Information on EC 2.5.1.54 - 3-deoxy-7-phosphoheptulonate synthase

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The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota

EC NUMBER
COMMENTARY
2.5.1.54
-
RECOMMENDED NAME
GeneOntology No.
3-deoxy-7-phosphoheptulonate synthase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
show the reaction diagram
mechanism
-
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
show the reaction diagram
mechanism
-
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
show the reaction diagram
sequential mechanism
-
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
show the reaction diagram
sequential mechanism
-
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
show the reaction diagram
sequential mechanism
-
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
show the reaction diagram
ordered sequential mechanism
-
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
show the reaction diagram
His268 is located in the active site
-
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
show the reaction diagram
ordered ping-pong bi-bi mechanism
-
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
show the reaction diagram
ordered ping-pong bi-bi mechanism
-
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
show the reaction diagram
ordered ping-pong bi-bi mechanism
-
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
show the reaction diagram
ordered ping-pong bi-bi mechanism
-
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
show the reaction diagram
first substrate is phosphoenolpyruvate
P0AB91
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
show the reaction diagram
first substrate is phosphoenolpyruvate
-
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
show the reaction diagram
first substrate is phosphoenolpyruvate
-
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
show the reaction diagram
Cys67 and Cys145 are important for the catalytic reaction
-
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
show the reaction diagram
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
-
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
show the reaction diagram
Lys186 is involved in hydrogen bonding with phosphoenolpyruvate
P0AB91
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
show the reaction diagram
active site cysteines: Cys61 and Cys328
-
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
show the reaction diagram
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
-
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
show the reaction diagram
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
P32449
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
show the reaction diagram
ordered ping-pong bi-bi mechanism, first substrate is phosphoenolpyruvate
Streptomyces aureofaciens Tu24
-
-
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
show the reaction diagram
sequential mechanism
Escherichia coli K12
-
-
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
show the reaction diagram
ordered ping-pong bi-bi mechanism, first substrate is phosphoenolpyruvate
Neurospora crassa 74A
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
condensation
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
3-dehydroquinate biosynthesis I
-
-
Biosynthesis of antibiotics
-
-
Biosynthesis of secondary metabolites
-
-
chorismate metabolism
-
-
Metabolic pathways
-
-
Phenylalanine, tyrosine and tryptophan biosynthesis
-
-
SYSTEMATIC NAME
IUBMB Comments
phosphoenolpyruvate:D-erythrose-4-phosphate C-(1-carboxyvinyl)transferase (phosphate-hydrolysing, 2-carboxy-2-oxoethyl-forming)
-
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2-dehydro-3-deoxy-D-arabino-heptonate-7-phosphate D-erythrose-4-phosphate-lyase (pyruvate-phosphorylating)
-
-
-
-
2-dehydro-3-deoxy-phosphoheptanoate aldolase
-
-
-
-
2-dehydro-3-deoxy-phosphoheptonate aldolase
-
-
-
-
2-keto-3-deoxy-D-arabino-heptonic acid 7-phosphate synthetase
-
-
-
-
3-deoxy-D-arabino-2-heptulosonic acid 7-phosphate synthetase
-
-
-
-
3-deoxy-D-arabino-heptolosonate-7-phosphate synthetase
-
-
-
-
3-deoxy-D-arabino-heptulosonate 7-phosphate synthetase
-
-
-
-
3-deoxy-D-arabino-heptulosonate-7-phosphate synthase
-
-
-
-
7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate D-erythrose-4-phosphate-lyase (pyruvate-phosphorylating)
-
-
-
-
7-phospho-2-keto-3-deoxy-D-arabino-heptonate D-erythrose-4-phosphate lyase (pyruvate-phosphorylating)
-
-
-
-
aldolase, phospho-2-keto-3-deoxyheptanoate
-
-
-
-
D-erythrose-4-phosphate-lyase
-
-
-
-
D-erythrose-4-phosphate-lyase (pyruvate-phosphorylating)
-
-
-
-
DAH7-P synthase
-
-
-
-
DAH7-P synthase (phe)
-
-
-
-
DAHP synthase
-
-
-
-
DAHP synthase-phe
-
-
-
-
DAHP synthase-trp
-
-
-
-
DAHP synthase-tyr
-
-
-
-
DAHP(Phe)
-
-
-
-
deoxy-D-arabino-heptulosonate-7-phosphate synthetase
-
-
-
-
KDPH synthase
-
-
-
-
KDPH synthetase
-
-
-
-
phospho-2-dehydro-3-deoxyheptonate aldolase
-
-
-
-
phospho-2-keto-3-deoxyheptanoate aldolase
-
-
-
-
Phospho-2-keto-3-deoxyheptonate aldolase
-
-
-
-
phospho-2-keto-3-deoxyheptonic aldolase
-
-
-
-
phospho-2-oxo-3-deoxyheptonate aldolase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9026-94-2
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Actinosynnema pretiosum ATCC31565
-
UniProt
Manually annotated by BRENDA team
strain U-32; Trp-sensitive isozyme
-
-
Manually annotated by BRENDA team
Amycolatopsis mediterranei U-32
strain U-32
-
-
Manually annotated by BRENDA team
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
-
-
Manually annotated by BRENDA team
enzyme is encoded by duplicated genes : DHS1 and DHS2
-
-
Manually annotated by BRENDA team
2 isozymes: DS-Co and DS-Mn; cv. JL-24
-
-
Manually annotated by BRENDA team
strain B-6
-
-
Manually annotated by BRENDA team
strain B-6
-
-
Manually annotated by BRENDA team
Marburg strain and strain 168, bifunctional enzyme with chorismate mutase activity in addition to enzymic activity
-
-
Manually annotated by BRENDA team
strain 12/60/X, strain 33/X; strain3/2; strain H1; strain H20
-
-
Manually annotated by BRENDA team
Bacteria H1
strain H1
-
-
Manually annotated by BRENDA team
Bacteria H20
strain H20
-
-
Manually annotated by BRENDA team
Bacteria strain3/2
strain3/2
-
-
Manually annotated by BRENDA team
strain ATCC 17409
-
-
Manually annotated by BRENDA team
strains ATCC 13032 and RES167
-
-
Manually annotated by BRENDA team
Tyr-sensitive isozyme
-
-
Manually annotated by BRENDA team
basonym Alcaligenes eutrophus; strain H16
-
-
Manually annotated by BRENDA team
3 enzymes: I, II, and II
-
-
Manually annotated by BRENDA team
cv. Kurodagosun; cytosolic isozyme
-
-
Manually annotated by BRENDA team
i.e. Comamonas terrigena; strain ATCC 11299a, two distinct regulatory isoenzymes: DAHP synthase-phe and DAHP synthase-tyr
-
-
Manually annotated by BRENDA team
3 isoenzymes
-
-
Manually annotated by BRENDA team
deletion mutant strain H80c from strain HfrH; tyrosine-sensitive isozyme
-
-
Manually annotated by BRENDA team
K12; phenylalanine-sensitive isozyme; strain HE 401
-
-
Manually annotated by BRENDA team
K12; strain W3110; tyrosine-sensitive isozyme
-
-
Manually annotated by BRENDA team
mutant 83-24
-
-
Manually annotated by BRENDA team
Phe-sensitive isozyme
Swissprot
Manually annotated by BRENDA team
phenylalanine-sensitive isozyme
-
-
Manually annotated by BRENDA team
phenylalanine-sensitive isozyme
Swissprot
Manually annotated by BRENDA team
strain NST37 (NST, ATCC31882)
-
-
Manually annotated by BRENDA team
tryptophan-sensitive isozyme
-
-
Manually annotated by BRENDA team
tyrosine-sensitive isozyme
-
-
Manually annotated by BRENDA team
Escherichia coli HE 401
strain HE 401
-
-
Manually annotated by BRENDA team
Escherichia coli K12
K12
-
-
Manually annotated by BRENDA team
Escherichia coli NST37
strain NST37 (NST, ATCC31882)
-
-
Manually annotated by BRENDA team
Escherichia coli W3110
strain W3110
-
-
Manually annotated by BRENDA team
strain ATCC 17724
-
-
Manually annotated by BRENDA team
recombinant protein, coexpression with Escherichia coli chaperonins GroEL and GroES in Escherichia coli
-
-
Manually annotated by BRENDA team
strain H37Rv, expression in Escherichia coli
-
-
Manually annotated by BRENDA team
strain H37Rv, expression in Escherichia coli
-
-
Manually annotated by BRENDA team
strain 74-OR23-1A; Trp-, Phe- and Tyr-sensitive isoenzymes
-
-
Manually annotated by BRENDA team
strain 74A; tryptophan-sensitive isozyme
-
-
Manually annotated by BRENDA team
tryptophan-sensitive isozyme
-
-
Manually annotated by BRENDA team
Neurospora crassa 74-OR23-1A
strain 74-OR23-1A
-
-
Manually annotated by BRENDA team
Neurospora crassa 74A
strain 74A
-
-
Manually annotated by BRENDA team
cytosolic isozyme
-
-
Manually annotated by BRENDA team
plastidic isozyme DS-Mn and cytosolic isozyme DS-Co
-
-
Manually annotated by BRENDA team
cv. Onyx; tyrosine-sensitive isozyme
-
-
Manually annotated by BRENDA team
cytosolic isozyme Ds-Co
-
-
Manually annotated by BRENDA team
2 isoenzymes: tyrosine-sensitive DAHP synthase-tyr and tryptophane-sensitive DAHP synthase-trp
-
-
Manually annotated by BRENDA team
