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Information on EC 2.5.1.54 - 3-deoxy-7-phosphoheptulonate synthase
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EC Tree
2.5.1.54 3-deoxy-7-phosphoheptulonate synthaseSpecify your search results
Word Map
- 2.5.1.54
- shikimate
- chorismate
- mutase
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4.1.2.15
- prephenate
- l-phenylalanine
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feedback-resistant
- l-tyrosine
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feedback-insensitive
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phenylalanine-sensitive
- kdo8ps
- 8-phosphate
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tyrosine-sensitive
- arogenate
- l-tyr
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3-deoxy-d-manno-octulosonate-8-phosphate
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feedback-inhibited
- 3-deoxy-d-manno-octulosonate
- 3-dehydroshikimate
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tryptophan-sensitive
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arogfbr
- synthesis
- biotechnology
- agriculture
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
2-dehydro-3-deoxy-D-arabino-heptonate-7-phosphate D-erythrose-4-phosphate-lyase (pyruvate-phosphorylating), 2-dehydro-3-deoxy-phosphoheptanoate aldolase, 2-dehydro-3-deoxy-phosphoheptonate aldolase, 2-keto-3-deoxy-D-arabino-heptonic acid 7-phosphate synthetase, 3-deoxy-7-phosphoheptulonate synthase, 3-deoxy-D-arabino heptulosonate 7-phosphate synthase, 3-deoxy-D-arabino-2-heptulosonic acid 7-phosphate synthetase, 3-deoxy-D-arabino-heptolosonate-7-phosphate synthetase, 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase, 3-deoxy-D-arabino-heptulosonate 7-phosphate synthetase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-dehydro-3-deoxy-D-arabino-heptonate-7-phosphate D-erythrose-4-phosphate-lyase (pyruvate-phosphorylating)
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2-dehydro-3-deoxy-phosphoheptanoate aldolase
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2-dehydro-3-deoxy-phosphoheptonate aldolase
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2-keto-3-deoxy-D-arabino-heptonic acid 7-phosphate synthetase
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3-deoxy-7-phosphoheptulonate synthase
3-deoxy-D-arabino-2-heptulosonic acid 7-phosphate synthetase
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3-deoxy-D-arabino-heptolosonate-7-phosphate synthetase
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3-deoxy-D-arabino-heptulosonate 7-phosphate synthase
3-deoxy-D-arabino-heptulosonate 7-phosphate synthetase
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3-deoxy-D-arabino-heptulosonate-7-phosphate synthase
3-deoxy-D-arabinoheptulosonate-7-phosphate synthetase
7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate D-erythrose-4-phosphate-lyase (pyruvate-phosphorylating)
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7-phospho-2-keto-3-deoxy-D-arabino-heptonate D-erythrose-4-phosphate lyase (pyruvate-phosphorylating)
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aldolase, phospho-2-keto-3-deoxyheptanoate
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Aro4
AroA
AroA(Q)
aroF
AroFFR
AroG
D-erythrose-4-phosphate-lyase
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D-erythrose-4-phosphate-lyase (pyruvate-phosphorylating)
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DAH7-P synthase
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DAH7-P synthase (phe)
DAH7P synthase
DAH7PS
DAHP synthase
DAHP synthase-phe
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DAHP synthase-trp
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DAHP synthase-tyr
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DAHP(Phe)
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DAHPS
DAHPS(Tyr)
deoxy-D-arabino-heptulosonate-7-phosphate synthetase
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DHS1
EC 4.1.2.15
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formerly
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KDPH synthase
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KDPH synthetase
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MtDS
phospho-2-dehydro-3-deoxyheptonate aldolase
phospho-2-keto-3-deoxyheptanoate aldolase
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Phospho-2-keto-3-deoxyheptonate aldolase
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phospho-2-keto-3-deoxyheptonic aldolase
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phospho-2-oxo-3-deoxyheptonate aldolase
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phzC
additional information
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2 distinct homology classes: AroAI and AroAII, both being found in bacteria and higher plant chloroplasts, AroAII can be devided into 4 subgroups, phylogenetic evolution
3-deoxy-D-arabino-heptulosonate 7-phosphate synthase
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3-deoxy-D-arabino-heptulosonate-7-phosphate synthase
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3-deoxy-D-arabino-heptulosonate-7-phosphate synthase
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DAH7-P synthase (phe)
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DAHP synthase
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phospho-2-dehydro-3-deoxyheptonate aldolase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
mechanism
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phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
mechanism
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phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
sequential mechanism
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phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
sequential mechanism
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phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
sequential mechanism
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phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
sequential mechanism
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
ordered sequential mechanism
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phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
His268 is located in the active site
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phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
ordered ping-pong bi-bi mechanism
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phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
ordered ping-pong bi-bi mechanism
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phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
ordered ping-pong bi-bi mechanism
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phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
ordered ping-pong bi-bi mechanism
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phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
first substrate is phosphoenolpyruvate
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phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
first substrate is phosphoenolpyruvate
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phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
first substrate is phosphoenolpyruvate
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
Cys67 and Cys145 are important for the catalytic reaction
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phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
rapid equilibrium ordered mechanism, in which phosphoenolpyruvate is the first substrate to bind and 3-deoxy-D-arabinoheptulosonate 7-phosphate is the second product to be released
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phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
Lys186 is involved in hydrogen bonding with phosphoenolpyruvate
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
active site cysteines: Cys61 and Cys328
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phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
product release is rate-limiting, rate constant for product formation is higher with Mn2+ than with Zn2+ or Cu2+. Role of metal ion is to position the amino acids with the appropriate geometry required to coordinate and activate the water molecule
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phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
simultaneous presence of a metal ion and phosphoenolpyruvate result in an ordering of the protein into a conformation that is prepared for binding the second substrate erythrose 4-phosphate. Initial step of reaction is a nucleophilic attack of the double bond of phosphoenolpyruvate on the metal-activated carbonyl group of erythrose 4-phosphate
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
proposed mechanism of catalysis of NmeDAH7PS showing key nucleophilic role for active site WAT1, overview
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
ordered ping-pong bi-bi mechanism
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phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
first substrate is phosphoenolpyruvate
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phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
ordered ping-pong bi-bi mechanism
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phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
first substrate is phosphoenolpyruvate
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phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
aldol condensation
condensation
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
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SYSTEMATIC NAME
IUBMB Comments
phosphoenolpyruvate:D-erythrose-4-phosphate C-(1-carboxyvinyl)transferase (phosphate-hydrolysing, 2-carboxy-2-oxoethyl-forming)
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CAS REGISTRY NUMBER
COMMENTARY
9026-94-2
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
phosphoenol-3-fluoropyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-erythro-hept-2-ulosonate 7-phosphate + phosphate
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enzyme does not discriminate between (E) and (Z)-form of phosphoenol-3-fluoropyruvate
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?
