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Information on EC 2.5.1.54 - 3-deoxy-7-phosphoheptulonate synthase
for references in articles please use BRENDA:EC2.5.1.54
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EC Tree 2 Transferases
2.5 Transferring alkyl or aryl groups, other than methyl groups
2.5.1 Transferring alkyl or aryl groups, other than methyl groups (only sub-subclass identified to date)
2.5.1.54 3-deoxy-7-phosphoheptulonate synthase
The enzyme appears in viruses and cellular organisms
- 2.5.1.54
- shikimate
- chorismate
- mutase
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4.1.2.15
- prephenate
- l-phenylalanine
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feedback-resistant
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feedback-insensitive
- l-tyrosine
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phenylalanine-sensitive
- kdo8ps
- 8-phosphate
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tyrosine-sensitive
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tryptophan-sensitive
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feedback-inhibited
- 3-deoxy-d-manno-octulosonate
- 3-dehydroshikimate
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arogfbr
- l-tyr
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3-deoxy-d-manno-octulosonate-8-phosphate
- arogenate
- synthesis
- agriculture
- biotechnology
Reaction Schemes
showSynonyms
dahp synthase, dahps, dah7ps, 3-deoxy-d-arabino-heptulosonate-7-phosphate synthase, ds-co, ds-mn, dah7p synthase, dahp synthase-phe, dah7p, 3-deoxy-d-arabinoheptulosonate 7-phosphate synthase, 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
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
sequential mechanism
-
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
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
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
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
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
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
ordered sequential mechanism
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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
3-dehydroquinate biosynthesis I
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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
LITERATURE
COMMENTARY
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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Substrates: enzyme does not discriminate between (E) and (Z)-form of phosphoenol-3-fluoropyruvate
Products: -
Products: -
?
phosphoenolpyruvate + (3S)-2-deoxyerythrose 4-phosphate + H2O
(5S)-[5H]-3,5-dideoxy-D-arabinoheptulosonate 7-phosphate + phosphate
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Substrates: -
Products: -
Products: -
ir
phosphoenolpyruvate + 2-deoxy-D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + 2-deoxy-D-ribose 5-phosphate
3,5-dideoxy-D-gluco-octulosonate 8-phosphate + 3,5-dideoxy-D-manno-octulosonate 8-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
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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Substrates: D-lyxose or L-lyxose, at 1.8% of the activity with D-erythrose 4-phosphate
Products: -
Products: -
?
phosphoenolpyruvate + D-arabinose
2-dehydro-3-deoxy-D-gluco-octonate + phosphate
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Substrates: at 0.7% of the activity with D-erythrose 4-phosphate
Products: -
Products: -
?
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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Substrates: at 93% of the activity with D-erythrose 4-phosphate
Products: -
Products: -
?
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
?
-
Substrates: same activity as with D-erythrose 4-phosphate
Products: -
Products: -
?
phosphoenolpyruvate + D-glyceraldehyde
2-dehydro-3-deoxy-D-threo-hexonate + phosphate
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Substrates: at 176% of the activity with D-erythrose 4-phosphate
Products: -
Products: -
?
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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Substrates: at 12% of the activity with D-erythrose 4-phosphate
Products: -
Products: -
?
phosphoenolpyruvate + D-threose
2-dehydro-3-deoxy-D-xylo-heptonate + phosphate
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Substrates: at 92% of the activity with D-erythrose 4-phosphate
Products: -
Products: -
?
phosphoenolpyruvate + D-xylose
2-dehydro-3-deoxy-D-ido-octonate + phosphate
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Substrates: at 1% of the activity with D-erythrose 4-phosphate
Products: -
Products: -
?
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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Substrates: at 245% of the activity with D-erythrose 4-phosphate
Products: -
Products: -
?
phosphoenolpyruvate + glyoxylate
S-4-hydroxy-2-oxo-1,5-pentanedioate + R-4-hydroxy-2-oxo-1,5-pentanedioate + phosphate
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Substrates: at 205% of the activity with D-erythrose 4-phosphate
Products: -
Products: -
?
phosphoenolpyruvate + L-erythrose
2-dehydro-3-deoxy-L-arabino-heptonate + phosphate
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Substrates: at 70% of the activity with D-erythrose 4-phosphate
Products: -
Products: -
?
phosphoenolpyruvate + L-glyceraldehyde
2-dehydro-3-deoxy-L-threo-hexonate + phosphate
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Substrates: at 212% of the activity with D-erythrose 4-phosphate
Products: -
Products: -
?
phosphoenolpyruvate + L-threose
2-dehydro-3-deoxy-L-xylo-heptonate + phosphate
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Substrates: at 52% of the activity with D-erythrose 4-phosphate
Products: -
Products: -
?
phosphoenolpyruvate + L-xylose
2-dehydro-3-deoxy-L-ido-octonate + phosphate
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Substrates: at 1% of the activity with D-erythrose 4-phosphate
Products: -
Products: -
?
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
-
Substrates: -
Products: -
Products: -
?
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
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-arabinose 5-phosphate
3-deoxy-D-manno-octulosonate 8-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-arabinose 5-phosphate
3-deoxy-D-manno-octulosonate 8-phosphate + phosphate
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-arabinose 5-phosphate
3-deoxy-D-manno-octulosonate 8-phosphate + phosphate
-
Substrates: at 8% of the activity with D-erythrose 4-phosphate
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: first enzyme of the aromatic amino acid biosynthesis
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: key regulatory enzyme in L-Phe and L-Tyr biosynthesis
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: first enzyme in the shikimic pathway leading to biosynthesis of aromatic amino acids
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: regulatory role of thioredoxin of photosystem I on the chloroplastic enzyme
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: 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
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: first enzyme of aromatic amino acids, folic acid and phenazine 1-carboxylic acid biosynthesis pathways
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: first enzyme of aromatic amino acids, folic acid and phenazine 1-carboxylic acid biosynthesis pathways
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: effect of external factors on regulation
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: one of the key regulator enzymes of the shikimic acid pathway
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: no repression by the aromatic amino acids
Products: -
Products: -
?
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
-
Substrates: -
Products: -
Products: -
?