ARO3-encoded isozyme is a phenylalanine-sensitive isozyme; ARO4-encoded isozyme is a tyrosine-sensitive isozyme
-
-
Manually annotated by BRENDA team
ARO4-encoded isozyme is a tyrosine-sensitive isozyme; strain RH1326
-
-
Manually annotated by BRENDA team
Phe-sensitive isozyme
-
-
Manually annotated by BRENDA team
strain strain CEN.PK666-1C
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae RH1326
strain RH1326
-
-
Manually annotated by BRENDA team
operator-constitutive strain tyrO; strain SG12; tyrosine-sensitive isozyme
-
-
Manually annotated by BRENDA team
operator-constitutive strain tyrO; tyrosine-sensitive isozyme
-
-
Manually annotated by BRENDA team
Salmonella enterica subsp. enterica serovar Typhimurium SG12
strain SG12
-
-
Manually annotated by BRENDA team
tyrosine-sensitive isozyme
-
-
Manually annotated by BRENDA team
cv. Superior
-
-
Manually annotated by BRENDA team
cytosolic isozyme Ds-Co
-
-
Manually annotated by BRENDA team
cytosolic isozyme Ds-Co
-
-
Manually annotated by BRENDA team
Streptomyces aureofaciens Tu24
strain T 24
-
-
Manually annotated by BRENDA team
strain A3(2); Trp-sensitive isozyme
-
-
Manually annotated by BRENDA team
Trp-sensitive isozyme
-
-
Manually annotated by BRENDA team
recombinant enzyme
-
-
Manually annotated by BRENDA team
2 differentially regulated isozymes: DS-Mn and DS-Co
-
-
Manually annotated by BRENDA team
Xanthobacter autotrophicus 7C
strain 7C
-
-
Manually annotated by BRENDA team
2 classes of enzymes: class AroAI and AroAII; strain ATCC 33436
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
catalysis of first step of shipmate pathway to aromatic amino acids
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
-
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
-
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
phosphoenol-3-fluoropyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-erythro-hept-2-ulosonate 7-phosphate + phosphate
show the reaction diagram
-
enzyme does not discriminate between (E) and (Z)-form of phosphoenol-3-fluoropyruvate
-
-
?
phosphoenolpyruvate + (3S)-2-deoxyerythrose 4-phosphate + H2O
(5S)-[5H]-3,5-dideoxy-D-arabinoheptulosonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
-
ir
phosphoenolpyruvate + 2-deoxy-D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
show the reaction diagram
Q8U0A9
-
-
-
?
phosphoenolpyruvate + 2-deoxy-D-ribose 5-phosphate
3,5-dideoxy-D-gluco-octulosonate 8-phosphate + 3,5-dideoxy-D-manno-octulosonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
?
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
show the reaction diagram
Q8U0A9
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + D,L-lyxose
2-dehydro-3-deoxy-D,L-galacto-octonate + phosphate
show the reaction diagram
-
D-lyxose or L-lyxose, at 1.8% of the activity with D-erythrose 4-phosphate
-
-
?
phosphoenolpyruvate + D-arabinose
2-dehydro-3-deoxy-D-gluco-octonate + phosphate
show the reaction diagram
-
at 0.7% of the activity with D-erythrose 4-phosphate
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
3-deoxy-D-manno-octulosonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
3-deoxy-D-manno-octulosonate 8-phosphate + phosphate
show the reaction diagram
Q8U0A9
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
3-deoxy-D-manno-octulosonate 8-phosphate + phosphate
show the reaction diagram
-
at 8% of the activity with D-erythrose 4-phosphate
-
-
?
phosphoenolpyruvate + D-erythrose
2-dehydro-3-deoxy-D-arabino-heptonate + phosphate
show the reaction diagram
-
at 93% of the activity with D-erythrose 4-phosphate
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
r
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
ir
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
ir
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
ir
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
ir
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
-
ir
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
ir
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
P0AB91
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
P0AB91
binds 1 molecule D-erythrose 4-phosphate per subunit
-
ir
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
in solution D-erythrose 4-phosphate forms dimers that are in slow equilibrium with monomers
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
no repression by the aromatic amino acids
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
P0AB91
first enzyme in the shikimic pathway leading to biosynthesis of aromatic amino acids
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
first enzyme in the shikimic pathway leading to biosynthesis of aromatic amino acids
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
the plastidic enzyme form is induced by fungal elicitor of Phytophthora megasperma, the cytosolic enzyme form is not induced
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
effect of external factors on regulation
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
enzyme is induced by N-[phosphomonomethyl]glycine
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
first enzyme of the aromatic amino acid biosynthesis
-
-
-
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
first enzyme of the aromatic amino acid biosynthesis
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
first enzyme of the aromatic amino acid biosynthesis
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
first enzyme of the aromatic amino acid biosynthesis
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
first enzyme of the aromatic amino acid biosynthesis
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
first enzyme of the aromatic amino acid biosynthesis
-
-
-
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
first enzyme of the aromatic amino acid biosynthesis
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
first enzyme of the aromatic amino acid biosynthesis
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
key regulatory enzyme in L-Phe and L-Tyr biosynthesis
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
first enzyme of aromatic amino acids, folic acid and phenazine 1-carboxylic acid biosynthesis pathways
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
regulatory role of thioredoxin of photosystem I on the chloroplastic enzyme
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
one of the key regulator enzymes of the shikimic acid pathway
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
DSH1 RNA levels increase in Arabidopsis leaves subjected either to physical wounding or to infiltration with pathogenic Pseudomonas syringae strains, DSH2 RNA levels are not increased by these treatments
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
Bacteria H1
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
Escherichia coli HE 401
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
Xanthobacter autotrophicus 7C
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
Salmonella enterica subsp. enterica serovar Typhimurium SG12
-
-
-
-
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
Amycolatopsis mediterranei U-32
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
Amycolatopsis mediterranei U-32
-
first enzyme of the aromatic amino acid biosynthesis
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
first enzyme of aromatic amino acids, folic acid and phenazine 1-carboxylic acid biosynthesis pathways
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
Neurospora crassa 74-OR23-1A
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
Streptomyces aureofaciens Tu24
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
Streptomyces aureofaciens Tu24
-
first enzyme of the aromatic amino acid biosynthesis
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
Streptomyces aureofaciens Tu24
-
-
-
-
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
Bacteria strain3/2, Bacteria H20
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
Escherichia coli K12
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
Escherichia coli K12
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
Escherichia coli K12
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
Escherichia coli K12
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
Escherichia coli K12, Escherichia coli W3110
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
Escherichia coli NST37
-
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
Neurospora crassa 74A
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
Saccharomyces cerevisiae RH1326
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
show the reaction diagram
Q8U0A9
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
show the reaction diagram
O53512
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
show the reaction diagram
Q9YEJ7
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
show the reaction diagram
Actinosynnema pretiosum, Actinosynnema pretiosum ATCC31565
O68903
-
-
-
-
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-erythro-hept-2-ulosonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-erythro-hept-2-ulosonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + D-fructose 1,6-diphosphate
?