phosphoenolpyruvate + (3S)-2-deoxyerythrose 4-phosphate + H2O
(5S)-[5H]-3,5-dideoxy-D-arabinoheptulosonate 7-phosphate + phosphate
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ir
phosphoenolpyruvate + 2-deoxy-D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
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?
phosphoenolpyruvate + 2-deoxy-D-ribose 5-phosphate
3,5-dideoxy-D-gluco-octulosonate 8-phosphate + 3,5-dideoxy-D-manno-octulosonate 8-phosphate + phosphate
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-
-
?
phosphoenolpyruvate + 2-deoxy-D-ribose 5-phosphate + H2O
3,5-dideoxy-D-gluco-octulosonate 8-phosphate + 3,5-dideoxy-D-manno-octulosonate 8-phosphate + phosphate
phosphoenolpyruvate + D,L-lyxose
2-dehydro-3-deoxy-D,L-galacto-octonate + phosphate
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D-lyxose or L-lyxose, at 1.8% of the activity with D-erythrose 4-phosphate
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-
?
phosphoenolpyruvate + D-arabinose
2-dehydro-3-deoxy-D-gluco-octonate + phosphate
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at 0.7% of the activity with D-erythrose 4-phosphate
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-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
3-deoxy-D-manno-octulosonate 8-phosphate + phosphate
phosphoenolpyruvate + D-erythrose
2-dehydro-3-deoxy-D-arabino-heptonate + phosphate
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at 93% of the activity with D-erythrose 4-phosphate
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?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-erythro-hept-2-ulosonate 7-phosphate + phosphate
phosphoenolpyruvate + D-fructose 1,6-diphosphate
?
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same activity as with D-erythrose 4-phosphate
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?
phosphoenolpyruvate + D-fructose 6-phosphate
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same activity as with D-erythrose 4-phosphate
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?
phosphoenolpyruvate + D-glyceraldehyde
2-dehydro-3-deoxy-D-threo-hexonate + phosphate
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at 176% of the activity with D-erythrose 4-phosphate
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?
phosphoenolpyruvate + D-ribose 5-phosphate
3-deoxy-D-altro-octulosonate 8-phosphate + phosphate
phosphoenolpyruvate + D-ribose 5-phosphate + H2O
3-deoxy-D-altro-octulosonate 8-phosphate + phosphate
phosphoenolpyruvate + D-ribulose 5-phosphate
?
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at 12% of the activity with D-erythrose 4-phosphate
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?
phosphoenolpyruvate + D-threose
2-dehydro-3-deoxy-D-xylo-heptonate + phosphate
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at 92% of the activity with D-erythrose 4-phosphate
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?
phosphoenolpyruvate + D-xylose
2-dehydro-3-deoxy-D-ido-octonate + phosphate
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at 1% of the activity with D-erythrose 4-phosphate
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?
phosphoenolpyruvate + erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
phosphoenolpyruvate + glycolaldehyde
(S)-2-oxo-4,5-dihydroxypentanoate + phosphate
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at 245% of the activity with D-erythrose 4-phosphate
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?
phosphoenolpyruvate + glyoxylate
S-4-hydroxy-2-oxo-1,5-pentanedioate + R-4-hydroxy-2-oxo-1,5-pentanedioate + phosphate
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at 205% of the activity with D-erythrose 4-phosphate
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?
phosphoenolpyruvate + L-erythrose
2-dehydro-3-deoxy-L-arabino-heptonate + phosphate
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at 70% of the activity with D-erythrose 4-phosphate
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?
phosphoenolpyruvate + L-glyceraldehyde
2-dehydro-3-deoxy-L-threo-hexonate + phosphate
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at 212% of the activity with D-erythrose 4-phosphate
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?
phosphoenolpyruvate + L-threose
2-dehydro-3-deoxy-L-xylo-heptonate + phosphate
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at 52% of the activity with D-erythrose 4-phosphate
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?
phosphoenolpyruvate + L-xylose
2-dehydro-3-deoxy-L-ido-octonate + phosphate
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at 1% of the activity with D-erythrose 4-phosphate
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?
phosphoenolpyruvate + 2-deoxy-D-ribose 5-phosphate + H2O
3,5-dideoxy-D-gluco-octulosonate 8-phosphate + 3,5-dideoxy-D-manno-octulosonate 8-phosphate + phosphate
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?
phosphoenolpyruvate + 2-deoxy-D-ribose 5-phosphate + H2O
3,5-dideoxy-D-gluco-octulosonate 8-phosphate + 3,5-dideoxy-D-manno-octulosonate 8-phosphate + phosphate
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?
phosphoenolpyruvate + D-arabinose 5-phosphate
3-deoxy-D-manno-octulosonate 8-phosphate + phosphate
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?
phosphoenolpyruvate + D-arabinose 5-phosphate
3-deoxy-D-manno-octulosonate 8-phosphate + phosphate
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?
phosphoenolpyruvate + D-arabinose 5-phosphate
3-deoxy-D-manno-octulosonate 8-phosphate + phosphate
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at 8% of the activity with D-erythrose 4-phosphate
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?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
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-
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?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
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-
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?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
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first enzyme of the aromatic amino acid biosynthesis
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?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
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-
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?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
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first enzyme of the aromatic amino acid biosynthesis
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?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
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-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
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key regulatory enzyme in L-Phe and L-Tyr biosynthesis
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?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
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-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
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-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
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first enzyme in the shikimic pathway leading to biosynthesis of aromatic amino acids
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?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
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regulatory role of thioredoxin of photosystem I on the chloroplastic enzyme
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?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
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DSH1 RNA levels increase in Arabidopsis leaves subjected either to physical wounding or to infiltration with pathogenic Pseudomonas syringae strains, DSH2 RNA levels are not increased by these treatments
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?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
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-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
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-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
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first enzyme of aromatic amino acids, folic acid and phenazine 1-carboxylic acid biosynthesis pathways
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?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
first enzyme of aromatic amino acids, folic acid and phenazine 1-carboxylic acid biosynthesis pathways
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?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
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-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
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effect of external factors on regulation
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-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
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one of the key regulator enzymes of the shikimic acid pathway
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-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
no repression by the aromatic amino acids
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
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-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
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no repression by the aromatic amino acids
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
first enzyme of the aromatic amino acid biosynthesis
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
ir
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
ir
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
ir
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
ir
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
-
ir
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
binds 1 molecule D-erythrose 4-phosphate per subunit
-
ir
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
first enzyme in the shikimic pathway leading to biosynthesis of aromatic amino acids
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
first enzyme of the aromatic amino acid biosynthesis
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
first enzyme of the aromatic amino acid biosynthesis
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
Escherichia coli NST 37 / ATCC 31882
-
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
Escherichia coli W3110 / ATCC 27325
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
first enzyme of the aromatic amino acid biosynthesis
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
first enzyme of the aromatic amino acid biosynthesis
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
in solution D-erythrose 4-phosphate forms dimers that are in slow equilibrium with monomers
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
the plastidic enzyme form is induced by fungal elicitor of Phytophthora megasperma, the cytosolic enzyme form is not induced
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
r
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
first enzyme of the aromatic amino acid biosynthesis
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
enzyme is induced by N-[phosphomonomethyl]glycine
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
first enzyme of the aromatic amino acid biosynthesis
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
ir
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
-
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
phosphoenolpyruvate binding structure analysis
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
phosphoenolpyruvate interacts with conserved residues Arg167, Arg236, Lys188, Arg94, and Lys99, condensation reaction
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
phosphoenolpyruvate interacts with conserved residues Arg167, Arg236, Lys188, Arg94, and Lys99, condensation reaction
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
-
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
-
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
-
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
-
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-erythro-hept-2-ulosonate 7-phosphate + phosphate
-
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-erythro-hept-2-ulosonate 7-phosphate + phosphate
-
-
-
-
?
phosphoenolpyruvate + D-glucose 6-phosphate
?
