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.40.50.720

H+
type: KeggProduct
compound type: others
references: KEGG:C00080
references: CHEBI:15378
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Phenylalanine, tyrosine and tryptophan biosynthesis
type: KeggPathway
references: KEGG:MAP00400

The crystal structure of shikimate dehydrogenase (AroE) reveals a unique NADPH binding mode.
type: BibliographicResource
authors:
  item: Ye S
  item: Von Delft F
  item: Brooun A
  item: Knuth MW
  item: Swanson RV
  item: McRee DE
journal: J Bacteriol
pages: 4144-51
published year: 2003
volume: 185
references: http://www.ncbi.nlm.nih.gov/pubmed/12837789
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P43876
comment: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH NADP, SUBUNIT.

A phylogenomic analysis of the shikimate dehydrogenases reveals broadscale functional diversification and identifies one functionally distinct subclass.
type: BibliographicResource
authors:
  item: Singh S
  item: Stavrinides J
  item: Christendat D
  item: Guttman DS
journal: Mol Biol Evol
pages: 2221-32
published year: 2008
volume: 25
references: http://www.ncbi.nlm.nih.gov/pubmed/18669580

The conserved Lysine69 residue plays a catalytic role in Mycobacterium tuberculosis shikimate dehydrogenase.
type: BibliographicResource
authors:
  item: Rodrigues VS Jr
  item: Breda A
  item: Santos DS
  item: Basso LA
journal: BMC Res Notes
pages: 227
published year: 2009
volume: 2
references: http://www.ncbi.nlm.nih.gov/pubmed/19917104

Structural studies of shikimate dehydrogenase from Bacillus anthracis complexed with cofactor NADP.
type: BibliographicResource
authors:
  item: Barcellos GB
  item: Caceres RA
  item: de Azevedo WF Jr
journal: J Mol Model
pages: 147-55
published year: 2009
volume: 15
references: http://www.ncbi.nlm.nih.gov/pubmed/19043750

The 2.3-A crystal structure of the shikimate 5-dehydrogenase orthologue YdiB from Escherichia coli suggests a novel catalytic environment for an NAD-dependent dehydrogenase.
type: BibliographicResource
authors:
  item: Benach J
  item: Lee I
  item: Edstrom W
  item: Kuzin AP
  item: Chiang Y
  item: Acton TB
  item: Montelione GT
  item: Hunt JF
journal: J Biol Chem
pages: 19176-82
published year: 2003
volume: 278
references: http://www.ncbi.nlm.nih.gov/pubmed/12624088
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P0A6D5
comment: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH NAD, FUNCTION, SUBUNIT.

Structures of shikimate dehydrogenase AroE and its Paralog YdiB. A common structural framework for different activities.
type: BibliographicResource
authors:
  item: Michel G
  item: Roszak AW
  item: Sauve V
  item: Maclean J
  item: Matte A
  item: Coggins JR
  item: Cygler M
  item: Lapthorn AJ
journal: J Biol Chem
pages: 19463-72
published year: 2003
volume: 278
references: http://www.ncbi.nlm.nih.gov/pubmed/12637497
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P15770
references: P0A6D5
comment: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH NADP, SUBUNIT. , X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH NAD, CATALYTIC ACTIVITY, SUBUNIT.

Site-directed mutagenesis of the active site region in the quinate/shikimate 5-dehydrogenase YdiB of Escherichia coli.
type: BibliographicResource
authors:
  item: Lindner HA
  item: Nadeau G
  item: Matte A
  item: Michel G
  item: Menard R
  item: Cygler M
journal: J Biol Chem
pages: 7162-9
published year: 2005
volume: 280
references: http://www.ncbi.nlm.nih.gov/pubmed/15596430

Structure of Arabidopsis dehydroquinate dehydratase-shikimate dehydrogenase and implications for metabolic channeling in the shikimate pathway.
type: BibliographicResource
authors:
  item: Singh SA
  item: Christendat D
journal: Biochemistry
pages: 7787-96
published year: 2006
volume: 45
references: http://www.ncbi.nlm.nih.gov/pubmed/16784230
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: Q9SQT8
comment: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 90-603 IN COMPLEX WITH SHIKIMATE AND TARTRATE, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF SER-336; SER-338; LYS-385; ASP-423 AND TYR-550.

Crystal structures of shikimate dehydrogenase AroE from Thermus thermophilus HB8 and its cofactor and substrate complexes: insights into the enzymatic mechanism.
type: BibliographicResource
authors:
  item: Bagautdinov B
  item: Kunishima N
journal: J Mol Biol
pages: 424-38
published year: 2007
volume: 373
references: http://www.ncbi.nlm.nih.gov/pubmed/17825835
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: Q5SJF8
comment: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).