show the reaction diagram
-
same activity as with D-erythrose 4-phosphate
-
-
?
phosphoenolpyruvate + D-fructose 6-phosphate
?
show the reaction diagram
-
same activity as with D-erythrose 4-phosphate
-
-
?
phosphoenolpyruvate + D-glucose 6-phosphate
?
show the reaction diagram
-
as effective as D-erythrose 4-phosphate
-
-
?
phosphoenolpyruvate + D-glucose 6-phosphate
?
show the reaction diagram
-
at 0.5% of the activity with D-erythrose 4-phosphate
-
-
?
phosphoenolpyruvate + D-glucose 6-phosphate
?
show the reaction diagram
Amycolatopsis mediterranei U-32
-
as effective as D-erythrose 4-phosphate
-
-
?
phosphoenolpyruvate + D-glyceraldehyde
2-dehydro-3-deoxy-D-threo-hexonate + phosphate
show the reaction diagram
-
at 176% of the activity with D-erythrose 4-phosphate
-
-
?
phosphoenolpyruvate + D-ribose 5-phosphate
3-deoxy-D-altro-octulosonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + D-ribose 5-phosphate
3-deoxy-D-altro-octulosonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + D-ribose 5-phosphate
3-deoxy-D-altro-octulosonate 8-phosphate + phosphate
show the reaction diagram
Amycolatopsis mediterranei, Amycolatopsis mediterranei U-32
-
as effective as D-erythrose 4-phosphate
-
-
?
phosphoenolpyruvate + D-ribose 5-phosphate + H2O
3-deoxy-D-altro-octulosonate 8-phosphate + phosphate
show the reaction diagram
Q8U0A9
-
-
-
?
phosphoenolpyruvate + D-ribose 5-phosphate + H2O
3-deoxy-D-altro-octulosonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + D-ribulose 5-phosphate
?
show the reaction diagram
-
at 12% of the activity with D-erythrose 4-phosphate
-
-
?
phosphoenolpyruvate + D-threose
2-dehydro-3-deoxy-D-xylo-heptonate + phosphate
show the reaction diagram
-
at 92% of the activity with D-erythrose 4-phosphate
-
-
?
phosphoenolpyruvate + D-xylose
2-dehydro-3-deoxy-D-ido-octonate + phosphate
show the reaction diagram
-
at 1% of the activity with D-erythrose 4-phosphate
-
-
?
phosphoenolpyruvate + D-xylulose 5-phosphate
?
show the reaction diagram
Amycolatopsis mediterranei, Amycolatopsis mediterranei U-32
-
at 67% of the activity with D-erythrose 4-phosphate
-
-
?
phosphoenolpyruvate + DL-glyceraldehyde 3-phosphate
pyruvate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + DL-glyceraldehyde 3-phosphate
pyruvate + phosphate
show the reaction diagram
-
at 142% of the activity with D-erythrose 4-phosphate
-
-
?
phosphoenolpyruvate + erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
show the reaction diagram
O53512
-
-
-
?
phosphoenolpyruvate + glycolaldehyde
(S)-2-oxo-4,5-dihydroxypentanoate + phosphate
show the reaction diagram
-
at 245% of the activity with D-erythrose 4-phosphate
-
-
?
phosphoenolpyruvate + glyoxylate
S-4-hydroxy-2-oxo-1,5-pentanedioate + R-4-hydroxy-2-oxo-1,5-pentanedioate + phosphate
show the reaction diagram
-
at 205% of the activity with D-erythrose 4-phosphate
-
-
?
phosphoenolpyruvate + L-erythrose
2-dehydro-3-deoxy-L-arabino-heptonate + phosphate
show the reaction diagram
-
at 70% of the activity with D-erythrose 4-phosphate
-
-
?
phosphoenolpyruvate + L-glyceraldehyde
2-dehydro-3-deoxy-L-threo-hexonate + phosphate
show the reaction diagram
-
at 212% of the activity with D-erythrose 4-phosphate
-
-
?
phosphoenolpyruvate + L-threose
2-dehydro-3-deoxy-L-xylo-heptonate + phosphate
show the reaction diagram
-
at 52% of the activity with D-erythrose 4-phosphate
-
-
?
phosphoenolpyruvate + L-xylose
2-dehydro-3-deoxy-L-ido-octonate + phosphate
show the reaction diagram
-
at 1% of the activity with D-erythrose 4-phosphate
-
-
?
additional information
?
-
-
no activity with D-erythrose, D-glyceraldehyde 3-phosphate, ribose 5-phosphate, glucose 6-phosphate, glucosamine 6-phosphate, N-acetylglucosamine 6-phosphate, and pyruvate
-
-
-
additional information
?
-
-
no substrates are: D-glucose 6-phosphate, D-arabinose, DL-glyceraldehyde, D-erythrose, glycoaldehyde, DL-glyceraldehyde 3-phosphate
-
-
-
additional information
?
-
-
structure comparison between 3-deoxy-7-phosphoheptulonate synthase and 3-deoxy-D-manno-octulosonate 8-phosphate synthase, EC 4.1.2.16, reveal that they share a common ancestor and adopt the same catalytic strategy
-
-
-
additional information
?
-
Q8U0A9
no substrate: D-glyceraldehyde 3-phosphate, D-glucose 6-phosphate
-
-
-
additional information
?
-
-
reaction involves interaction of si face of phosphoenolpyruvate with re face of eryxthrose 4-phosphate
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
no repression by the aromatic amino acids
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
P0AB91
first enzyme in the shikimic pathway leading to biosynthesis of aromatic amino acids
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
first enzyme in the shikimic pathway leading to biosynthesis of aromatic amino acids
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
the plastidic enzyme form is induced by fungal elicitor of Phytophthora megasperma, the cytosolic enzyme form is not induced
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
effect of external factors on regulation
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
enzyme is induced by N-[phosphomonomethyl]glycine
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
first enzyme of the aromatic amino acid biosynthesis
-
-
-
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
first enzyme of the aromatic amino acid biosynthesis
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
first enzyme of the aromatic amino acid biosynthesis
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
first enzyme of the aromatic amino acid biosynthesis
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
first enzyme of the aromatic amino acid biosynthesis
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
first enzyme of the aromatic amino acid biosynthesis
-
-
-
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
first enzyme of the aromatic amino acid biosynthesis
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
first enzyme of the aromatic amino acid biosynthesis
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
key regulatory enzyme in L-Phe and L-Tyr biosynthesis
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
first enzyme of aromatic amino acids, folic acid and phenazine 1-carboxylic acid biosynthesis pathways
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
regulatory role of thioredoxin of photosystem I on the chloroplastic enzyme
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
one of the key regulator enzymes of the shikimic acid pathway
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
DSH1 RNA levels increase in Arabidopsis leaves subjected either to physical wounding or to infiltration with pathogenic Pseudomonas syringae strains, DSH2 RNA levels are not increased by these treatments
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
show the reaction diagram
O53512
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
Amycolatopsis mediterranei U-32
-
first enzyme of the aromatic amino acid biosynthesis
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
-
first enzyme of aromatic amino acids, folic acid and phenazine 1-carboxylic acid biosynthesis pathways
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
Streptomyces aureofaciens Tu24
-
first enzyme of the aromatic amino acid biosynthesis
-
-
?
phosphoenolpyruvate + erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
show the reaction diagram
O53512
-
-
-
?
additional information
?