-
as effective as D-erythrose 4-phosphate
-
-
?
phosphoenolpyruvate + D-glucose 6-phosphate
?
-
as effective as D-erythrose 4-phosphate
-
-
?
phosphoenolpyruvate + D-glucose 6-phosphate
?
-
at 0.5% of the activity with D-erythrose 4-phosphate
-
-
?
phosphoenolpyruvate + D-ribose 5-phosphate
3-deoxy-D-altro-octulosonate 8-phosphate + phosphate
-
as effective as D-erythrose 4-phosphate
-
-
?
phosphoenolpyruvate + D-ribose 5-phosphate
3-deoxy-D-altro-octulosonate 8-phosphate + phosphate
-
as effective as D-erythrose 4-phosphate
-
-
?
phosphoenolpyruvate + D-ribose 5-phosphate
3-deoxy-D-altro-octulosonate 8-phosphate + phosphate
-
-
-
-
?
phosphoenolpyruvate + D-ribose 5-phosphate
3-deoxy-D-altro-octulosonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-ribose 5-phosphate + H2O
3-deoxy-D-altro-octulosonate 8-phosphate + phosphate
-
-
-
-
?
phosphoenolpyruvate + D-ribose 5-phosphate + H2O
3-deoxy-D-altro-octulosonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-xylulose 5-phosphate
?
-
at 67% of the activity with D-erythrose 4-phosphate
-
-
?
phosphoenolpyruvate + D-xylulose 5-phosphate
?
-
at 67% of the activity with D-erythrose 4-phosphate
-
-
?
phosphoenolpyruvate + DL-glyceraldehyde 3-phosphate
pyruvate + phosphate
-
-
-
?
phosphoenolpyruvate + DL-glyceraldehyde 3-phosphate
pyruvate + phosphate
-
at 142% of the activity with D-erythrose 4-phosphate
-
-
?
phosphoenolpyruvate + erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
-
-
-
?
additional information
?
-
-
no activity with D-erythrose, D-glyceraldehyde 3-phosphate, ribose 5-phosphate, glucose 6-phosphate, glucosamine 6-phosphate, N-acetylglucosamine 6-phosphate, and pyruvate
-
-
?
additional information
?
-
-
no substrates are: D-glucose 6-phosphate, D-arabinose, DL-glyceraldehyde, D-erythrose, glycoaldehyde, DL-glyceraldehyde 3-phosphate
-
-
?
additional information
?
-
-
structure comparison between 3-deoxy-7-phosphoheptulonate synthase and 3-deoxy-D-manno-octulosonate 8-phosphate synthase, EC 4.1.2.16, reveal that they share a common ancestor and adopt the same catalytic strategy
-
-
?
additional information
?
-
kinetic mechanism is rapid equilibrium sequential ordered ter ter, with the essential divalent metal ion, Mn2+, binding first, followed by phosphoenolpyruvate and D-erythrose 4-phosphate
-
-
-
additional information
?
-
-
reaction involves interaction of si face of phosphoenolpyruvate with re face of eryxthrose 4-phosphate
-
-
?
additional information
?
-
no substrate: D-glyceraldehyde 3-phosphate, D-glucose 6-phosphate
-
-
?
additional information
?
-
-
no substrate: D-glyceraldehyde 3-phosphate, D-glucose 6-phosphate
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
phosphoenolpyruvate + erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
additional information
?
-
-
structure comparison between 3-deoxy-7-phosphoheptulonate synthase and 3-deoxy-D-manno-octulosonate 8-phosphate synthase, EC 4.1.2.16, reveal that they share a common ancestor and adopt the same catalytic strategy
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
first enzyme of the aromatic amino acid biosynthesis
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
first enzyme of the aromatic amino acid biosynthesis
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
key regulatory enzyme in L-Phe and L-Tyr biosynthesis
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
first enzyme in the shikimic pathway leading to biosynthesis of aromatic amino acids
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
regulatory role of thioredoxin of photosystem I on the chloroplastic enzyme
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
DSH1 RNA levels increase in Arabidopsis leaves subjected either to physical wounding or to infiltration with pathogenic Pseudomonas syringae strains, DSH2 RNA levels are not increased by these treatments
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
first enzyme of aromatic amino acids, folic acid and phenazine 1-carboxylic acid biosynthesis pathways
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
first enzyme of aromatic amino acids, folic acid and phenazine 1-carboxylic acid biosynthesis pathways
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
effect of external factors on regulation
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
one of the key regulator enzymes of the shikimic acid pathway
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
no repression by the aromatic amino acids
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
no repression by the aromatic amino acids
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
first enzyme of the aromatic amino acid biosynthesis
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
first enzyme in the shikimic pathway leading to biosynthesis of aromatic amino acids
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
first enzyme of the aromatic amino acid biosynthesis
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
first enzyme of the aromatic amino acid biosynthesis
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
first enzyme of the aromatic amino acid biosynthesis
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
first enzyme of the aromatic amino acid biosynthesis
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
the plastidic enzyme form is induced by fungal elicitor of Phytophthora megasperma, the cytosolic enzyme form is not induced
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
first enzyme of the aromatic amino acid biosynthesis
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
enzyme is induced by N-[phosphomonomethyl]glycine
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
first enzyme of the aromatic amino acid biosynthesis
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
-
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
-
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
-
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ba2+
presence of Ba2+ stimulates the activity by more than 300%
Ca2+
Cd2+
Co2+
Cu2+
Fe2+
Mg2+
Mn2+
Ni2+
Zn2+
additional information
Ca2+
presence of Ca2+ stimulates the activity by more than 300%
Co2+
-
90.6% increase of activity at 2 mM for isozyme NCgl0950 DAHP synthase, 31.8% increase of activity at 2 mM for isozyme NCgl2098 DAHP synthase
Co2+
-
2fold lower inhibition by fosmidomycin with Co2+ as cofactor than with Mn2+ or Fe2+, no effect with sulfoenolpyruvate 7 as potential inhibitor