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
-
Substrates: no repression by the aromatic amino acids
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: first enzyme of the aromatic amino acid biosynthesis
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
ir
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
637413, 639746, 639747, 639748, 639749, 639750, 639753, 639767, 639768, 639771, 639775, 639776, 639777, 639783, 639792
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
Substrates: binds 1 molecule D-erythrose 4-phosphate per subunit
Products: -
Products: -
ir
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
Substrates: first enzyme in the shikimic pathway leading to biosynthesis of aromatic amino acids
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: first enzyme of the aromatic amino acid biosynthesis
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
ir
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
Escherichia coli NST 37 / ATCC 31882
-
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
Escherichia coli W3110 / ATCC 27325
-
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: first enzyme of the aromatic amino acid biosynthesis
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: first enzyme of the aromatic amino acid biosynthesis
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: in solution D-erythrose 4-phosphate forms dimers that are in slow equilibrium with monomers
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: the plastidic enzyme form is induced by fungal elicitor of Phytophthora megasperma, the cytosolic enzyme form is not induced
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
r
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: first enzyme of the aromatic amino acid biosynthesis
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: enzyme is induced by N-[phosphomonomethyl]glycine
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: first enzyme of the aromatic amino acid biosynthesis
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
ir
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
-
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
Substrates: phosphoenolpyruvate binding structure analysis
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
Substrates: phosphoenolpyruvate interacts with conserved residues Arg167, Arg236, Lys188, Arg94, and Lys99, condensation reaction
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
Substrates: phosphoenolpyruvate interacts with conserved residues Arg167, Arg236, Lys188, Arg94, and Lys99, condensation reaction
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
A0A482F152
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-erythro-hept-2-ulosonate 7-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-erythro-hept-2-ulosonate 7-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-fructose 6-phosphate
?
-
Substrates: same activity as with D-erythrose 4-phosphate
Products: -
Products: -
?
phosphoenolpyruvate + D-fructose 6-phosphate
?
-
Substrates: same activity as with D-erythrose 4-phosphate
Products: -
Products: -
?
phosphoenolpyruvate + D-glucose 6-phosphate
?
-
Substrates: as effective as D-erythrose 4-phosphate
Products: -
Products: -
?
phosphoenolpyruvate + D-glucose 6-phosphate
?
-
Substrates: as effective as D-erythrose 4-phosphate
Products: -
Products: -
?
phosphoenolpyruvate + D-glucose 6-phosphate
?
-
Substrates: at 0.5% of the activity with D-erythrose 4-phosphate
Products: -
Products: -
?
phosphoenolpyruvate + D-ribose 5-phosphate
3-deoxy-D-altro-octulosonate 8-phosphate + phosphate
-
Substrates: as effective as D-erythrose 4-phosphate
Products: -
Products: -
?
phosphoenolpyruvate + D-ribose 5-phosphate
3-deoxy-D-altro-octulosonate 8-phosphate + phosphate
-
Substrates: as effective as D-erythrose 4-phosphate
Products: -
Products: -
?
phosphoenolpyruvate + D-ribose 5-phosphate
3-deoxy-D-altro-octulosonate 8-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-ribose 5-phosphate + H2O
3-deoxy-D-altro-octulosonate 8-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-ribose 5-phosphate + H2O
3-deoxy-D-altro-octulosonate 8-phosphate + phosphate
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-xylulose 5-phosphate
?
-
Substrates: at 67% of the activity with D-erythrose 4-phosphate
Products: -
Products: -
?
phosphoenolpyruvate + D-xylulose 5-phosphate
?
-
Substrates: at 67% of the activity with D-erythrose 4-phosphate
Products: -
Products: -
?
phosphoenolpyruvate + DL-glyceraldehyde 3-phosphate
pyruvate + phosphate
-
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + DL-glyceraldehyde 3-phosphate
pyruvate + phosphate
-
Substrates: at 142% of the activity with D-erythrose 4-phosphate
Products: -
Products: -
?
phosphoenolpyruvate + erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with D-erythrose, D-glyceraldehyde 3-phosphate, ribose 5-phosphate, glucose 6-phosphate, glucosamine 6-phosphate, N-acetylglucosamine 6-phosphate, and pyruvate
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrates are: D-glucose 6-phosphate, D-arabinose, DL-glyceraldehyde, D-erythrose, glycoaldehyde, DL-glyceraldehyde 3-phosphate
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: reaction involves interaction of si face of phosphoenolpyruvate with re face of eryxthrose 4-phosphate
Products: -
Products: -
?
additional information
?
-
Substrates: no substrate: D-glyceraldehyde 3-phosphate, D-glucose 6-phosphate
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrate: D-glyceraldehyde 3-phosphate, D-glucose 6-phosphate
Products: -
Products: -
?
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
LITERATURE
COMMENTARY
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
?
-
-
Substrates: 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
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: first enzyme of the aromatic amino acid biosynthesis
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: key regulatory enzyme in L-Phe and L-Tyr biosynthesis
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: first enzyme in the shikimic pathway leading to biosynthesis of aromatic amino acids
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: regulatory role of thioredoxin of photosystem I on the chloroplastic enzyme
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: 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
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: first enzyme of aromatic amino acids, folic acid and phenazine 1-carboxylic acid biosynthesis pathways
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: first enzyme of aromatic amino acids, folic acid and phenazine 1-carboxylic acid biosynthesis pathways
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: effect of external factors on regulation
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: one of the key regulator enzymes of the shikimic acid pathway
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: no repression by the aromatic amino acids
Products: -
Products: -
?