-
-
structure comparison between 3-deoxy-7-phosphoheptulonate synthase and 3-deoxy-D-manno-octulosonate 8-phosphate synthase, EC 4.1.2.16, reveal that they share a common ancestor and adopt the same catalytic strategy
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
O68903
0.1 mM, up to 500% of initial activity
Cd2+
-
activates, Tyr-sensitive isozyme
Co2+
-
required for full activity; stimulates
Co2+
-
not required, Co2+ is inhibitory at concentrations above 0.1 mM
Co2+
-
2-2.5fold increase in activity at 0.1 mM
Co2+
-
no stimulation of purified enzyme
Co2+
-
no effect
Co2+
-
slightly stimulating
Co2+
-
stimulates
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
Co2+
-
isozyme DS-Co
Co2+
-
stimulates; wild-type and mutants, best activator
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+
O68903
0.1 mM, up to 535% of initial activity
Cu2+
-
3 isozymes contain traces of Cu2+
Cu2+
-
activates, Tyr-sensitive isozyme
Fe2+
-
stimulates
Fe2+
-
contains 0.6 mol of iron per mol of enzyme
Fe2+
-
stimulates; the 3 isozymes contain 0.2-0.3 mol of iron per mol of enzyme monomer
Fe2+
-
activates, Tyr-sensitive isozyme
Fe2+
-
2fold greater inhibition by fosmidomycin with Fe2+ as cofactor than with Co2+, no effect with sulfoenolpyruvate 7 as potential inhibitor
Mg2+
-
slightly
Mg2+
-
stimulates
Mg2+
-
activates, Tyr-sensitive isozyme
Mg2+
-
absolute requirement for divalent metal, Mg2+ is most effective
Mg2+
-
stimulating, can partly substitute for Mn2+
Mn2+
-
stimulates
Mn2+
-
stimulates
Mn2+
-
stimulates
Mn2+
-
Tyr-sensitive isozyme, best activator
Mn2+
-
absolute requirement for divalent metal, 15% of the activation with Mg2+
Mn2+
-
isoenzyme DS-Mn is activated 2.6fold by 0.4 mM Mn2+
Mn2+
-
isozyme DS-Mn
Mn2+
-
absolutely required, can partly be substituted by Mg2+, but not by Ca2+, Fe2+, and Co2+; isozyme DS-Mn
Mn2+
-
assay with 0.1 mM
Mn2+
-
0.06 mM, required
Mn2+
-
required
Mn2+
-
dependent
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+
O68903
0.1 mM, up to 550% of initial activity
Ni2+
-
highly activating; wild-type and mutants
Ni2+
O68903
0.1 mM, up to 495% of initial activity
Zn2+
-
stimulates
Zn2+
-
3 isozymes contain variable amounts of zinc
Zn2+
-
activates, Tyr-sensitive isozyme
Zn2+
-
no effect with sulfoenolpyruvate 7 as potential inhibitor
Zn2+
Q9YEJ7
enzyme contains 0.8 molar equivalents of Zn2+ per subunit
Mn2+
-
a manganese ion is present at the active site, crystallization data
additional information
-
metalloenzyme
additional information
-
Tyr-sensitive isozyme, metal factor required
additional information
-
no effect by Ca2+, Co2+, Cu2+, Fe3+, Mg2+
additional information
-
Phe-sensitive isozyme: Mn2+, Co2+, Zn2+, Fe3+ have no effect
additional information
-
-
additional information
-
reactivation of EDTA-treated enzyme by divalent metyl ions, in decreasing order: Co2+, Mn2+, Ca2+, Mg2+, Cu2+, Zn2+
additional information
-
reactivation of EDTA-inactivated enzyme in decreasing order by Zn2+, Cd2+, Mn2+, Cu2+, Co2+, Ni2+
additional information
-
EDTA-inactivated enzyme, restoration in decreasing order of effectiveness by Zn2+, Cd2+, Mn2+, Co2+, Ni2+, Ca2+, Hg2+, Cu2+
additional information
-
Mg2+ and Ni2+ are not stimulatory
INHIBITORS
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
1,10-phenanthroline
-
activity is restored by Fe2+ or Zn2+
2,3-bisphosphoglycerate
-
-
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
2-Methyl-DL-Trp
-
0.02 mM, 30% inhibition
2-phosphoglycerate
-
competitive with respect to phosphoenolpyruvate
3,4-dihydroxycinnamate
-
isoenzyme DS-Co
3-deoxy-D-arabino-heptonic acid 7-phosphate
-
-
3-deoxy-D-erythro-hept-2-ulosonate 7-phosphate
-
-
3-Methylphosphoenolpyruvate
-
-
3-Propylphosphoenolpyruvate
-
-
4-Methyl-DL-Trp
-
0.02 mM, 30% inhibition
5,5'-dithiobis(2-nitrobenzoate)
-
-
5-Fluoro-DL-Trp
-
0.02 mM, 56% inhibition
5-hydroxy-DL-Trp
-
0.02 mM, 10% inhibition
6-Methyl-DL-Trp
-
0.02 mM, 6% inhibition
7-Aza-DL-Trp
-
0.02 mM, 9% inhibition
7-Methyl-DL-Trp
-
0.02 mM, 14% inhibition
7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate
-
product inhibition
7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate
-
competitive against D-erythrose 4-phosphate and phosphoenolpyruvate
alpha-Methylphenylalanine
-
-
beta-2-Thienyl-D,L-Ala
-
-
beta-phenylserine
-
-
beta-Thienylalanine
-
-
chorismate
-
competitive against phosphoenolpyruvate, noncompetitive against D-erythrose 4-phosphate; DAHP synthase-trp
chorismate
-
50% at 0.12 mM; feedback inhibition, noncompetitive against D-erythrose 4-phosphate and phosphoenolpyruvate
chorismate
-
main allosteric feedback inhibitor and regulator for enzyme of class AroAII
chorismate
-
1 mM, 3% residual activity
chorismate
-
IC50: 1 mM
CN-
-
Tyr-sensitive isozyme, strong inhibition, reactivation by divalent cations only to a small extent
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
-
substrate-inhibition
D-erythrose 4-phosphate
-
-
D-erythrose 4-phosphate
-
isoenzyme DS-Mn: substrate inhibition above 0.5 mM
D-erythrose 4-phosphate
P0AB91
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
D-fructose 1,6-diphosphate
-
-
D-sedoheptulose 1,7-diphosphate
-
-
D-sedoheptulose 7-phosphate
-
-
diethyl dicarbonate
-
Phe-sensitive isozyme, pH-dependent, phosphoenolpyruvate protects wild-type and mutants H64G, H207G, H304G
dihydroxyphenylalanine
-
-
dipicolinic acid
-
inactivation, reactivation by divalent cations
dipicolinic acid