Co2+
-
not required, Co2+ is inhibitory at concentrations above 0.1 mM
Co2+
-
absolute requirement for divalent metal, 70% of the activation with Mg2+
Co2+
-
isoenzyme Ds-Co has an absolute requirement for divalent cations, Co2+ being best
Fe2+
-
2fold greater inhibition by fosmidomycin with Fe2+ as cofactor than with Co2+, no effect with sulfoenolpyruvate 7 as potential inhibitor
Fe2+
a mononuclear iron enzyme, the enzyme required divalent metal cations, Fe2+ activates best, iron is the prosthetic metal in vivo
Mn2+
-
absolutely required, can partly be substituted by Mg2+, but not by Ca2+, Fe2+, and Co2+
Mn2+
-
257.5% increase of activity at 2 mM for isozyme NCgl0950 DAHP synthase, 1343.3% increase of activity at 2 mM for isozyme NCgl2098 DAHP synthase
Mn2+
-
2fold greater inhibition by fosmidomycin with Mn2+ as cofactor than with Co2+, no effect with sulfoenolpyruvate 7 as potential inhibitor
Mn2+
can substitute for Fe2+, activates DAHP synthase to about 70% of the iron-activated sample
Mn2+
-
a manganese ion is present at the active site, crystallization data
Mn2+
activates, best activating metal ion. The metal ion is coordinated by four protein ligands Cys63, His 270, Glu304, and Asp324
Mn2+
required, Mn2+ coordinates the PEP carboxylate functionality and a water molecule
Mn2+
-
absolute requirement for divalent metal, 15% of the activation with Mg2+
Mn2+
presence of Mn2+ stimulates the activity by more than 250%, Mn2+ is liganded by residues C36, H206, E232, and D243
Zn2+
cannot well substitute for Fe2+, activates DAHP synthase to about 20% of the iron-activated sample
additional information
-
Phe-sensitive isozyme: Mn2+, Co2+, Zn2+, Fe3+ have no effect
additional information
-
reactivation of EDTA-treated enzyme by divalent metyl ions, in decreasing order: Co2+, Mn2+, Ca2+, Mg2+, Cu2+, Zn2+
additional information
no effect by Mg2+, Ni2+, Ca2+, Ba2+, and Sr2+
additional information
-
no effect by Mg2+, Ni2+, Ca2+, Ba2+, and Sr2+
additional information
-
EDTA-inactivated enzyme, restoration in decreasing order of effectiveness by Zn2+, Cd2+, Mn2+, Co2+, Ni2+, Ca2+, Hg2+, Cu2+
additional information
-
Tyr-sensitive isozyme, metal factor required
additional information
-
reactivation of EDTA-inactivated enzyme in decreasing order by Zn2+, Cd2+, Mn2+, Cu2+, Co2+, Ni2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1R,2S)-1,2-epoxypropylphosphonic acid
-
-
(2R)-2-(phosphonooxy)propanoic acid
-
mimicking phosphohemiketal 2 (instable), competitive to substrate phosphoenolpyruvate
(2S)-2-(phosphonooxy)propanoic acid
-
mimicking phosphohemiketal 2 (instable), competitive to substrate phosphoenolpyruvate
(2Z)-3-phosphono-2-(trifluoromethyl)prop-2-enoic acid
-
trifluorinated phosphonate
(E)-2-methyl-3-phosphonoacrylic acid
-
most potent of the tested inhibitors mimicking intermediates in the reaction, vinyl phosphonate 4
2-(phosphonomethyl)prop-2-enoic acid
-
mimics substrate phosphoenolpyruvate, and should be inert due to alkene structure but lacking an electron-donor, acts as competitive inhibitor
CN-
-
Tyr-sensitive isozyme, strong inhibition, reactivation by divalent cations only to a small extent
diethyl dicarbonate
-
Phe-sensitive isozyme, pH-dependent, phosphoenolpyruvate protects wild-type and mutants H64G, H207G, H304G
fosmidomycin
-
uncompetitive inhibitor, maximum level of inhibition after 10 min incubation, extent of inhibition dependent on the type of the metal cofactor, competitive inhibitor with respect to phosphoenolpyruvate
H2O2
DAHP synthase enzymes are inactivated by H2O2 in vitro and in vivo, H2O2 displaces the iron atom from the enzyme, only the Fe2+-metalloform of the enzyme can be inactivated by hydrogen peroxide or superoxide
L-arogenate
-
isozyme DS-Mn, competitive against D-erythrose 4-phosphate, non-competitive against phosphoenolpyruvate
p-chloromercuribenzoate
-
complete inhibition at 0.02 mM, reversible by cysteine
phosphoenolpyruvate
pronounced substrate inhibition above 1 mM
superoxide
displaces the iron atom from the enzyme, only the Fe2+-metalloform of the enzyme can be inactivated by hydrogen peroxide or superoxide. Superoxide stress promotes the mismetallation of DAHP synthase
tetraammonium (((carboxymethyl)[(2S,3R,4S)-2,3,4-trihydroxy-5-(phosphonatooxy)pentyl]amino)methyl)phosphonate
-
IC50: 0.0066 mM
[(1E)-7-bromo-2-carboxyhept-1-en-1-yl]phosphonate
-
inhibitor based on vinyl phosphonate, designed to fit into the binding sites of both phosphoenolpyruvate and D-erythrose 4-phosphate substrates simultaneously. Competitive with respect to phosphoenolpyruvate
[2-carboxy-7-(phosphonatooxy)hept-1-en-1-yl]phosphonate
-
inhibitor based on vinyl phosphonate ratio Z:E enantiomer 1:1. Inhibitor is designed to fit into the binding sites of both phosphoenolpyruvate and D-erythrose 4-phosphate substrates simultaneously. Competitive with respect to phosphoenolpyruvate
[2-carboxy-7-(phosphonatooxy)hept-2-en-1-yl]phosphonate
-
inhibitor based on allyl phosphonate, ratio Z:E enantiomer 7:3. Inhibitor is designed to fit into the binding sites of both phosphoenolpyruvate and D-erythrose 4-phosphate substrates simultaneously. Competitive with respect to phosphoenolpyruvate
3-deoxy-D-arabinoheptulosonate-7-phosphate oxime
binding is competitive with respect to all three substrates.The oxime functional group, combined with two crystallographic waters, binds at the same location in the catalytic center as the phosphate group of the tetrahedral intermediate. DAHP oxime binds to only one subunit of each tight dimer
3-deoxy-D-arabinoheptulosonate-7-phosphate oxime
inhibitor shows a good correlation between transition state stabilization and inhibition. DAHP oxime is mimicking the first irreversible transition state of the DAHP synthase reaction, presumably phosphate departure from the tetrahedral intermediate
3-deoxy-D-arabinoheptulosonate-7-phosphate oxime
inhibition is competitive with respect to the essential metal ion, Mn2+. Inhibition shifts from metal-competitive at physiological pH to metal-noncompetitive at pH above 8.7 in response to deprotonation of the Cys61 side chain. Metal-competitive inhibition arises from interactions between Mn2+, DAHP oxime's O4 hydroxyl group, and the Cys61 and Asp326 side chains
7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate
-
competitive against D-erythrose 4-phosphate and phosphoenolpyruvate
chorismate
-