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
-
Substrates: no repression by the aromatic amino acids
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: first enzyme of the aromatic amino acid biosynthesis
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
Substrates: first enzyme in the shikimic pathway leading to biosynthesis of aromatic amino acids
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: first enzyme of the aromatic amino acid biosynthesis
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: first enzyme of the aromatic amino acid biosynthesis
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: first enzyme of the aromatic amino acid biosynthesis
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: the plastidic enzyme form is induced by fungal elicitor of Phytophthora megasperma, the cytosolic enzyme form is not induced
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: first enzyme of the aromatic amino acid biosynthesis
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: enzyme is induced by N-[phosphomonomethyl]glycine
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: first enzyme of the aromatic amino acid biosynthesis
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
-
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
Substrates: -
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ba2+
A0A482F152
presence of Ba2+ stimulates the activity by more than 300%
Ca2+
Cd2+
Co2+
Cu2+
Fe2+
Mg2+
Mn2+
Ni2+
Zn2+
additional information
Ca2+
A0A482F152
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+
required, Mn2+ coordinates the PEP carboxylate functionality and a water molecule
Mn2+
activates, best activating metal ion. The metal ion is coordinated by four protein ligands Cys63, His 270, Glu304, and Asp324
Mn2+
-
absolute requirement for divalent metal, 15% of the activation with Mg2+
Mn2+
A0A482F152
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
-
DAHP synthase-trp; competitive against phosphoenolpyruvate, noncompetitive against D-erythrose 4-phosphate
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
-
Phe-sensitive isozyme; feed-back inhibition, Phe-sensitive isozyme
Phe
-
Tyr-sensitive isozyme is less inhibited than the Phe-sensitive isozyme; competitive with respect to D-erythrose 4-phosphate and non-competitive to phosphoenolpyruvate
Phe
-
Phe-sensitive isozyme; competitive with respect to D-erythrose 4-phosphate and non-competitive to phosphoenolpyruvate
Phe
-
Phe-sensitive isozyme; no inhibition; 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; Trp-sensitive isozyme; non-competitive against phosphoenolpyruvate and competitive for D-erythrose 4-phosphate; strongly dependent on pH
Trp
-
Trp-sensitive isozyme; non-competitive against phosphoenolpyruvate and competitive for D-erythrose 4-phosphate
Trp
-
Trp-sensitive isozyme; allosteric, best at pH 6.0, no inhibition at pH 7.3
Trp
-
DAHP synthase-trp; Trp-sensitive isozyme; non-competitive against phosphoenolpyruvate and competitive for D-erythrose 4-phosphate
Tyr
-
Tyr-sensitive isozyme; feedback inhibition; noncompetitive with respect to D-erythrose 4-phosphate, competitive with respect to phosphoenolpyruvate; wild-type and mutant S187A
Tyr
-
0.04 mM, 50% inhibition of DAHP synthase-tyr; L-Tyr; Tyr-sensitive isozyme
Tyr
-
Tyr-sensitive isozyme; feedback inhibition; noncompetitive with respect to D-erythrose 4-phosphate, competitive with respect to phosphoenolpyruvate
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
-
Tyr-sensitive isozyme; noncompetitive with respect to D-erythrose 4-phosphate, competitive with respect to phosphoenolpyruvate
Tyr
-
Tyr-sensitive isozyme; noncompetitive with respect to D-erythrose 4-phosphate, competitive with respect to phosphoenolpyruvate
Tyr
-
Tyr-sensitive isozyme; strain 33/X strongly but not totally inhibited; strain H1, strain H20 and strain 3/2: cumulative inhibition of Tyr and Phe
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
Confusion
Bacillus subtilis 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase revisited: resolution of two long-standing enigmas.
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
7.2
7.3
7.4
7.5
8.6
8.8
additional information
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 8.5
-
pH 5.5: about 50% of maximal activity, pH 8.5: about 40% of maximal activity
5.7 - 8.5
-
pH 5.7: about 25% of maximal activity, pH 8.5: about 30% of maximal activity
6 - 7.6
-
pH 6.0: about 30% of maximal activity, pH 7.6: about 60% of maximal activity
6 - 8.5
-
pH 6.0: about 65% of maximal activity, pH 8.5: about 50% of maximal activity
6 - 9
6.2 - 7.9
-
pH 6.2: about 35% of maximal activity, pH 7.9: about 55% of maximal activity
6.5 - 9
-
pH 6.5: about 35% of maximal activity, pH 9.0: about 60% of maximal activity
6 - 9
pH 6.0: about 55% of maximal activity, pH 9.0: about 35% of maximal activity, mutant enzyme I181D
6 - 9
at pH 9.0 the activity is about 60% of the activity at pH 6.0, wid-type enzyme
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
37
40
47 - 49
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
wild type strain WV2 contains DS I, a leaky L-Phe-requiring auxotroph mutant strain GH141 grown under L-Phe limitation possesses additional DS II activity
-
-
brenda
bifunctional enzyme, catalyzes reactions of EC 2.5.1.54 and EC 5.4.99.5
UniProt
brenda
metagenomic library from subtropical marine mangrove sediment
A0A482F152
UniProt
brenda
bifunctional enzyme, catalyzes reactions of EC 2.5.1.54 and EC 5.4.99.5
UniProt
brenda
Marburg strain and strain 168, bifunctional enzyme with chorismate mutase activity in addition to enzymic activity
-
-
brenda
strain ATCC 11299a, two distinct regulatory isoenzymes: DAHP synthase-phe and DAHP synthase-tyr
-
-
brenda
phenylalanine-sensitive isozyme
-
-
brenda
recombinant protein, coexpression with Escherichia coli chaperonins GroEL and GroES in Escherichia coli
-
-
brenda
2 isoenzymes: tyrosine-sensitive DAHP synthase-tyr and tryptophane-sensitive DAHP synthase-trp
-
-
brenda
ARO3-encoded isozyme is a phenylalanine-sensitive isozyme
-
-
brenda
ARO4-encoded isozyme is a tyrosine-sensitive isozyme
-
-
brenda
operator-constitutive strain tyrO
-
-
brenda
tyrosine-sensitive isozyme
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
differential expression of the enzyme in various vegetative and reproductive organs
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
presence of amino-terminal extension characteristic of chloroplast transit peptides on DSH1 and DSH2 suggests that both proteins may be targeted to the chloroplast
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
additional information
evolution