Q9YEJ7
1 mM, 1 h, 21% residual activity
DL-Dibromotryptophan
-
0.02 mM, 52% inhibition
DL-erythro-beta-Methyltryptophan
-
0.02 mM, 40% inhibition
DL-Homotryptophan
-
0.02 mM, 46% inhibition
EDTA
-
reversible by Co2+
EDTA
-
no inhibition
EDTA
-
reversible by Co2+
EDTA
-
phosphoenolpyruvate or 3-deoxy-D-arabino-heptulosonate 7-phosphate and Mn2+, Co2+, Ca2+ and Mg2+ protect
EDTA
-
Co2+, Zn2+, Cu2+, and Fe3+ restore activity
EDTA
-
activity is restored by Fe2+ or Zn2+
EDTA
-
Co2+, Mn2+, Zn2+ and Fe2+ restore activity; phosphoenolpyruvate, 2 mM, partially protects from inactivation, does not restore activity
EDTA
-
reversible by diverse divalent metal ions with varying efficiency
EDTA
-
Mn2+, Cd2+, Co2+, Fe2+, Cu2+, Mg2+ or Zn2+ reactivate, Fe2+ and Cu2+ only partially reactivate
EDTA
-
strong, reversible by dialysis
EDTA
-
inactivation, reactivation by divalent metyl ions, in decreasing order: Co2+, Mn2+, Ca2+, Mg2+, Cu2+, Zn2+
EDTA
-
inactivation, reactivation in decreasing order by Zn2+, Cd2+, Mn2+, Cu2+, Co2+, Ni2+
EDTA
-
inactivation, restoration in decreasing order of effectiveness by Zn2+, Cd2+, Mn2+, Co2+, Ni2+, Ca2+, Hg2+, Cu2+
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
Q9YEJ7
10 mM, 1 h, 21% residual activity
EDTA
O68903
2 mM, complete inactivation within 10 min
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
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
Hg2+
-
complete inhibition at 1 mM
iodoacetamide
-
alkylation, abolishes the dependence on reducing agents
L-arogenate
-
isozyme DS-Mn, competitive against D-erythrose 4-phosphate, non-competitive against phosphoenolpyruvate
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
-
1 mM, 3% residual activity
L-phenylalanine
-
1 mM, 32% residual activity
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-tryptophan
-
1 mM, 3% residual activity
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
-
1 mM, 3% residual activity
L-tyrosine
-
1 mM, 23% residual activity
L-tyrosine
-
almost complete inhibition at 0.5 mM
m-Chlorophenylalanine
-
-
m-Fluorophenylalanine
-
-
m-hydroxyphenylalanine
-
-
Metal chelators
-
-
-
N-alpha-methyl-DL-Trp
-
0.02 mM, 60% inhibition
N-bromosuccinimide
-
-
N-ethylmaleimide
-
-
N-[Phosphomonomethyl]glycine
-
concentration of Co2+ markedly increases the concentration of N-[phosphomonomethyl]glycine required for inhibition; cytosolic isozyme; i.e. glyphosate
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
Na2SO4
-
slightly
o-Chlorophenylalanine
-
-
o-Fluorophenylalanine
-
-
o-Hydroxyphenylalanine
-
-
p-aminophenylalanine
-
-
p-chloromercuribenzoate
-
complete inhibition at 0.02 mM, reversible by cysteine
p-Fluorophenylalanine
-
-
p-hydroxymercuribenzoate
-
-
Phe
-
no inhibition
Phe
-
Phe-sensitive isozyme; strain 12/60/X, no inhibition; strain H1, strain H20 and strain 3/2: cumulative inhibition of Tyr and Phe
Phe
-
0.5 mM, 60% inhibition; Phe-sensitive isozyme
Phe
-
no inhibition
Phe
-
no inhibition
Phe
-
L-Phe; Phe-sensitive isozyme
Phe
-
L-Phe; Phe-sensitive isozyme; strong
Phe
-
0.04 mM, 50% inhibition of DAHP synthase-phe; L-Phe; Phe-sensitive isozyme
Phe
-
Phe-sensitive isozyme
Phe
-
competitive with respect to D-erythrose 4-phosphate and non-competitive to phosphoenolpyruvate; Tyr-sensitive isozyme is less inhibited than the Phe-sensitive isozyme
Phe
-
competitive with respect to D-erythrose 4-phosphate and non-competitive to phosphoenolpyruvate; Phe-sensitive isozyme
Phe
-
feed-back inhibition, Phe-sensitive isozyme; Phe-sensitive isozyme
Phe
-
DSI; Phe-sensitive isozyme
Phe
-
no inhibition
Phe
-
slight inhibition of the wild-type, activation of mutants
Phe
-
Phe-sensitive isozyme
phenylalanine
-
1 Mn, wild-type 8.2% residual activity
phenylalanine
-
-
phenylalanine
-
inhibition of the synthase-chorismate mutase complex, based on mutase activity measurements at 30C, 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
phenylpyruvate
-
DAHP synthase-tyr
phosphate
-
phosphate buffer destabilizes
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
phosphoenolpyruvate
O68903
pronounced substrate inhibition above 1 mM
prephenate
-
isozyme DS-Mn, competitive against D-erythrose 4-phosphate, non-competitive against phosphoenolpyruvate
prephenate
-
50% at 0.02 mM; feedback inhibition, noncompetitive against D-erythrose 4-phosphate and phosphoenolpyruvate
prephenate
-
1 mM, 3% residual activity
prephenate
-
IC50: 0.1 mM
shikimate
-
1 mM, 3% residual activity
tetraammonium (((carboxymethyl)[(2S,3R,4S)-2,3,4-trihydroxy-5-(phosphonatooxy)pentyl]amino)methyl)phosphonate
-
IC50: 0.0066 mM
Tetranitromethane
-
-
Trinitrobenzene sulfonate
-
-
Trp
-
0.02 mM, 65% inhibition; non-competitive against phosphoenolpyruvate and competitive for D-erythrose 4-phosphate; strongly dependent on pH; Trp-sensitive isozyme
Trp
-
DAHP synthase-trp; non-competitive against phosphoenolpyruvate and competitive for D-erythrose 4-phosphate; Trp-sensitive isozyme
Trp
-
non-competitive against phosphoenolpyruvate and competitive for D-erythrose 4-phosphate; Trp-sensitive isozyme
Trp
-
allosteric, best at pH 6.0, no inhibition at pH 7.3; Trp-sensitive isozyme
Trp
-
Trp-sensitive isozyme
Trp
-
noncompetitive to both substrates; Trp-sensitive isozyme
Trp
-
DSI; Trp-sensitive isozyme
Trp
-
Trp-sensitive isozyme
Trp
-
Trp-sensitive isozyme
Trp
-
Trp-sensitive isozyme
Trp
-
L-Trp, weak
Trp
-
isozyme DS-Mn
Trp
-
minor feedback inhibitor