50% at 0.12 mM; feedback inhibition, noncompetitive against D-erythrose 4-phosphate and phosphoenolpyruvate
chorismate
-
competitive against phosphoenolpyruvate, noncompetitive against D-erythrose 4-phosphate; DAHP synthase-trp
chorismate
-
main allosteric feedback inhibitor and regulator for enzyme of class AroAII
Cu2+
-
0.02 mM, complete inactivation; Phe-sensitive isozyme, complete inactivation at 0.02 mM, destabilization of the enzymes quarternary structure; phosphoenolpyruvate protects
D-erythrose 4-phosphate
Phe-sensitive isozyme: in absence of phosphoenolpyruvate the enzyme is inhibited via formation of a covalent binding to Lys186 via a slow Schiff base reaction, mechanism
EDTA
2 mM, complete inactivation within 10 min
EDTA
-
22.7% residual activity at 2 mM EDTA for isozyme NCgl0950 DAHP synthase, 49.1% residual activity at 2 mM EDTA for isozyme NCgl2098 DAHP synthase
EDTA
-
Mn2+, Cd2+, Co2+, Fe2+, Cu2+, Mg2+ or Zn2+ reactivate, Fe2+ and Cu2+ only partially reactivate
EDTA
-
inactivation, reactivation by divalent metyl ions, in decreasing order: Co2+, Mn2+, Ca2+, Mg2+, Cu2+, Zn2+
EDTA
-
phosphoenolpyruvate or 3-deoxy-D-arabino-heptulosonate 7-phosphate and Mn2+, Co2+, Ca2+ and Mg2+ protect
EDTA
-
inactivation, restoration in decreasing order of effectiveness by Zn2+, Cd2+, Mn2+, Co2+, Ni2+, Ca2+, Hg2+, Cu2+
EDTA
-
Co2+, Mn2+, Zn2+ and Fe2+ restore activity; phosphoenolpyruvate, 2 mM, partially protects from inactivation, does not restore activity
EDTA
-
inactivation, reactivation in decreasing order by Zn2+, Cd2+, Mn2+, Cu2+, Co2+, Ni2+
Fe2+
-
0.02 mM: 60% inactivation. 0.2 mM: 90% inactivation; Phe-sensitive isozyme, 60% inactivation at 0.02 mM, 90% inactivation at 0.2 mM; phosphoenolpyruvate protects
L-Phe
-
NCgl0950 DAHP synthase is sensitive to feedback inhibition with 29.1 to 38.8% inhibition at 2 mM, NCgl2098 DAHP synthase is insensitive
L-phenylalanine
involved in allosteric regulation of the enzyme, inhibits the wild-type enzyme, and enzyme mutants H29A and H29S/S31H
L-Trp
-
NCgl0950 DAHP synthase is sensitive to feedback inhibition, NCgl2098 DAHP synthase is slightly sensitive to feedback inhibition with 10-15% decrease of activity at 5 mM L-Trp
L-Tyr
-
NCgl0950 DAHP synthase is sensitive to feedback inhibition with 80% loss of activity at 0.03 mM, NCgl2098 DAHP synthase is insensitive, Tyr-linked inhibition is competitive to phophoenolpyruvate
L-tyrosine
allosteric regulation of the enzyme is mediated by L-Tyr binding to a discrete ACT regulatory domain appended to a core catalytic (beta/alpha)8 barrel, highly reduced inhibition of enzyme mutant S31G. Comparison of the position of the regulatory ACT domain of TmaDAH7PS in the unbound and L-Tyr-bound conformations, overview
N-[Phosphomonomethyl]glycine
-
i.e. glyphosate; inhibition of isozyme DS-Co in vitro and in vivo, isozyme DS-Mn is only slightly inhibited in vitro
N-[Phosphomonomethyl]glycine
-
concentration of Co2+ markedly increases the concentration of N-[phosphomonomethyl]glycine required for inhibition; cytosolic isozyme; i.e. glyphosate
Phe
-
0.04 mM, 50% inhibition of DAHP synthase-phe; L-Phe; Phe-sensitive isozyme
Phe
-
feed-back inhibition, Phe-sensitive isozyme; Phe-sensitive isozyme
Phe
-
competitive with respect to D-erythrose 4-phosphate and non-competitive to phosphoenolpyruvate; Tyr-sensitive isozyme is less inhibited than the Phe-sensitive isozyme
Phe
-
competitive with respect to D-erythrose 4-phosphate and non-competitive to phosphoenolpyruvate; Phe-sensitive isozyme
Phe
-
no inhibition; Phe-sensitive isozyme; strain 12/60/X, no inhibition; strain H1, strain H20 and strain 3/2: cumulative inhibition of Tyr and Phe
phenylalanine
inhibition of the synthase-chorismate mutase complex, based on mutase activity measurements at 30°C, 50 mM BTP (1,3-bis[tris(hydroxymethyl)methylamino]propane), pH 7.5, 0.5 mM TCEP [tris(2-carboxyethyl)phosphine hydrochloride], 0.2 mM phosphoenolpyruvate, and 0.1 mM MnCl2
phosphate
-
non-competitive with respect to both phosphoenolpyruvate and D-erythrose 4-phosphate
phosphate
-
non-competitive with respect to both phosphoenolpyruvate and D-erythrose 4-phosphate
phosphate
-
non-competitive with respect to both phosphoenolpyruvate and D-erythrose 4-phosphate
phosphate
-
competitive to D-erythrose 4-phosphate, noncompetitive to phosphoenolpyruvate
phosphate
-
phosphate buffer destabilizes
prephenate
-
50% at 0.02 mM; feedback inhibition, noncompetitive against D-erythrose 4-phosphate and phosphoenolpyruvate
prephenate
-
isozyme DS-Mn, competitive against D-erythrose 4-phosphate, non-competitive against phosphoenolpyruvate
Trp
-
0.02 mM, 65% inhibition; non-competitive against phosphoenolpyruvate and competitive for D-erythrose 4-phosphate; strongly dependent on pH; Trp-sensitive isozyme
Trp
-
non-competitive against phosphoenolpyruvate and competitive for D-erythrose 4-phosphate; Trp-sensitive isozyme
Trp
-
allosteric, best at pH 6.0, no inhibition at pH 7.3; Trp-sensitive isozyme
Trp
-
DAHP synthase-trp; non-competitive against phosphoenolpyruvate and competitive for D-erythrose 4-phosphate; Trp-sensitive isozyme
Tyr
-
feedback inhibition; noncompetitive with respect to D-erythrose 4-phosphate, competitive with respect to phosphoenolpyruvate; Tyr-sensitive isozyme; wild-type and mutant S187A
Tyr
-
0.04 mM, 50% inhibition of DAHP synthase-tyr; L-Tyr; Tyr-sensitive isozyme
Tyr
-
feedback inhibition; noncompetitive with respect to D-erythrose 4-phosphate, competitive with respect to phosphoenolpyruvate; Tyr-sensitive isozyme
Tyr
-
wild-type isozyme, mutant N8K and N-terminal deletion mutant are not inhibited, N-terminus is structurally involved in the sensitivity for feedback inhibition
Tyr
-
noncompetitive with respect to D-erythrose 4-phosphate, competitive with respect to phosphoenolpyruvate; Tyr-sensitive isozyme
Tyr
-
noncompetitive with respect to D-erythrose 4-phosphate, competitive with respect to phosphoenolpyruvate; Tyr-sensitive isozyme
Tyr
-
strain 33/X strongly but not totally inhibited; strain H1, strain H20 and strain 3/2: cumulative inhibition of Tyr and Phe; Tyr-sensitive isozyme
tyrosine
inhibition of the synthase-chorismate mutase complex, based on mutase activity measurements at 30°C, 50 mM BTP (1,3-bis[tris(hydroxymethyl)methylamino]propane), pH 7.5, 0.5 mM TCEP [tris(2-carboxyethyl)phosphine hydrochloride], 0.2 mM phosphoenolpyruvate, and 0.1 mM MnCl2
additional information