despite significant sequence diversity, all known DAH7PS enzymes share a common (beta/alpha)8-barrel core and similar active site architectures formed by conserved residues that support a similar catalytic mechanism. On the basis of sequence and size, DAH7PS enzymes are classified into groups (type Ialpha, type Ibeta and type II). Each group features distinct structural elements appended to the core catalytic barrel that are associated with the allosteric inhibition of the enzymes and different quaternary structure associations. Neisseria meningitidis DAH7PS belongs to the type Ialpha group
evolution
DAHP synthase belongs to a family of mononuclear iron-containing enzymes that are disabled by oxidative stress
metabolism
initial step in the shikimate biosynthesis pathway, enhances the catalytic efficiency of chorismate mutase in a noncovalent enzyme complex
metabolism
shikimate biosynthetic pathway, noncovalent binding to chorismate mutase enhances the mutase activity more than 100fold, 4 enzyme molecules sandwiched between the chorismate mutase dimers reposition the active site of the mutases
metabolism
-
catalysis of first step of shipmate pathway to aromatic amino acids
metabolism
first enzyme of the shikimate pathway in the biosynthesis of aromatic compounds which is responsible for primary carbohydrate metabolism with the biosynthesis of most aromatic amino acids
metabolism
3-deoxy-D-arabino-heptulosonate 7-phosphate synthase catalyses the first committed step of the shikimate pathway, which involves the aldol-like condensation of D-erythrose 4-phosphate and phosphoenolpyruvate to form 3-deoxy-D-arabino-heptulosonate 7-phosphate
metabolism
the enzyme catalyzes the first step in shikimate pathway
metabolism
the enzyme catalyses the first step of the shikimate pathway for the biosynthesis of aromatic amino acids
metabolism
first committed enzyme in the aromatic biosynthetic pathway of Escherichia coli, shikimate biosynthesis pathway overview
metabolism
first enzyme of the shikimate pathway that link the primary and specialized metabolism derived from aromatic amino acids. Isozyme AroG expression influences the levels of number of primary metabolites, such as shikimic acid and aromatic amino acids, as well as multiple volatile and non-volatile phenylpropanoids specialized metabolites and carotenoids
metabolism
the enzyme catalyzes the first reaction in the shikimate pathway leading to the biosynthesis of aromatic metabolites including the aromatic acids L-Trp, L-Phe, and L-Tyr. As the entry point, feedback inhibition of DAH7PS by pathway end products is a key mechanism for the control of pathway flux
metabolism
the enzyme is involved in L-phenylalanine biosynthesis pathway
metabolism
-
shikimate biosynthetic pathway, noncovalent binding to chorismate mutase enhances the mutase activity more than 100fold, 4 enzyme molecules sandwiched between the chorismate mutase dimers reposition the active site of the mutases
-
metabolism
-
the enzyme catalyzes the first reaction in the shikimate pathway leading to the biosynthesis of aromatic metabolites including the aromatic acids L-Trp, L-Phe, and L-Tyr. As the entry point, feedback inhibition of DAH7PS by pathway end products is a key mechanism for the control of pathway flux
-
physiological function
expression of wild-type enzyme and phenylalanine-feedback insensitive mutant L175Q in Arabidopsis thaliana. Transgenic plants have comparable phenotypes and are fully fertile. The levels of shikimate, prephenate and Phe are higher in the different lines expressing the mutant enzyme than in the lines expressing the natural feedback-sensitive bacterial enzyme, and the control plants. Results imply that the bacterial enzyme is active in the transgenic plants and, similar to its operation in bacteria, the feedback insensitivity trait of the mutant enzyme is fundamental for enhancement of the flow of primary carbon metabolites via the shikimate pathway into the production of aromatic amino acids also in the plant
physiological function
the enzyme is involved in shikimate biosynthesis pathway
physiological function
3-deoxy-D-arabino-heptulosonate 7-phosphate synthase catalyses the aldol-like condensation of D-erythrose 4-phosphate and phosphoenolpyruvate to form 3-deoxy-D-arabino-heptulosonate 7-phosphate. Entry into the pathway is controlled by the allosteric regulation of enzyme DAH7PS by the pathway end products Phe, Tyr and Trp, or other intermediates of the pathway
physiological function
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
additional information
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. The nature of the extra barrel extensions is directly implicated in the sensitivity of the DAH7PS enzymes to allosteric control
additional information
-
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. The nature of the extra barrel extensions is directly implicated in the sensitivity of the DAH7PS enzymes to allosteric control
additional information
-
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. The nature of the extra barrel extensions is directly implicated in the sensitivity of the DAH7PS enzymes to allosteric control
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100000
110000
141000
homotetrameric wild-type enzyme, analytical ultracentrifugation
200000
-
tryptophan-sensitive isozyme, sedimentation equilibrium centrifugation
35000
39000
40000
42000
50000
-
2 * 50000, native isozyme NCgl2098 DAHP synthase, gel filtration
51830
53000
54000
59000
66000
69000
39000
-
x * 39000, either a rapid monomer-dimer equilibrium or a very asymetric shape for the native enzyme, SDS-PAGE
42000
-
2 * 42000, native isozyme NCgl0950 DAHP synthase, gel filtration
69000
homodimeric mutant R126S enzyme, analytical ultracentrifugation
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
homotetramer
pentamer
tetramer
additional information
?
x * 38009-38014, Phe-sensitive isozyme, electron mass spectroscopy and amino acid sequence determination
?
-
x * 39000, either a rapid monomer-dimer equilibrium or a very asymetric shape for the native enzyme, SDS-PAGE
dimer
although the enzyme crystallizes as a tetramer, equilibrium exists between tetrameric and dimeric forms with a dissociation constant of 0.022 mM
homodimer
-
2 * 42000, native isozyme NCgl0950 DAHP synthase, gel filtration
homodimer
-
2 * 50000, native isozyme NCgl2098 DAHP synthase, gel filtration
homotetramer
a dimer of tight dimers, crystal structure analysis
tetramer
at pH 7.5 and 20°C, the wild-type enzyme is present as a tetramer in solution. Although the enzyme crystallizes as a tetramer, equilibrium exists between tetrameric and dimeric forms with a dissociation constant of 0.022 mM
additional information
the enzyme forms a homotetrameric structure with an extensive and a less extensive interface, but the functional unit of the enzyme is dimeric. The tetrameric association enabled by this Arg126-Glu27 salt-bridge appears to contribute solely to the stability of the protein. Analysis of quarternary structure, PDB ID 4HSN, and SAXS data analysis
additional information
-