Tyr
-
strain 33/X strongly but not totally inhibited; strain H1, strain H20 and strain 3/2: cumulative inhibition of Tyr and Phe; Tyr-sensitive isozyme
Tyr
-
0.5 mM, 20% inhibition; Tyr-sensitive isozyme
Tyr
-
0.02 mM, 50% inhibition; Tyr-sensitive isozyme
Tyr
-
feedback inhibition; noncompetitive with respect to D-erythrose 4-phosphate, competitive with respect to phosphoenolpyruvate; Tyr-sensitive isozyme
Tyr
-
L-Tyr; Tyr-sensitive isozyme
Tyr
-
noncompetitive with respect to D-erythrose 4-phosphate, competitive with respect to phosphoenolpyruvate; Tyr-sensitive isozyme
Tyr
-
at pH 6.2-7.8; Tyr-sensitive isozyme
Tyr
-
0.04 mM, 50% inhibition of DAHP synthase-tyr; L-Tyr; Tyr-sensitive isozyme
Tyr
-
DAHP synthase-tyr; L-Tyr; Tyr-sensitive isozyme
Tyr
-
L-Tyr; Tyr-sensitive isozyme
Tyr
-
Tyr-sensitive isozyme
Tyr
-
noncompetitive with respect to D-erythrose 4-phosphate, competitive with respect to phosphoenolpyruvate; Tyr-sensitive isozyme
Tyr
-
Tyr-sensitive isozyme
Tyr
-
DSI and DSII; Tyr-sensitive isozyme
Tyr
-
no inhibition
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
-
feedback inhibition; noncompetitive with respect to D-erythrose 4-phosphate, competitive with respect to phosphoenolpyruvate; Tyr-sensitive isozyme; wild-type and mutant S187A
tyrosine
-
inhibition of the synthase-chorismate mutase complex, based on mutase activity measurements at 30C, 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
Zn2+
-
no inhibition of mutant C67L; wild-type and mutants
[(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
Mg2+
-
no inhibition of mutant C67L; wild-type and mutants
additional information
-
no inhibition by Tyr and Phe
-
additional information
-
inhibition mechanism
-
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
-
not inhibitory: phenylalanine, tyrosine, tryptophan, chorismate
-
additional information
-
no inhibitory: EDTA
-
additional information
-
not inhibitory: phenylalanine, tyrosine, tryptophane
-
additional information
-
not inhibitory: L-tryptophan, chorismate, shikimate, D-phenylalanine, L-histidine
-
additional information
-
resistant to denaturation by sodium dodecyl sulfate, not inhibitory: phenylalanine, tyrosine, tryptophan
-
additional information
-
not inhibited by tryptophan
-
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
Q9YEJ7
none of the downstream products of the shikimate biosynthetic pathway tested inhibits the activity of the enzyme
-
additional information
O68903
substrate D-erythrose 4-phosphate is not inhibitory
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
activates
beta-mercaptoethanol
-
-
Chorismic acid
-
stimulates
Chorismic acid
-
activates isozyme DS-Mn
dithiothreitol
-
stimulates
dithiothreitol
-
can partially substitute thioredoxin as activating agent
L-Trp
-
activates
N-[Phosphomonomethyl]glycine
-
i.e. glyphosate; induces synthesis of enzyme
Phe
-
slightly activating, mutants S187Y, S187F, S187C
reduced thioredoxin
-
required for activity, can be partially substituted by dithiothreitol
Tyr
-
2.3fold activation of isozyme DS-Mn
Tyr
-
mutants S187Y, S187F, S187C
L-Trp
-
activates
additional information
-
sulfhydryl groups and possibly a Lys residue may be implicated in activity
-
additional information
-
DHS1 is induced 3-5fold by wounding of the leaf and pathogen attack
-
additional information
-
not hysteretically activated by dithiols, e.g. DTT
-
additional information
-
enzyme uses divalent metal ion to activate a phosphorylated carbohydrate-like substrate
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.65
(3S)-2-deoxyerythrose 4-phosphate
-
pH 6.8
0.006
2-deoxy-D-erythrose 4-phosphate
-
pH 6.8, 60C
2.5
2-deoxy-D-ribose 5-phosphate
-
pH 6.8, 60C
6.8
2-deoxyribose 5-phosphate
-
recombinant enzyme, pH 7.5, 25C
0.03
D-arabinose 5-phosphate
-
recombinant enzyme, pH 7.5, 25C
2.7
D-arabinose 5-phosphate
-
pH 6.8, 60C
2.5
D-erythrose
-
cytosolic isozyme DS-Co, pH 8.6, 37C
0.0026
D-erythrose 4-phosphate
-
pH 7.0, 37C
0.009
D-erythrose 4-phosphate
-
pH 6.8, 60C
0.013
D-erythrose 4-phosphate
-
pH 7.4, 37C
0.018
D-erythrose 4-phosphate
-
wild-type, pH 7.9, 30C
0.021
D-erythrose 4-phosphate
-
pH 6.8
0.028
D-erythrose 4-phosphate
-
60C, pH 6.8
0.055
D-erythrose 4-phosphate
-
pH 7.8, 25C
0.0573
D-erythrose 4-phosphate
-
pH 7.5, 50C
0.07
D-erythrose 4-phosphate
-
pH 7.0, 25C
0.071
D-erythrose 4-phosphate
-
pH 7.5, 60C, mutant enzyme I181D
0.0814
D-erythrose 4-phosphate
-
Tyr-sensitive isozyme, 25C
0.086
D-erythrose 4-phosphate
-
Phe-sensitive isozyme, pH 6.8, 25C
0.092
D-erythrose 4-phosphate
-
pH 7.5, 60C, wild-type enzyme
0.0965
D-erythrose 4-phosphate
-
pH 7.0, 37C
0.13
D-erythrose 4-phosphate
-
Phe-sensitive isozyme, pH 6.8, 30C
0.138
D-erythrose 4-phosphate
-
pH 7.5, 60C
0.141
D-erythrose 4-phosphate
-
recombinant enzyme, pH 7.5, 25C
0.16
D-erythrose 4-phosphate
-
30C, pH 7.0
0.195
D-erythrose 4-phosphate
-
Trp-sensitive isozyme, pH 7.0, 30C
0.25
D-erythrose 4-phosphate
-
Trp-sensitive isozyme, pH 7.2, 37C
0.25
D-erythrose 4-phosphate
-
wild-type, 25C, pH 6.4
0.278
D-erythrose 4-phosphate
-
mutant I10A, 25C, pH 6.4
0.28
D-erythrose 4-phosphate
Q9YEJ7
pH 7.0, 60C
0.29
D-erythrose 4-phosphate
-
isozyme NCgl0950 DAHP synthase, in 50 mM Tris-HCl buffer, pH 7.5, at 30C
0.3506
D-erythrose 4-phosphate
-
pH 7.5, 70C
0.392
D-erythrose 4-phosphate
-
mutant N5K, 25C, pH 6.4
0.43
D-erythrose 4-phosphate
O68903
pH 7.5, 30C
0.5
D-erythrose 4-phosphate
-