1.6 angstroms structure of an NAD+-dependent quinate dehydrogenase from Corynebacterium glutamicum.
type: BibliographicResource
authors:
  item: Schoepe J
  item: Niefind K
  item: Schomburg D
journal: Acta Crystallogr D Biol Crystallogr
pages: 803-9
published year: 2008
volume: D64
references: http://www.ncbi.nlm.nih.gov/pubmed/18566515
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: Q9X5C9
comment: X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS), FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, REACTION MECHANISM.

X-ray crystallographic and enzymatic analyses of shikimate dehydrogenase from Staphylococcus epidermidis.
type: BibliographicResource
authors:
  item: Han C
  item: Hu T
  item: Wu D
  item: Qu S
  item: Zhou J
  item: Ding J
  item: Shen X
  item: Qu D
  item: Jiang H
journal: FEBS J
pages: 1125-39
published year: 2009
volume: 276
references: http://www.ncbi.nlm.nih.gov/pubmed/19215302
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).

Crystal structure of shikimate 5-dehydrogenase (SDH) bound to NADP: insights into function and evolution.
type: BibliographicResource
authors:
  item: Padyana AK
  item: Burley SK
journal: Structure
pages: 1005-13
published year: 2003
volume: 11
references: http://www.ncbi.nlm.nih.gov/pubmed/12906831
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: Q58484
comment: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEX WITH NADP, SUBUNIT.

Crystal structure of a novel shikimate dehydrogenase from Haemophilus influenzae.
type: BibliographicResource
authors:
  item: Singh S
  item: Korolev S
  item: Koroleva O
  item: Zarembinski T
  item: Collart F
  item: Joachimiak A
  item: Christendat D
journal: J Biol Chem
pages: 17101-8
published year: 2005
volume: 280
references: http://www.ncbi.nlm.nih.gov/pubmed/15735308
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P44774
comment: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS), FUNCTION, MUTAGENESIS OF LYS-67 AND ASP-103, SUBUNIT.

Structural analysis of a set of proteins resulting from a bacterial genomics project.
type: BibliographicResource
authors:
  item: Badger J
  item: Christopher JA
  item: Emtage S
  item: Eroshkina A
  item: Feil I
  item: Furlong EB
  item: Gajiwala KS
  item: Gao X
  item: He D
  item: Hendle J
  item: Huber A
  item: Sauder JM
  item: Hoda K
  item: Kearins P
  item: Kissinger C
  item: Laubert B
  item: Lewis HA
  item: Lin J
  item: Loomis K
  item: Lorimer D
  item: Louie G
  item: Maletic M
  item: Adams JM
  item: Marsh CD
  item: Miller I
  item: Molinari J
  item: Muller-Dieckmann HJ
  item: Newman JM
  item: Noland BW
  item: Pagarigan B
  item: Park F
  item: Peat TS
  item: Post KW
  item: Antonysamy S
  item: Radojicic S
  item: Ramos A
  item: Romero R
  item: Rutter ME
  item: Sanderson WE
  item: Schwinn KD
  item: Tresser J
  item: Winhoven J
  item: Wright TA
  item: Wu L
  item: Bain K
  item: Xu J
  item: Harris TJ
  item: Bergseid MG
  item: Buchanan SG
  item: Buchanan MD
  item: Batiyenko Y
journal: Proteins
pages: 787-96
published year: 2005
volume: 60
references: http://www.ncbi.nlm.nih.gov/pubmed/16021622
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P0A6D5
comment: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 2-288 IN COMPLEX WITH NAD.

Structural and biochemical analyses of shikimate dehydrogenase AroE from Aquifex aeolicus: implications for the catalytic mechanism.
type: BibliographicResource
authors:
  item: Gan J
  item: Ji X
  item: Wu Y
  item: Prabakaran P
  item: Gu Y
  item: Li Y
  item: Andrykovitch M
  item: Liu H
  item: Gong Y
  item: Yan H
journal: Biochemistry
pages: 9513-22
published year: 2007
volume: 46
references: http://www.ncbi.nlm.nih.gov/pubmed/17649975
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).