the enzyme forms a homotetrameric structure with an extensive and a less extensive interface, but the functional unit of the enzyme is dimeric. The tetrameric association enabled by this Arg126-Glu27 salt-bridge appears to contribute solely to the stability of the protein. Analysis of quarternary structure, PDB ID 4HSN, and SAXS data analysis
additional information
the monomer of Nme-DAH7PS is a (beta/alpha)8 TIM-barrel
additional information
-
the monomer of Nme-DAH7PS is a (beta/alpha)8 TIM-barrel
additional information
-
the monomer of Nme-DAH7PS is a (beta/alpha)8 TIM-barrel
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with a manganese ion and phosphoenolpyruvate. Crystals contain a tetramer in the asymmetric unit. A water molecule occupies the presumed binding site for the phosphate group of 4-erythrose 4-phosphate
modeling of the three dimensional structure of the type II enzyme present in Arabidopsis thaliana and comparison with type I DAHPS. The enzyme belongs to the (beta/alpha)8 TIM barrel family. At the N-terminus of the Arabidopsis thaliana enzyme, there are three non-core helices, alpha0a (Ala72-Lys83), alpha0b (Ala94-Ala106) and alpha0c (Ala113-Val128), but no beta0, in contrast to the microbial type II DAHPS. Also, the (I/L)GAR motif in the type I DAHPS is substituted with xGxR in the case of type II DAHPS. A motif NK(/I)PGR(/K) is present in the sequences of type II DAHPS including At-DAHPS
structure of N-terminal domain AroQ in complex with citrate and chlorogenic acid at 1.9 A and 1.8 A resolution, respectively. Helix H2' undergoes uncoiling at the first turn and increases the mobility of loop L1'. The side chains of Arg45, Phe46, Arg52 and Lys76 undergo conformational changes, which may play an important role in DAHPS regulation by the formation of the domain-domain interface. Chlorogenic acid binds with a higher affinity than chorismate
in complex with inhibitor 3-deoxy-D-arabinoheptulosonate-7-phosphate oxime
native and selenomethionine-substituted protein, in complex with phosphoenolpyruvate and Mn2+, mutant E24Q in complex with phosphoenolpyruvate and Mn2+
Phe-sensitive isozyme, enzyme-Mn2+-2-phosphoglycolate-complexes, hanging drop vapour diffusion method, room temperature, all solutions, except the MnSO4 and the enzyme solution, are treated with Chelex-100 to remove metals, 0.2 mM enzyme subunit solution: 0.37 MnSO4, 4.2 mM 2-phosphoglycolate, 0.1 M Li2SO4, 12% PEG 100 w/v, 20% ethanol v/v, 50 mM 1,3-bis[tris(hydroxy-methyl)methylamino]propane buffer, pH 8.7, reservoir solution: 19% PEG 1000, 0.1 M Li2SO4, 20% ethanol v/v, 50 mM 1,3-bis[tris(hydroxy-methyl)methylamino]propane buffer, X-ray diffraction structure determination and analysis
Phe-sensitive isozyme, hanging drop vapour diffusion method, 22°C, with or without inhibitor phenylalanine, at pH 6.3-9.4, 0.1-0.2 M monovalent cations, PEG 1000-4000, 0.01 ml protein solution + 0.3 ml precipitant solution, X-ray diffraction structure determination and analysis
-
structures of apo form and complex with the inhibitor tyrosine at 2.5 and 2.0 A resolutions, respectively. DAHPS(Tyr) has a typical (beta/alpha)8 TIM barrel, which is decorated with an N-terminal extension and an antiparallel beta sheet. Inhibitor tyrosine binds at a cavity formed by residues of helices alpha3, alpha4, strands beta6a, beta6b and the adjacent loops, and directly interacts with residues P148, Q152, S181, I213 and N8*. Conformational changes of residues P148, Q152 and I213 initiate a transmission pathway to propagate the allosteric signal from the tyrosine-binding site to the active site
structures in complex with Mn2+ and Mn+ and phosphoenolpyruvate, to 1.95 A resolution. The domains assemble as a tetramer, from either side of which chorismate mutase-like regulatory domains asymmetrically emerge to form a pair of dimers. Domain organization suggests that chorismate/prephenate binding promotes a stable interaction between the discrete regulatory and catalytic domains and supports a mechanism of allosteric inhibition similar to tyrosine/phenylalanine control of a related DAHPS class. The catalytic domain adopts a classic TIM barrel (alpha/beta)8 fold. The active site is located on the inside of the C-terminal end of the barrel and is formed by several alpha-beta-connecting loops and two beta-strands. In the holo structure, a manganese ion is present at the active site. In the phosphoenolpyruvate structure, the substrate is adjacent to the manganese ion in a similar position as has been observed in related enzymes
-
in complex with chorismate mutase, hanging-drop method, in 20 mM BTP, pH 7.5, 150 mM NaCl, 0.5 mM tris(2-carboxyethyl)phosphine hydrochloride, 0.2 mM phosphoenolpyruvate and 0.1 mM MnCl2, crystallization after 2 months with no ammonium sulfate and 0.1 M Tris-HCl, pH 7.9-8.0 and PEG 400 or glycerol
in complex with chorismate mutase, streak-seeding conditions in 20 mM BTP (1,3-bis[tris(hydroxymethyl)methylamino]propane), pH 7.5, 150 mM NaCl, 0.5 mM TCEP [tris(2-carboxyethyl)phosphine hydrochloride], 0.2 mM phosphoenolpyruvate, crystallization by 0.9 M ammonium sulfate, 100 mM Tris, pH 7.9 to 8.0, and 1 to 5% PEG 400
recombinant protein, after coexpression with Escherichia coli chaperonins GroEL and GroES in Escherichia coli, crystallized as native and selenomethionine-substituted proten
-
purified enzyme mutant S213G with phosphoenolpyruvate and Mn2+, hanging drop vapor diffusion, mixing of 0.001 ml of 11 mg/mL in 10 mM BTP buffer, pH 7.3, in a 1:1 v/v with a reservoir solution containing 0.2 M trimethylamine N-oxide, 0.1 M Tris, pH 8.5, 15-20% w/v PEG 2000 MME, 0.4 mM MnSO4, and 0.4 mM phosphoenolpyruvate, equilibration against 0.5 ml of reservoir solution, 20°C, 3 days, X-ray diffractin structure determination and analysis at 2.0-2.1 A resolution
purified recombinant enzyme complexed with inhibitors (S)-phospholactate, (R)-phospholactate, and vinyl phosphonate, hanging drop vapour diffusion method, mixing of 0.001 ml of 10 mg/mL protein in 10 mM bis(tris(hydroxymethyl)methylamino)propane, pH 7.3, and 5 mM inhibitor, with 0.001 ml of crystallisation buffer containing 0.1 Tris HCl, pH 7.3, 0.2 M trimethyl-amino-N-oxide, 0.4 mM MnSO4, and 15-20% w/v PEG 2000MME, equilibration over 0.5 ml of reservoir solution, 20°C, 3 days, X-ray diffraction structure determination and analysis at 1.76-2.34 A resolution
purified recombinant enzyme mutant R126S, hanging drop vapour diffusion method, mixing of 0.001 ml of 10 mg/mL protein solution with 0.001 ml of crystallisation buffer containing 0.1 Tris HCl, pH 7.3, 0.2 M trimethyl-amino-N-oxide, 0.6 mM MnSO4, and 15-20% w/v PEG 2000MME, equilibration over 0.5 ml of reservoir solution, 20°C, 7 days, X-ray diffraction structure determination and analysis at 2.0 A resolution
structure of type II DAH7PS, encoded by phzC as part of the duplicated phenazine biosynthetic cluster, to 2.7 A resolution, space group C2221 with two DAH7PS chains present in the asymmetric unit