Tyr-sensitive isozyme, pH 6.8
0.56
D-erythrose 4-phosphate
-
DAHP synthase-trp, pH 7.0, 37C
0.77
D-erythrose 4-phosphate
-
DAHP synthase-tyr, pH 7.0, 37C
0.87
D-erythrose 4-phosphate
-
DAHP synthase-phe, pH 7.0, 37C
0.9
D-erythrose 4-phosphate
-
pH 7.0, 37C
1
D-erythrose 4-phosphate
-
DAHP synthase-tyr, pH 7.0, 37C
1.1
D-erythrose 4-phosphate
-
DS II isozyme, pH 7.5, 37C
1.2
D-erythrose 4-phosphate
-
pH 6.4, 37C
1.4
D-erythrose 4-phosphate
-
at 37C
1.76
D-erythrose 4-phosphate
-
pH 7.5, 37C
1.95
D-erythrose 4-phosphate
-
cytosolic isozyme DS-Co, pH 8.6, 37C
2.17
D-erythrose 4-phosphate
-
isozyme NCgl2098 DAHP synthase, in 50 mM Tris-HCl buffer, pH 7.5,at 30C
3.3
D-erythrose 4-phosphate
-
cytosolic isozyme, pH 8.6
3.638
D-erythrose 4-phosphate
-
at 37C
52.36
D-erythrose 4-phosphate
-
N-terminal deletion mutant, 25C, pH 6.4
3.5
D-glyceraldehyde
-
cytosolic isozyme DS-Co, pH 8.6, 37C
1.58
D-ribose 5-phosphate
-
pH 6.8, 60C
8.4
D-threose
-
cytosolic isozyme DS-Co, pH 8.6, 37C
3
DL-glyceraldehyde 3-phosphate
-
cytosolic isozyme DS-Co, pH 8.6, 37C
0.006
erythrose 4-phosphate
-
pH 7.5, 30C
8.6
glycolaldehyde
-
cytosolic isozyme DS-Co, pH 8.6, 37C
3.6
glyoxylate
-
cytosolic isozyme DS-Co, pH 8.6, 37C
5.1
L-erythrose
-
cytosolic isozyme DS-Co, pH 8.6, 37C
3.3
L-Glyceraldehyde
-
cytosolic isozyme DS-Co, pH 8.6, 37C
0.003
phosphoenolpyruvate
-
pH 7.5, 30C
0.0032
phosphoenolpyruvate
-
wild-type, pH 7.9, 30C
0.0043
phosphoenolpyruvate
-
recombinant wild-type, 30C, pH 6.5
0.005
phosphoenolpyruvate
-
recombinant enzyme, with D-arabinose 5-phosphate as cosubstrate, pH 7.5, 25C
0.0053
phosphoenolpyruvate
-
recombinant enzyme, with erythrose 4-phosphate as cosubstrate, pH 7.5, 25C
0.0058
phosphoenolpyruvate
-
pH 7.0, 37C
0.0067
phosphoenolpyruvate
-
pH 7.0, 37C
0.009
phosphoenolpyruvate
-
Phe-sensitive isozyme, pH 6.8, 25C
0.009
phosphoenolpyruvate
-
pH 7.5
0.0095
phosphoenolpyruvate
-
pH 7.5, 70C
0.01
phosphoenolpyruvate
-
recombinant enzyme, with ribose 5-phosphate as cosubstrate, pH 7.5, 25C
0.0117
phosphoenolpyruvate
-
pH 7.5, 60C
0.013
phosphoenolpyruvate
-
Tyr-sensitive isozyme, 25C
0.013
phosphoenolpyruvate
-
pH 7.5, 50C
0.015
phosphoenolpyruvate
-
pH 7.4, 37C
0.015
phosphoenolpyruvate
-
recombinant enzyme, with 2-deoxyribose 5-phosphate as cosubstrate, pH 7.5, 25C
0.018
phosphoenolpyruvate
-
Phe-sensitive isozyme, pH 6.8, 30C
0.028
phosphoenolpyruvate
-
mutant N5K, 25C, pH 6.4
0.03
phosphoenolpyruvate
-
pH 7.0, 25C
0.031
phosphoenolpyruvate
-
mutant I10A, 25C, pH 6.4
0.033
phosphoenolpyruvate
-
pH 6.8, 60C, cosubstrate 2-deoxy-D-erythrose 4-phosphate
0.035
phosphoenolpyruvate
-
pH 6.8, 60C, cosubstrate 2-deoxy-D-ribose 5-phosphate
0.035
phosphoenolpyruvate
-
wild-type, 25C, pH 6.4
0.036
phosphoenolpyruvate
-
pH 6.8, 60C, cosubstrate D-ribose 5-phosphate
0.043
phosphoenolpyruvate
-
pH 7.8, 25C
0.062
phosphoenolpyruvate
-
pH 6.8, 60C, cosubstrate D-arabinose 5-phosphate
0.066
phosphoenolpyruvate
-
pH 7.5, 60C, mutant enzyme I181D
0.08
phosphoenolpyruvate
-
37C, pH 7.0
0.09
phosphoenolpyruvate
O68903
pH 7.5, 30C
0.092
phosphoenolpyruvate
-
Trp-sensitive isozyme, pH 7.0, 30C
0.093
phosphoenolpyruvate
-
pH 6.8, 60C, cosubstrate D-erythrose 4-phosphate
0.112
phosphoenolpyruvate
-
pH 7.5, 60C, wild-type enzyme
0.12
phosphoenolpyruvate
-
60C, pH 6.8
0.125
phosphoenolpyruvate
-
Tyr-sensitive isozyme, pH 6.8
0.139
phosphoenolpyruvate
-
pH 7.5, 37C
0.1415
phosphoenolpyruvate
-
at 37C
0.16
phosphoenolpyruvate
-
isozyme NCgl0950 DAHP synthase, in 50 mM Tris-HCl buffer, pH 7.5, at 30C
0.2
phosphoenolpyruvate
-
DAHP synthase-phe, pH 7.0, 37C
0.26
phosphoenolpyruvate
-
DAHP synthase-tyr, pH 7.0, 37C
0.3
phosphoenolpyruvate
-
30C, pH 7.0
0.4
phosphoenolpyruvate
-
Trp-sensitive isozyme, pH 7.2, 37C
0.4
phosphoenolpyruvate
-
isozyme DS II, pH 7.5, 37C
0.891
phosphoenolpyruvate
Q9YEJ7
pH 7.0, 60C
1
phosphoenolpyruvate
-
DAHP synthase-tyr, pH 7.0, 37C
1.11
phosphoenolpyruvate
-
DAHP synthase-trp, pH 7.0, 37C
2
phosphoenolpyruvate
P0AB91
Phe-sensitive isozyme, pH 6.8, 25C
2.724
phosphoenolpyruvate
-
at 37C
3.5
phosphoenolpyruvate
-
pH 6.4, 37C
8.52
phosphoenolpyruvate
-
isozyme NCgl2098 DAHP synthase, in 50 mM Tris-HCl buffer, pH 7.5, at 30C
12.25
phosphoenolpyruvate
-
N-terminal deletion mutant, 25C, pH 6.4
21
phosphoenolpyruvate
P0AB91
Phe-sensitive isozyme, pH 6.8, 25C; sensitive to metal ion
6
ribose 5-phosphate
-
recombinant enzyme, pH 7.5, 25C
13.9
L-threose
-
cytosolic isozyme DS-Co, pH 8.6, 37C
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetics; pH-dependence
-
additional information
additional information
-
-
-
additional information
additional information
-
mutants
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.233
(3S)-2-deoxyerythrose 4-phosphate
-
pH 6.8
0.03
D-erythrose 4-phosphate
O68903
pH 7.5, 30C
0.3
D-erythrose 4-phosphate
-
isozyme NCgl0950 DAHP synthase, in 50 mM Tris-HCl buffer, pH 7.5, at 30C
1.14
D-erythrose 4-phosphate
-
isozyme NCgl2098 DAHP synthase, in 50 mM Tris-HCl buffer, pH 7.5, at 30C
1.183
D-erythrose 4-phosphate
-
pH 6.8
5.5
D-erythrose 4-phosphate
-
pH 7.5, 60C, wild-type enzyme
6.08
D-erythrose 4-phosphate
-
pH 6.8
14.9
D-erythrose 4-phosphate
-
pH 7.5, 60C, mutant enzyme I181D
21
D-erythrose 4-phosphate
-
Trp-sensitive isozyme, pH 7.0, 25C
32
D-erythrose 4-phosphate
-
Phe-sensitive isozyme, pH 6.8, 25C
71
D-erythrose 4-phosphate
P0AB91
Phe-sensitive isozyme, pH 6.8, 25C
0.0035
phosphoenolpyruvate
-