substrate D-erythrose 4-phosphate is not inhibitory
-
additional information
none of the downstream products of the shikimate biosynthetic pathway tested inhibits the activity of the enzyme
-
additional information
-
none of the downstream products of the shikimate biosynthetic pathway tested inhibits the activity of the enzyme
-
additional information
-
no inhibition by aromatic amino acids, folic acid, phenazine 1-carboxylic acid, anthranilic acid, shikimic acid, p-aminobenzoic acid and 3-hydroxyanthranilic acid
-
additional information
-
structure and reaction intermediate mimic inhibitors; sulfoenolpyruvate 7 mimics substrate phosphoenolpyruvate, sulfate exchanges phosphate ester, no inhibition up to a concentration of 10 mM
-
additional information
isozyme AroG is not inhibited by L-Phe. In peroxide-stressed cells, the enzyme accumulates as an apoprotein, potentially with an oxidized cysteine residue. In superoxide-stressed cells, the enzyme acquires a nonactivating zinc ion in its active site, an apparent consequence of the repeated ejection of iron. Manganese supplementation protects the activity in both cases, which matches the ability of manganese to metallate the enzyme and to provide substantial oxidant-resistant activity. The damage to DAHP synthase can be completely restored in vivo, while in vitro, restoration is only partly, overview. Escherichia coli attempts to compensate for diminished DAHP synthase activity by increasing expression
-
additional information
-
isozyme AroG is not inhibited by L-Phe. In peroxide-stressed cells, the enzyme accumulates as an apoprotein, potentially with an oxidized cysteine residue. In superoxide-stressed cells, the enzyme acquires a nonactivating zinc ion in its active site, an apparent consequence of the repeated ejection of iron. Manganese supplementation protects the activity in both cases, which matches the ability of manganese to metallate the enzyme and to provide substantial oxidant-resistant activity. The damage to DAHP synthase can be completely restored in vivo, while in vitro, restoration is only partly, overview. Escherichia coli attempts to compensate for diminished DAHP synthase activity by increasing expression
-
additional information
-
not inhibitory: phenylalanine, tyrosine, tryptophan, chorismate
-
additional information
inhibitor screening, docking study, molecular dynamics and molecular modelling, induced fit docking scores, overview. alpha-Tocopherol, 3-pyridine carboxyaldehyde, and rutin can be drug leads to inhibit mtDAH7Ps in Mycobacterium tuberculosis
-
additional information
-
inhibitor screening, docking study, molecular dynamics and molecular modelling, induced fit docking scores, overview. alpha-Tocopherol, 3-pyridine carboxyaldehyde, and rutin can be drug leads to inhibit mtDAH7Ps in Mycobacterium tuberculosis
-
additional information
binding structure determination and analysis, overview. The side chains of enzyme residues Lys188, Arg167 and Arg236 and the main chain peptide N of Ala166 that interact with the phosphate moiety of phosphoenolpyruvate form similar interactions with the phosphate or phosphonate functionalities of the three ligands, consistent with this portion of each inhibitor being able to mimic the phosphoenolpyruvate binding characteristics well. The tetrameric quaternary structures of enzyme NmeDAH7PS bound with (S)-phospholactate and vinyl phosphonate are identical to that of the isomorphous phosphoenolpyruvate-bound parent structure, PDB ID 4HSN. The increased inhibitor potency observed for the vinyl phosphonate over the (R)-phospholactate suggests that the active site is better prepared to accommodate a planar rather than tetrahedral intermediate
-
additional information
-
binding structure determination and analysis, overview. The side chains of enzyme residues Lys188, Arg167 and Arg236 and the main chain peptide N of Ala166 that interact with the phosphate moiety of phosphoenolpyruvate form similar interactions with the phosphate or phosphonate functionalities of the three ligands, consistent with this portion of each inhibitor being able to mimic the phosphoenolpyruvate binding characteristics well. The tetrameric quaternary structures of enzyme NmeDAH7PS bound with (S)-phospholactate and vinyl phosphonate are identical to that of the isomorphous phosphoenolpyruvate-bound parent structure, PDB ID 4HSN. The increased inhibitor potency observed for the vinyl phosphonate over the (R)-phospholactate suggests that the active site is better prepared to accommodate a planar rather than tetrahedral intermediate
-
additional information
undergoes no significant conformational change on inhibitor binding, crystal structure analysis, overview. Allosteric response arising from changes in protein motion rather than conformation, and suggest ligands that modulate protein dynamics may be effective inhibitors of this enzyme
-
additional information
-
undergoes no significant conformational change on inhibitor binding, crystal structure analysis, overview. Allosteric response arising from changes in protein motion rather than conformation, and suggest ligands that modulate protein dynamics may be effective inhibitors of this enzyme
-
additional information
not inhibitory: phenylalanine, tyrosine, tryptophane
-
additional information
-
not inhibitory: phenylalanine, tyrosine, tryptophane
-
additional information
-
resistant to denaturation by sodium dodecyl sulfate, not inhibitory: phenylalanine, tyrosine, tryptophan
-
additional information
-
not inhibitory: L-tryptophan, chorismate, shikimate, D-phenylalanine, L-histidine
-
additional information
small angle X-ray (SAXS) scattering analysis
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
reduced thioredoxin
-
required for activity, can be partially substituted by dithiothreitol
dithiothreitol
-
can partially substitute thioredoxin as activating agent
additional information
-
DHS1 is induced 3-5fold by wounding of the leaf and pathogen attack
-
additional information
-
sulfhydryl groups and possibly a Lys residue may be implicated in activity
-
additional information
-
enzyme uses divalent metal ion to activate a phosphorylated carbohydrate-like substrate
-
additional information
-
not hysteretically activated by dithiols, e.g. DTT
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Infections
Increased phenylalanine levels in plant leaves reduces susceptibility to Botrytis cinerea.