hanging-drop vapor diffusion, ctystal structure of wild-type enzyme and mutant enzyme I181D
Tyr-sensitive isozyme, hanging drop vapour diffusion method, protein solution in 1:1 mixture with precipitant, 0.004 ml, + 1 ml precipitant solution: 1. 50 mM KH2PO4, 20% polyethylene glycol 8000 w/v or 2. 0.1 M Tris, pH 9.0, 10 mM NiCl2, 20% polyethylene glycol monomethylester 2000 w/v, room temperature for 3 days, X-ray diffraction structure analysis, usage of cryoprotectant glycerol for investigations
-
crystals grown in presence of phosphoenolpyruvate and Cd2+, soaked with erythrose 4-phosphate
-
molecular modeling of structure. The monomeric structure of Aro1A is a (beta/alpha)8 barrel structure. Phosphoenolpyruvate combines with residues R60, Q116, S119, K141, and R171 through eight hydrogen bonds. D-erythrose 4-phosphate combines with residues R60, K65, Q116, S119, K141, and R171 through nine hydrogen bonds
A0A482F152
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C145S
-
site-directed mutagenesis, 16% remaining activity compared to the wild-type, 4.6fold increased Km, 1.6fold decreased kcat, and 13.6fold decreased kcat/Km for phosphoenolpyruvate
C67L
-
site-directed mutagenesis, highly reduced activity, insensitive to inhibition by divalent metal ions
S187C
-
site-directed mutagenesis, reduced activity, activation by tyrosine and phenylalanine instead of inhibition like the wild-type
S187F
-
site-directed mutagenesis, highly reduced activity, activation by tyrosine and phenylalanine instead of inhibition like the wild-type
S187Y
-
site-directed mutagenesis, highly reduced activity, activation by tyrosine and phenylalanine instead of inhibition like the wild-type
C328V
-
oligo-nucleotide mutagenesis, expression in Escherichia coli strains, 20% reduction in the catalytic constant, 2-3fold increase in Km for the substrates, completely resistant to both spontaneous and Cu2+-catalysed inactivation
C61G
-
site-directed mutagenesis, highly reduced activity, highly increased Km for phosphoenolpyruvate, higher pH-optimum than the wild-type
C61V
-
oligo-nucleotide mutagenesis, expression in Escherichia coli strains, inactive, does not bind metal ions, resistant to metal attack, no subunit dissociation upon Cu2+ treatment
DELTA1-15
-
N-terminal deletion of amino acids 1-15, no formation of dimeric form
H207G
-
site-directed mutagenesis, reduced activity, increased Km values for the substrates, reduced kcat
H304G
-
site-directed mutagenesis, reduced activity, increased Km values for the substrates, increased kcat
H64G
-
site-directed mutagenesis, reduced activity, increased Km values for the substrates, increased kcat
H64L
-
oligo-nucleotide mutagenesis, expression in Escherichia coli strains, unstable to treatment with phosphoenolpyruvate, half-life of about 24 h at 0.4 mM compared to 6 days for the wild-type
I10A
I213P
overexpression of variant leads to less decrease in the accumulation of phenylalanine than overexpression of wild-type
L175Q
N5K
N8A
overexpression of variant leads to less decrease in the accumulation of phenylalanine than overexpression of wild-type
N8K
-
similar activity and substrate affinities like the wild-type, but insensitive against inhibition by tyrosine, decreased thermostability
P148A
overexpression of variant leads to less decrease in the accumulation of phenylalanine than overexpression of wild-type
Q152A
overexpression of variant leads to higher accumulation of phenylalanine
S181A
overexpression of variant leads to higher accumulation of phenylalanine
I213P
-
overexpression of variant leads to less decrease in the accumulation of phenylalanine than overexpression of wild-type
-
N8A
-
overexpression of variant leads to less decrease in the accumulation of phenylalanine than overexpression of wild-type
-
P148A
-
overexpression of variant leads to less decrease in the accumulation of phenylalanine than overexpression of wild-type
-
Q152A
-
overexpression of variant leads to higher accumulation of phenylalanine
-
S181A
-
overexpression of variant leads to higher accumulation of phenylalanine
-
N8K
Escherichia coli W3110 / ATCC 27325
-
similar activity and substrate affinities like the wild-type, but insensitive against inhibition by tyrosine, decreased thermostability
-
R126S
site-directed mutagenesis, mutation of the residue involved in the salt bridge formation of Arg126-Glu27 results in perturbation of the less extensive interface in the enzyme tetramer and formation of enzyme dimers in solution. The dimeric NmeDAH7PSR126S variant exhibits a slight reduction in thermal stability by differential scanning calorimetry experiments and a slow loss of activity over time compared to the wild-type enzyme. Although NmeDAH7PSR126S crystallised as a tetramer, like the wild-type enzyme, structural asymmetry at the less extensive interface was observed consistent with its destabilisation
S213G
I181D
mutant enzyme is catalytically more active than the wild type enzyme from 20 to 80°C, the mutation disrupts the tetrameric structure of the enzyme, the melting temperatures of the wild-type protein are significantly higher than the melting temperatures of mutant enzyme I181D at pH values greater than 6.5
H29A
site-directed mutagenesis, the mutant is inhibited by both L-Tyr and L-Phe
H29S/S31H
site-directed mutagenesis, the mutant is inhibited to a greater extent by L-Phe than L-Tyr
S31G
site-directed mutagenesis, the mutation severely reduces inhibition by L-Tyr
additional information
I10A
-
kinetic parameter similar to wild-type, part of enzyme is monomer instead of dimer
S213G
site-directed mutagenesis, a single Ser residue at the bottom of the inhibitor-binding cavity is substituted to Gly, which alters inhibitor specificity from L-Phe to L-Tyr
S213G
-
site-directed mutagenesis, a single Ser residue at the bottom of the inhibitor-binding cavity is substituted to Gly, which alters inhibitor specificity from L-Phe to L-Tyr
-
additional information
random mutagenesis, the AroF variant with a deficiency in residue Ile11 is insensitive to L-tyrosine. Construction of feedback-resistant 3-deoxy-D-arabino-heptulosonate-7-phosphate synthases by engineering the N-terminal domain for L-phenylalanine synthesis, generation of nine AroF variants with truncation of different N-terminal fragments, the variants AroFD(1-9), AroFD(1-10), AroFD(1-12) and, in particular, AroFD(1-11) significantly lead to the accumulation of L-phenylalanine, overview. Mutant AroFDELTA(1-11) does not show any feedback inhibition by L-Phe, demonstrated in a strain that has a high L-Phe level through coexpression of L-Phe producing chorismate mutase-4-prephenate dehydratase
additional information
-
