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Information on EC 1.3.1.12 - prephenate dehydrogenase

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EC Tree
IUBMB Comments
This enzyme in the enteric bacteria also possesses chorismate mutase activity (EC 5.4.99.5 chorismate mutase) and converts chorismate into prephenate.
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This record set is specific for:
UNIPROT: O67636
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The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
t-protein, prephenate dehydrogenase, hydroxyphenylpyruvate synthase, pdhe-1, bifunctional t-protein, tyrap, tyra dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dehydrogenase, prephenate
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hydroxyphenylpyruvate synthase
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PDH
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
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redox reaction
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oxidation
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reduction
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SYSTEMATIC NAME
IUBMB Comments
prephenate:NAD+ oxidoreductase (decarboxylating)
This enzyme in the enteric bacteria also possesses chorismate mutase activity (EC 5.4.99.5 chorismate mutase) and converts chorismate into prephenate.
CAS REGISTRY NUMBER
COMMENTARY hide
9044-92-2
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9044-92-2
prephenate dehydrogenase
94859-19-5
hydroxyphenylpyruvate synthase: chorismate mutase-prephenate dehydrogenase bifunctional enzyme
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
prephenate + NAD+
4-hydroxyphenylpyruvate + CO2 + NADH
show the reaction diagram
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
tyrosine
binds directly to the active site of the enzyme and not to an allosteric site. Linear competitive inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01 - 0.099
NAD+
0.104 - 4.132
prephenate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.3 - 11.6
NAD+
0.0034 - 13
prephenate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0159 - 0.37
tyrosine
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
O67636_AQUAE
Aquifex aeolicus (strain VF5)
311
0
34850
TrEMBL
Secretory Pathway (Reliability: 1)
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
prephenate dehydrogenase bound with NAD+ plus either 4-hydroxyphenylpyuvate, 4-hydroxyphenylpropionate, or L-tyrosine. Resiudes His147 and Arg250 are key catalytic and binding groups, respectively, and Ser126 participates in both catalysis and substrate binding through the ligand 4-hydroxyl group. Inhibitor tyrosine binds directly to the active site of the enzyme and not to an allosteric site
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H147N
inactive, binds prephenate with apparent affinity similar to wild-type
H217A
40fold increase in Km for prephenate, no inhibition by tyrosine
H217N
30fold increase in Km for prephenate, no inhibition by tyrosine
R250Q
10fold increase in the Km for prephenate and a 20fold increase in Ki for tyrosine
S126A
15fold reduction in kcat, a 10fold increase in the Km value for prephenate, and a 2-fold increase in Ki for tyrosine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sun, W.; Shahinas, D.; Bonvin, J.; Hou, W.; Kimber, M.S.; Turnbull, J.; Christendat, D.
The crystal structure of Aquifex aeolicus prephenate dehydrogenase reveals the mode of tyrosine inhibition
J. Biol. Chem.
284
13223-13232
2009
Aquifex aeolicus (O67636), Aquifex aeolicus
Manually annotated by BRENDA team