Meningitis, Bacterial
Structural analysis of substrate-mimicking inhibitors in complex with Neisseria meningitidis 3-deoxy-d-arabino-heptulosonate 7-phosphate synthase - The importance of accommodating the active site water.
Tuberculosis
A novel noncovalent complex of chorismate mutase and DAHP synthase from Mycobacterium tuberculosis: protein purification, crystallization and X-ray diffraction analysis.
Tuberculosis
A pseudo-isostructural type II DAH7PS enzyme from Pseudomonas aeruginosa: alternative evolutionary strategies to control shikimate pathway flux.
Tuberculosis
Complex Formation between Two Biosynthetic Enzymes Modifies the Allosteric Regulatory Properties of Both: AN EXAMPLE OF MOLECULAR SYMBIOSIS.
Tuberculosis
Crystallization and preliminary X-ray crystallographic analysis of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Mycobacterium tuberculosis.
Tuberculosis
DAHP synthase from Mycobacterium tuberculosis H37Rv: cloning, expression, and purification of functional enzyme.
Tuberculosis
Dynamic cross-talk among remote binding sites: the molecular basis for unusual synergistic allostery.
Tuberculosis
Functional mapping of protein-protein interactions in an enzyme complex by directed evolution.
Tuberculosis
In Silico sequence analysis and molecular modeling of the three-dimensional structure of DAHP synthase from Pseudomonas fragi.
Tuberculosis
Inter-Enzyme Allosteric Regulation of Chorismate Mutase in Corynebacterium glutamicum: Structural Basis of Feedback Activation by Trp.
Tuberculosis
Interaction between DAHP synthase and chorismate mutase endows new regulation on DAHP synthase activity in Corynebacterium glutamicum.
Tuberculosis
Investigating the role of the hydroxyl groups of substrate erythrose 4-phosphate in the reaction catalysed by the first enzyme of the shikimate pathway.
Tuberculosis
Potent inhibitors of a shikimate pathway enzyme from Mycobacterium tuberculosis: combining mechanism- and modeling-based design.
Tuberculosis
Probing the Sophisticated Synergistic Allosteric Regulation of Aromatic Amino Acid Biosynthesis in Mycobacterium tuberculosis Using ?-Amino Acids.
Tuberculosis
Quaternary structure is an essential component that contributes to the sophisticated allosteric regulation mechanism in a key enzyme from Mycobacterium tuberculosis.
Tuberculosis
Synergistic allostery, a sophisticated regulatory network for the control of aromatic amino acid biosynthesis in Mycobacterium tuberculosis.
Tuberculosis
Three Sites and You Are Out: Ternary Synergistic Allostery Controls Aromatic Amino Acid Biosynthesis in Mycobacteriumtuberculosis.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.013
D-erythrose 4-phosphate
-
pH 7.4, 37°C
0.013
D-erythrose 4-phosphate
pH 7.3, temperature not specified in the publication, wild-type enzyme
0.028
D-erythrose 4-phosphate
pH 7.3, temperature not specified in the publication, mutant H29S/S31H
0.03
D-erythrose 4-phosphate
pH 7.3, temperature not specified in the publication, mutant H29A
0.033
D-erythrose 4-phosphate
pH 7.3, temperature not specified in the publication, mutant S31G
0.25
D-erythrose 4-phosphate
-
Trp-sensitive isozyme, pH 7.2, 37°C
0.29
D-erythrose 4-phosphate
-
isozyme NCgl0950 DAHP synthase, in 50 mM Tris-HCl buffer, pH 7.5, at 30°C
2.17
D-erythrose 4-phosphate
-
isozyme NCgl2098 DAHP synthase, in 50 mM Tris-HCl buffer, pH 7.5,at 30°C
0.00485
phosphoenolpyruvate
pH 7.3, temperature not specified in the publication, wild-type enzyme
0.005
phosphoenolpyruvate
-
recombinant enzyme, with D-arabinose 5-phosphate as cosubstrate, pH 7.5, 25°C
0.0053
phosphoenolpyruvate
-
recombinant enzyme, with erythrose 4-phosphate as cosubstrate, pH 7.5, 25°C
0.01
phosphoenolpyruvate
-
recombinant enzyme, with ribose 5-phosphate as cosubstrate, pH 7.5, 25°C
0.0128
phosphoenolpyruvate
pH 7.3, temperature not specified in the publication, mutant S31G
0.015
phosphoenolpyruvate
-
pH 7.4, 37°C
0.015
phosphoenolpyruvate
-
recombinant enzyme, with 2-deoxyribose 5-phosphate as cosubstrate, pH 7.5, 25°C
0.021
phosphoenolpyruvate
pH 7.3, temperature not specified in the publication, mutant H29A
0.033
phosphoenolpyruvate
pH 6.8, 60°C, cosubstrate 2-deoxy-D-erythrose 4-phosphate
0.035
phosphoenolpyruvate
pH 6.8, 60°C, cosubstrate 2-deoxy-D-ribose 5-phosphate
0.036
phosphoenolpyruvate
pH 6.8, 60°C, cosubstrate D-ribose 5-phosphate
0.039
phosphoenolpyruvate
pH 7.3, temperature not specified in the publication, mutant H29S/S31H
0.062
phosphoenolpyruvate
pH 6.8, 60°C, cosubstrate D-arabinose 5-phosphate
0.093
phosphoenolpyruvate
pH 6.8, 60°C, cosubstrate D-erythrose 4-phosphate
0.16
phosphoenolpyruvate
-
isozyme NCgl0950 DAHP synthase, in 50 mM Tris-HCl buffer, pH 7.5, at 30°C
8.52
phosphoenolpyruvate
-
isozyme NCgl2098 DAHP synthase, in 50 mM Tris-HCl buffer, pH 7.5, at 30°C
additional information
additional information
-
kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics, kinetics in presence of inhibitors L-phe and L-Tyr
-
additional information
additional information
-
Michaelis-Menten kinetics, kinetics in presence of inhibitors L-phe and L-Tyr
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.3
D-erythrose 4-phosphate
-
isozyme NCgl0950 DAHP synthase, in 50 mM Tris-HCl buffer, pH 7.5, at 30°C
1.14
D-erythrose 4-phosphate
-
isozyme NCgl2098 DAHP synthase, in 50 mM Tris-HCl buffer, pH 7.5, at 30°C
11.7
D-erythrose 4-phosphate
pH 7.3, temperature not specified in the publication, wild-type enzyme
14.1
D-erythrose 4-phosphate
pH 7.3, temperature not specified in the publication, mutant H29S/S31H
14.3
D-erythrose 4-phosphate
pH 7.3, temperature not specified in the publication, mutant S31G
17.5
D-erythrose 4-phosphate
pH 7.3, temperature not specified in the publication, mutant H29A
0.35
phosphoenolpyruvate
-
isozyme NCgl0950 DAHP synthase, in 50 mM Tris-HCl buffer, pH 7.5, at 30°C
1.12
phosphoenolpyruvate