random mutagenesis, the AroF variant with a deficiency in residue Ile11 is insensitive to L-tyrosine. Construction of feedback-resistant 3-deoxy-D-arabino-heptulosonate-7-phosphate synthases by engineering the N-terminal domain for L-phenylalanine synthesis, generation of nine AroF variants with truncation of different N-terminal fragments, the variants AroFD(1-9), AroFD(1-10), AroFD(1-12) and, in particular, AroFD(1-11) significantly lead to the accumulation of L-phenylalanine, overview. Mutant AroFDELTA(1-11) does not show any feedback inhibition by L-Phe, demonstrated in a strain that has a high L-Phe level through coexpression of L-Phe producing chorismate mutase-4-prephenate dehydratase
-
additional information
-
deletion mutant of Tr-sensitive isozyme, gene aroF, lacking the first 7 amino acid residues of the N-terminus, mutant is insensitive against inhibition by tyrosine
additional information
-
N-terminal deletion mutant, no inhibition by phenylalanine
additional information
-
KDPGal aldolase mutant EC03-1 (F33I/D58N/Q72H/A75V/V85A/V154F) develops increased DAHP synthase activity
additional information
recombinant expression of aroG in transgenic Solanum lycopersicum cv. 82 fruits results in ripe AroG-expressing tomato fruits that have a preferred floral aroma compare with fruits of the wild-type line. Plants expressing the bacterial gene exhibit enhanced levels of a number of aromatic specialized metabolites in a manner that is specific to the bacterial enzyme. Metabolic profiling of transgenic tomato plants expressing a bacterial feedback-insensitive AroG gene, overview
additional information
Escherichia coli W3110 / ATCC 27325
-
deletion mutant of Tr-sensitive isozyme, gene aroF, lacking the first 7 amino acid residues of the N-terminus, mutant is insensitive against inhibition by tyrosine
-
additional information
overexpression of 3-deoxy-7-phosphoheptulonate synthase gene from Gossypium hirsutum enhances Arabidopsis resistance to infection by Verticillium dahliae and Verticillium wilt. GhDHS1 overexpression is associated with longer primary roots for Arabidopsis plants. GhDHS1 overexpression increases xylem lignification of Arabidopsis plants in response to Verticillium dahliae infection
additional information
-
overexpression of 3-deoxy-7-phosphoheptulonate synthase gene from Gossypium hirsutum enhances Arabidopsis resistance to infection by Verticillium dahliae and Verticillium wilt. GhDHS1 overexpression is associated with longer primary roots for Arabidopsis plants. GhDHS1 overexpression increases xylem lignification of Arabidopsis plants in response to Verticillium dahliae infection
additional information
-
loss of 81 N-terminal amino acid resiudes leads to more flexibility in global terms of structure and a higher degree of compaction. A strain carrying the mutant shows an increased 2-phenylethanol production
additional information
Kluyveromyces marxianus CCT 7735
-
loss of 81 N-terminal amino acid resiudes leads to more flexibility in global terms of structure and a higher degree of compaction. A strain carrying the mutant shows an increased 2-phenylethanol production
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
-
half-life: 1.2 days in absence of phosphoenolpyruvate, half-life: 4 days in presence of 1 mM phosphoenolpyruvate
25
37
50
60
70
95
-
presence of 0.1 mM Mn2+, 130 min, 50% residual activity, absence of Mn2+, 3 min, 50% residual activity
98
melting temperature of the wild-type enzyme by differential scanning calorimetry at a protein monomer concentration of 0.034 mM and a pH of 7.5
additional information
25
-
2 h, in 3(N-morpholono)propane-sulfonic acid buffer, 50% loss of activity
25
-
1 h, in 1,3-bis[tris(hydroxymethyl)methylamino]propane buffer, 10% loss of activity
37
-
Tyr-sensitive isozyme, wild-type: 50% loss of activity in 80 min in presence of phosphoenolpyruvate, mutant N8K: 50% loss of activity in 20 min in presence of phosphoenolpyruvate
37
-
isoenzyme Ds-Co, 95% loss of activity in absence of phosphoenolpyruvate, 1.1 mM phosphoenolpyruvate almost completely protects from inactivation
additional information
-
phosphoenolpyruvate protects against inactivation
additional information
-
phosphoenolpyruvate protects against inactivation
additional information
-
D-erythrose 4-phosphate, erythrose and ribose 5-phosphate increase rate of inactivation
additional information
-
phosphoenolpyruvate, D-erythrose 4-phosphate and inorganic phosphate protect the purified enzyme against heat denaturation
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
DTT stabilizes the active protein, no influence on the alkylated enzyme
-
metal-catalysed oxidation of the enzyme, the apoenzyme shows an exponentially decrease in activity with a half-life of about 1 day at 22°C, Cu2+ and Fe2+ accelerated the rate of inactivation and subunit dissociation, phosphoenolpyruvate and EDTA stabilize, mutants are insensitive
-
overnight dialysis against buffer containing 10 mM EDTA at 4°C results in 85% inactivation
-
spontaneous inactivation with a net loss of two of the seven thiol groups per subunit is restored by dithiothreitol
-
unstable during manipulations such as dialysis, dilution, ammonium sulfate fractionation, chromatography on DEAE-cellulose or Sephadex G-200
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15°C, ammonium sulfate and acetone fractions, stable for at least several weeks
-
-20°C, 0.1 M potassium phosphate, pH 6.5, 1 mM phosphoenolpyruvate, stable for at least 6 months
-
-20°C, in phosphate buffer containing phosphoenolpyruvate, stable for several months
-
0.1 M potassium phosphate, pH 7.4, 1 mM phosphoenolpyruvate, 0.02% NaN3, purified enzyme, stable for 2-3 months
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
2350fold purification of the tryptophan sensitive isozyme, partial purification of the tyrosine- and phenylalanine-sensitive isozyme
-
cells centrifuged and resuspended in 20 mM BTP (1,3-bis[tris(hydroxymethyl)methylamino]propane), pH 7.5, 150 mM NaCl, 0.5 mM TCEP (tris(2-carboxyethyl)phosphine hydrochloride), 0.2 mM phosphoenolpyruvate and 0.1 mM MnCl2, cell lysis with lysozyme and sonication, centrifugation, crude extract subjected to Ni-NTA agarose chromatography, elution with 250 mM imidazole in buffer, further purification by preparative FPLC HiLoad 26/60 Superdex 75 gel-filtration column
Ni-NTA affinity chromatography followed by gel filtration, in 20 mM BTP (1,3-bis[tris(hydroxymethyl)methylamino]propane), pH 7.5, 150 mM NaCl, 0.5 mM TCEP [tris(2-carboxyethyl)phosphine hydrochloride], 0.2 mM phosphoenolpyruvate, and 0.1 mM MnCl2, ultrafiltration for concentration of enzyme
partial
Phe-sensitive isozyme, 11fold to homogeneity from overproducing strain
-
Phe-sensitive isozyme, recombinant wild-type from overexpressing strain and recombinant mutants
-
recombinant from Escherichia coli, mature chloroplastic form, purified to homogeneity
-
recombinant His-tagged wild-type and mutants from Escherichia coli
-
recombinant His10-tagged enzyme from Escherichia coli strain BL21 by affinity chromatography, followed by tag cleavage with factor Xa and again affinity chromatography and dialysis to remove the tag