2d5cA01
type: Pdb
catalytic residue: LYS 64;ASP 100
references: 2d5c
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2d5c

2d5cB01
type: Pdb
catalytic residue: LYS 64;ASP 100
references: 2d5c
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2d5c

2ev9A01
type: Pdb
catalytic residue: LYS 64;ASP 100
references: 2ev9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2ev9

2ev9B01
type: Pdb
catalytic residue: LYS 64;ASP 100
references: 2ev9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2ev9

2hk9A01
type: Pdb
catalytic residue: LYS 70;ASP 106
references: 2hk9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2hk9

2hk9B01
type: Pdb
catalytic residue: LYS 70;ASP 106
references: 2hk9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2hk9

2hk9C01
type: Pdb
catalytic residue: LYS 70;ASP 106
references: 2hk9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2hk9

2hk9D01
type: Pdb
catalytic residue: LYS 70;ASP 106
references: 2hk9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2hk9

3dooA01
type: Pdb
catalytic residue: LYS 64;ASP 100
references: 3doo
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3doo

1nvtA01
type: Pdb
catalytic residue: LYS 75;ASP 111
references: 1nvt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1nvt

1nvtB01
type: Pdb
catalytic residue: LYS 75;ASP 111
references: 1nvt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1nvt

1nytA01
type: Pdb
catalytic residue: LYS 65;ASP 102
references: 1nyt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1nyt

1nytB01
type: Pdb
catalytic residue: LYS 65;ASP 102
references: 1nyt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1nyt

1nytC01
type: Pdb
catalytic residue: LYS 65;ASP 102
references: 1nyt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1nyt

1nytD01
type: Pdb
catalytic residue: LYS 65;ASP 102
references: 1nyt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1nyt

1p74A01
type: Pdb
catalytic residue: LYS 65;ASP 102
references: 1p74
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1p74

1p74B01
type: Pdb
catalytic residue: LYS 65;ASP 102
references: 1p74
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1p74

1p77A01
type: Pdb
catalytic residue: LYS 65;ASP 102
references: 1p77
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1p77

1wxdA01
type: Pdb
catalytic residue: LYS 64;ASP 100
references: 1wxd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1wxd

1wxdB01
type: Pdb
catalytic residue: LYS 64;ASP 100
references: 1wxd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1wxd

2cy0A01
type: Pdb
catalytic residue: LYS 64;ASP 100
references: 2cy0
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2cy0

2cy0B01
type: Pdb
catalytic residue: LYS 64;ASP 100
references: 2cy0
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2cy0

2eggA01
type: Pdb
catalytic residue: LYS 87;ASP 123
references: 2egg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2egg

2eggB01
type: Pdb
catalytic residue: LYS 87;ASP 123
references: 2egg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2egg

2hk7A01
type: Pdb
catalytic residue: LYS 70;ASP 106
references: 2hk7
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2hk7

2hk7B01
type: Pdb
catalytic residue: LYS 70;ASP 106
references: 2hk7
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2hk7

2hk8A01
type: Pdb
catalytic residue: LYS 70;ASP 106
references: 2hk8
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2hk8

2hk8B01
type: Pdb
catalytic residue: LYS 70;ASP 106
references: 2hk8
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2hk8

2hk8C01
type: Pdb
catalytic residue: LYS 70;ASP 106
references: 2hk8
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2hk8

2hk8D01
type: Pdb
catalytic residue: LYS 70;ASP 106
references: 2hk8
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2hk8

2hk8E01
type: Pdb
catalytic residue: LYS 70;ASP 106
references: 2hk8
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2hk8

2hk8F01
type: Pdb
catalytic residue: LYS 70;ASP 106
references: 2hk8
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2hk8

2hk8G01
type: Pdb
catalytic residue: LYS 70;ASP 106
references: 2hk8
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2hk8

2hk8H01
type: Pdb
catalytic residue: LYS 70;ASP 106
references: 2hk8
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2hk8

3donA01
type: Pdb
catalytic residue: LYS 64;ASP 100
references: 3don
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3don

NADP+
type: KeggSubstrate
compound type: amide group
compound type: amine group
compound type: nucleotide
references: KEGG:C00006
references: CHEBI:18009
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

shikimate
type: KeggSubstrate
compound type: carbohydrate
compound type: carboxyl group
references: KEGG:C00493
references: CHEBI:16119
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

NADPH
type: KeggProduct
compound type: amide group
compound type: amine group
compound type: nucleotide
references: KEGG:C00005
references: CHEBI:16474
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

3-dehydroshikimate
type: KeggProduct
compound type: carbohydrate
compound type: carboxyl group
references: KEGG:C02637
references: CHEBI:30918
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Dehydroshikimic reductase
type: KeggEnzyme

Shikimate oxidoreductase
type: KeggEnzyme

Shikimate:NADP+ oxidoreductase
type: KeggEnzyme

5-Dehydroshikimate reductase
type: KeggEnzyme

Shikimate 5-dehydrogenase
type: KeggEnzyme

5-Dehydroshikimic reductase
type: KeggEnzyme

DHS reductase
type: KeggEnzyme

Shikimate:NADP+ 5-oxidoreductase
type: KeggEnzyme

AroE
type: KeggEnzyme