pH 6.8, 60°C, cosubstrate D-arabinose 5-phosphate
1.4
phosphoenolpyruvate
pH 6.8, 60°C, cosubstrate D-erythrose 4-phosphate
1.65
phosphoenolpyruvate
-
isozyme NCgl2098 DAHP synthase, in 50 mM Tris-HCl buffer, pH 7.5, at 30°C
1.7
phosphoenolpyruvate
pH 6.8, 60°C, cosubstrate 2-deoxy-D-ribose 5-phosphate
2.5
phosphoenolpyruvate
pH 6.8, 60°C, cosubstrate D-ribose 5-phosphate
3
phosphoenolpyruvate
pH 6.8, 60°C, cosubstrate 2-deoxy-D-erythrose 4-phosphate
11.7
phosphoenolpyruvate
pH 7.3, temperature not specified in the publication, wild-type enzyme
14.1
phosphoenolpyruvate
pH 7.3, temperature not specified in the publication, mutant H29S/S31H
14.3
phosphoenolpyruvate
pH 7.3, temperature not specified in the publication, mutant H29A
17.5
phosphoenolpyruvate
pH 7.3, temperature not specified in the publication, mutant S31G
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
430
D-erythrose 4-phosphate
pH 7.3, temperature not specified in the publication, mutant S31G
500
D-erythrose 4-phosphate
pH 7.3, temperature not specified in the publication, mutant H29S/S31H
580
D-erythrose 4-phosphate
pH 7.3, temperature not specified in the publication, mutant H29A
900
D-erythrose 4-phosphate
pH 7.3, temperature not specified in the publication, wild-type enzyme
84
phosphoenolpyruvate
results within factor two of this otherwise published value, 30°C, 50 mM BTP (1,3-bis[tris(hydroxymethyl)methylamino]propane), pH 7.5 with 100 microM MnCl2, 240 microM D-erythrose-4-phosphate (saturating), less than 10 microM phosphoenolpyruvate, no influence of chorismate mutase concentration on activity
360
phosphoenolpyruvate
pH 7.3, temperature not specified in the publication, mutant H29S/S31H
700
phosphoenolpyruvate
pH 7.3, temperature not specified in the publication, mutant H29A
1400
phosphoenolpyruvate
pH 7.3, temperature not specified in the publication, mutant S31G
2400
phosphoenolpyruvate
pH 7.3, temperature not specified in the publication, wild-type enzyme
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.049
(2R)-2-(phosphonooxy)propanoic acid
-
buffer bis-tris-propane, 50 mM, pH 6.8, Mn2+, UV-visible spectroscopy at 232 nm, substrates phosphoenolpyruvate and D-erythrose 4-phosphate
0.67
(2S)-2-(phosphonooxy)propanoic acid
-
buffer bis-tris-propane, 50 mM, pH 6.8, Mn2+, UV-visible spectroscopy at 232 nm, substrates phosphoenolpyruvate and D-erythrose 4-phosphate
0.0088
(2Z)-3-phosphono-2-(trifluoromethyl)prop-2-enoic acid
-
buffer bis-tris-propane, 50 mM, pH 6.8, Mn2+, UV-visible spectroscopy at 232 nm, substrates phosphoenolpyruvate and D-erythrose 4-phosphate
0.0047
(E)-2-methyl-3-phosphonoacrylic acid
-
buffer bis-tris-propane, 50 mM, pH 6.8, Mn2+, UV-visible spectroscopy at 232 nm, substrates phosphoenolpyruvate and D-erythrose 4-phosphate
0.27
2-(phosphonomethyl)prop-2-enoic acid
-
buffer bis-tris-propane, 50 mM, pH 6.8, Mn2+, UV-visible spectroscopy at 232 nm, substrates phosphoenolpyruvate and D-erythrose 4-phosphate
0.035
fosmidomycin
-
buffer bis-tris-propane, 50 mM, pH 6.8, Mn2+, UV-visible spectroscopy at 232 nm, substrates phosphoenolpyruvate and D-erythrose 4-phosphate
0.27
3-deoxy-D-erythro-hept-2-ulosonate 7-phosphate
-
pH 7.5, 30°C, cosubstrate phosphoenolpyruvate
1.5
3-deoxy-D-erythro-hept-2-ulosonate 7-phosphate
-
pH 7.5, 30°C, cosubstrate erythrose 4-phosphate
1.35
chorismate
-
synthase-trp isozyme, versus phosphoenolpyruvate, 37°C, pH 7.0
2.25
chorismate
-
synthase-trp isozyme, versus D-erythrose 4-phosphate, 37°C, pH 7.0
1.35
phenylpyruvate
-
synthase-tyr isozyme, versus D-erythrose 4-phosphate, 37°C, pH 7.0
2.55
phenylpyruvate
-
synthase-tyr isozyme, versus phosphoenolpyruvate, 37°C, pH 7.0
22
phosphate
-
slope, tryptophan-sensitive isozyme, versus phosphoenolpyruvate, pH 7.4, 37°C
25
phosphate
-
slope, tryptophan-sensitive isozyme, versus D-erythrose 4-phosphate, pH 7.4, 37°C
54
phosphate
-
intercept, tryptophan-sensitive isozyme, versus phosphoenolpyruvate, pH 7.4, 37°C
0.005
Trp
-
synthase-trp isozyme, versus D-erythrose 4-phosphate, 37°C, pH 7.0
0.04
Trp
-
synthase-trp isozyme, versus phosphoenolpyruvate, 37°C, pH 7.0
0.023
Tyr
-
synthase-tyr isozyme, versus D-erythrose 4-phosphate, 37°C, pH 7.0
0.023
Tyr
-
synthase-tyr isozyme, versus phosphoenolpyruvate, 37°C, pH 7.0
additional information
additional information
-
product inhibition pattern
-
additional information
additional information
inhibition kinetics of wld-type and mutant enzymes, overview
-
additional information
additional information
-
inhibition kinetics of wld-type and mutant enzymes, overview
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.054
3-pyridine carboxyaldehyde
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.021
alpha-tocopherol
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.042
rutin
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.0066
tetraammonium (((carboxymethyl)[(2S,3R,4S)-2,3,4-trihydroxy-5-(phosphonatooxy)pentyl]amino)methyl)phosphonate
Escherichia coli
-
IC50: 0.0066 mM
0.0036
[(1E)-7-bromo-2-carboxyhept-1-en-1-yl]phosphonate
Escherichia coli
-
pH not specified in the publication, temperature not specified in the publication
0.0053
[2-carboxy-7-(phosphonatooxy)hept-1-en-1-yl]phosphonate
Escherichia coli
-
pH not specified in the publication, temperature not specified in the publication
0.154
[2-carboxy-7-(phosphonatooxy)hept-2-en-1-yl]phosphonate
Escherichia coli
-
pH not specified in the publication, temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.81
additional information
additional information
-
mutants, influence of aromatic amino acids on activity
additional information
-
mutants, influence of aromatic amino acids on activity
additional information
metal ions are removed form the buffer solution via Chelex 100
additional information
-
metal ions are removed form the buffer solution via Chelex 100
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.4
6.8