recombinant mutant enzyme R126S from Escherichia coli strain BL21 StarTM (DE3)
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3) by anion exchange chromatography, ultrafiltration, and gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
2 clones M1 and M2, expression in Escherichia coli strain BL21(DE3) and strain AB3248, which is defective in all endogenous isozyme forms, functional complementation of the mutant
-
ARO3 gene, expression in deficient strain and in Escherichia coli strain JA196
-
ARO4 gene, tyrosine-sensitive isozyme, overexpression from plasmid in strain RH1326
-
DHS1 and DHS2, complementation of Saccharomyces cerevisiae mutant strain YBK7
-
expressed in Escherichia coli
expressed in soluble form by co-expression with chaperonins GroEL/GroES in Escherichia coli
expression in Escherichia coli
expression of enzyme with affinity purification tagwith plasmid pKTDS-HN in Escherichia coli KA13
expression of mature chloroplastic form, without signal sequence, in Escherichia coli
-
gene aroF, cloning of mutant enzymes in Escherichia coli strain JM109, recombinant overexpression of mutant enzyme variants AroFD(1-9), AroFD(1-10), AroFD(1-12) and AroFD(1-11)
gene aroF, Tyr-sensitive isozyme, expression of wild-type and mutants in strain AB3257
-
gene aroG, Phe-sensitive isozyme, overexpression in strain gene aroH, Trp-sensitive isozyme, overexpression in deficient strain AB3248
-
gene aroG, recombinant expression of a truncated coding DNA sequence of aroG in transgenic Solanum lycopersicum cv. 82 fruits under control of a fruit ripening-specific promoter, E8. Metabolic profiling of transgenic tomato plants expressing a bacterial feedback-insensitive AroG gene, overview
gene aroG, recombinant expression of His10-tagged enzyme in Escherichia coli strain BL21, subcloning in Escherichia coli strain DH5alpha
gene aroG, recombinant expression of mutant enzyme R126S in Escherichia coli strain BL21 StarTM (DE3)
gene aroG, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain (DE3) Star
gene aroG, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3)
gene GhDHS1, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, overexpressionin transgenic Arabidopsis thaliana plants via Agrobacterium tumefaciens-mediated transformation
gene Os07g0622200, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, recombinant functional expression in Escherichia coli aroH mutant strain ME8637 and complementating it
N-terminally histidine-tagged enzyme is expressed in Escherichia coli KA13
overexpression of His-tagged wild-type and mutants in Escherichia coli
-
Phe-sensitive isozyme, wild-type and mutants, expression in Escherichia coli strain BL21(DE3)
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme damage by reactive oxidants, H2O2 and superoxide, induces the enzyme expression in Escherichia coli, which attempts to compensate for diminished DAHP synthase activity by increasing expression
expression of gene DHS1 in cotton is induced upon infection by Verticillium dahliae strain Linxi2-1. DHS1 expression is more significantly upregulated in the roots of resistant Gossypium barbadense cv. Pima90-53 and Gossypium hirsutum cv. Jimian20 than in the susceptible Gossypium hirsutum cv. Han208
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
EDTA-inactivated enzyme, restoration in decreasing order of effectiveness by Zn2+, Cd2+, Mn2+, Co2+, Ni2+, Ca2+, Hg2+, Cu2+
-
reactivation of EDTA-inactivated enzyme in decreasing order by Zn2+, Cd2+, Mn2+, Cu2+, Co2+, Ni2+
-
reactivation of EDTA-treated enzyme by divalent metyl ions, in decreasing order: Co2+, Mn2+, Ca2+, Mg2+, Cu2+, Zn2+
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
biotechnology
synthesis
agriculture
-
isozyme DS-Co is a possible target for the herbicide glyphosate, i.e. N-[phosphomonomethyl]glycine
agriculture
expression of wild-type enzyme and phenylalanine-feedback insensitive mutant L175Q in Arabidopsis thaliana. Transgenic plants have comparable phenotypes and are fully fertile. The levels of shikimate, prephenate and Phe are higher in the different lines expressing the mutant enzyme than in the lines expressing the natural feedback-sensitive bacterial enzyme, and the control plants. Results imply that the bacterial enzyme is active in the transgenic plants and, similar to its operation in bacteria, the feedback insensitivity trait of the mutant enzyme is fundamental for enhancement of the flow of primary carbon metabolites via the shikimate pathway into the production of aromatic amino acids also in the plant
biotechnology
-
increased production of aromatic amino acids in E. coli mutants with modified phosphoenolpyruvate metabolism and enhanced transketolase activity
biotechnology
-
E. coli strains, overproducing the enzyme, excrete it to the medium, which can also be used as a bioindicator for enhanced carbon commitment into the pathway
biotechnology
fruit-specific manipulation of the conversion of primary to specialized metabolism, e.g. by expressing 3-deoxy-7-phosphoheptulonate synthase in tomato fruits, is an attractive approach for improving fruit aroma and flavour qualities as well as discovering novel fruit-specialized metabolites. Metabolic profiling of transgenic tomato plants expressing a bacterial feedback-insensitive AroG gene, overview
synthesis
synthesis of L-phenylalanine (an important amino acid that is widely used in the production of food flavors and pharmaceuticals) by engineered Escherichia coli. Coexpression of Vitreoscilla hemoglobin gene, driven by a tac promoter, with the genes encoding 3-deoxy-D-arabinoheptulosonate-7-phosphate synthetase (aroF) and feedback-resistant chorismate mutase/prephenate dehydratase (pheAfbr), leads to increased productivity of L-phenylalanine and decreased demand for aeration by Escherichia coli CICC10245
synthesis
-
a strain carrying a mutant protein lacking 81 N-terminal amino acids shows an increased 2-phenylethanol production
synthesis
-
synthesis of L-phenylalanine (an important amino acid that is widely used in the production of food flavors and pharmaceuticals) by engineered Escherichia coli. Coexpression of Vitreoscilla hemoglobin gene, driven by a tac promoter, with the genes encoding 3-deoxy-D-arabinoheptulosonate-7-phosphate synthetase (aroF) and feedback-resistant chorismate mutase/prephenate dehydratase (pheAfbr), leads to increased productivity of L-phenylalanine and decreased demand for aeration by Escherichia coli CICC10245
-
synthesis
Kluyveromyces marxianus CCT 7735
-
a strain carrying a mutant protein lacking 81 N-terminal amino acids shows an increased 2-phenylethanol production
-
EXTERNAL LINKS (specific for EC-Number 2.5.1.54)
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Release 2026.1 (March 2026)
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