recombinant wild-type, 30C, pH 6.5
0.032
phosphoenolpyruvate
O68903
pH 7.5, 30C
0.35
phosphoenolpyruvate
-
isozyme NCgl0950 DAHP synthase, in 50 mM Tris-HCl buffer, pH 7.5, at 30C
1
phosphoenolpyruvate
Q9YEJ7
pH 7.0, 60C
1.12
phosphoenolpyruvate
-
pH 6.8, 60C, cosubstrate D-arabinose 5-phosphate
1.4
phosphoenolpyruvate
-
pH 6.8, 60C, cosubstrate D-erythrose 4-phosphate
1.5
phosphoenolpyruvate
-
60C, pH 6.8
1.65
phosphoenolpyruvate
-
isozyme NCgl2098 DAHP synthase, in 50 mM Tris-HCl buffer, pH 7.5, at 30C
1.7
phosphoenolpyruvate
-
pH 6.8, 60C, cosubstrate 2-deoxy-D-ribose 5-phosphate
2.3
phosphoenolpyruvate
-
pH 7.5, 50C
2.5
phosphoenolpyruvate
-
pH 6.8, 60C, cosubstrate D-ribose 5-phosphate
3
phosphoenolpyruvate
-
pH 6.8, 60C, cosubstrate 2-deoxy-D-erythrose 4-phosphate
3.3
phosphoenolpyruvate
-
pH 7.5, 30C
4.2
phosphoenolpyruvate
-
N-terminal deletion mutant, 25C, pH 6.4
4.6
phosphoenolpyruvate
-
pH 7.5, 37C
5
phosphoenolpyruvate
-
pH 7.5, 60C
5.5
phosphoenolpyruvate
-
pH 7.5, 60C, wild-type enzyme
7.6
phosphoenolpyruvate
-
pH 7.5, 70C
14.9
phosphoenolpyruvate
-
pH 7.5, 60C, mutant enzyme I181D
21
phosphoenolpyruvate
-
Trp-sensitive isozyme, pH 7.0, 25C
29.5
phosphoenolpyruvate
-
-
32
phosphoenolpyruvate
-
Phe-sensitive isozyme, pH 6.8, 25C
32
phosphoenolpyruvate
-
pH 7.5
56.7
phosphoenolpyruvate
-
mutant N5K, 25C, pH 6.4
58.2
phosphoenolpyruvate
-
mutant I10A, 25C, pH 6.4
62.3
phosphoenolpyruvate
-
wild-type, 25C, pH 6.4
71
phosphoenolpyruvate
P0AB91
Phe-sensitive isozyme, pH 6.8, 25C
122
phosphoenolpyruvate
-
pH 7.0, 37C, MW 79000 assumed
122
D-erythrose 4-phosphate
-
pH 7.0, 37C, MW 79000 assumed
additional information
additional information
-
mutants
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.069
D-erythrose 4-phosphate
O68903
pH 7.5, 30C
500
0.21
D-erythrose 4-phosphate
-
pH 7.5, 60C, mutant enzyme I181D
500
60
D-erythrose 4-phosphate
-
pH 7.5, 60C, wild-type enzyme
500
0.22
phosphoenolpyruvate
-
pH 7.5, 60C, mutant enzyme I181D
51
0.35
phosphoenolpyruvate
O68903
pH 7.5, 30C
51
49
phosphoenolpyruvate
-
pH 7.5, 60C, wild-type enzyme
51
84
phosphoenolpyruvate
-
results within factor two of this otherwise published value, 30C, 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
51
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
0.27
3-deoxy-D-erythro-hept-2-ulosonate 7-phosphate
-
pH 7.5, 30C, cosubstrate phosphoenolpyruvate
1.5
3-deoxy-D-erythro-hept-2-ulosonate 7-phosphate
-
pH 7.5, 30C, cosubstrate erythrose 4-phosphate
1.35
chorismate
-
synthase-trp isozyme, versus phosphoenolpyruvate, 37C, pH 7.0
2.25
chorismate
-
synthase-trp isozyme, versus D-erythrose 4-phosphate, 37C, pH 7.0
0.01
Phe
-
Phe-sensitive isozyme, pH 6.8, 30C
0.27
Phe
-
Tyr-sensitive isozyme, pH 6.8
1.35
phenylpyruvate
-
synthase-tyr isozyme, versus D-erythrose 4-phosphate, 37C, pH 7.0
2.55
phenylpyruvate
-
synthase-tyr isozyme, versus phosphoenolpyruvate, 37C, pH 7.0
22
phosphate
-
slope, tryptophan-sensitive isozyme, versus phosphoenolpyruvate, pH 7.4, 37C
25
phosphate
-
slope, tryptophan-sensitive isozyme, versus D-erythrose 4-phosphate, pH 7.4, 37C
54
phosphate
-
intercept, tryptophan-sensitive isozyme, versus phosphoenolpyruvate, pH 7.4, 37C
0.005
Trp
-
synthase-trp isozyme, versus D-erythrose 4-phosphate, 37C, pH 7.0
0.04
Trp
-
synthase-trp isozyme, versus phosphoenolpyruvate, 37C, pH 7.0
0.0009
Tyr
-
Tyr-sensitive isozyme, pH 6.8
0.02
Tyr
-
pH 7.0, 24C
0.023
Tyr
-
synthase-tyr isozyme, versus D-erythrose 4-phosphate, 37C, pH 7.0; synthase-tyr isozyme, versus phosphoenolpyruvate, 37C, pH 7.0
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
additional information
additional information
-
product inhibition pattern
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1
chorismate
-
IC50: 1 mM
0.1
prephenate
-
IC50: 0.1 mM
0.0066
tetraammonium (((carboxymethyl)[(2S,3R,4S)-2,3,4-trihydroxy-5-(phosphonatooxy)pentyl]amino)methyl)phosphonate
-
IC50: 0.0066 mM
0.0036
[(1E)-7-bromo-2-carboxyhept-1-en-1-yl]phosphonate
-
pH not specified in the publication, temperature not specified in the publication
0.0053
[2-carboxy-7-(phosphonatooxy)hept-1-en-1-yl]phosphonate
-
pH not specified in the publication, temperature not specified in the publication
0.154
[2-carboxy-7-(phosphonatooxy)hept-2-en-1-yl]phosphonate
-
pH not specified in the publication, temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.005
-
partially purified isozyme synthase-trp
0.008
-
partially purified isoenzyme DS-Mn
0.0127
O68903
pH 7.5, 30C
0.026
-
partially purified enzyme
0.056
-
partially purified isozyme synthase-tyr
0.11
-
partially purified isozyme DS-Mn, with Mn2+
0.14
-
partially purified isozyme DS-Co, with Co2+
0.21
-
partially purified isozyme DS-Co
0.27
-
partially purified Tyr-sensitive isozyme
0.29
-
N-terminal deletion mutant, 37C, pH 6.4
0.4
-
partially purified enzyme
0.8
-
recombinant clone M1 in Escherichia coli strain BL21(DE3)
0.81
-
mutant W215A, 37C, pH 6.4
0.91
-
purified enzyme
0.92
-
mutant I10A, 37C, pH 6.4
1.3
-
partially purified enzyme
1.97
-
mutant N5K, 37C, pH 6.4
2.1
-
purified enzyme
2.3
-
purified cytosolic isozyme
2.37
-
mutant V221A, 37C, pH 6.4
2.4
-
partially purified native enzyme
2.7
-
wild-type, 37C, pH 6.4
2.81
-
mutant L179A, 37C, pH 6.4; mutant P150L, 37C, pH 6.4
3.07
-
mutant F144A, 37C, pH 6.4
3.11
-
recombinant clone M2 in Escherichia coli strain BL21(DE3)
3.25
-
mutant F209A, 37C, pH 6.4
3.6
-
mutant L175Q, 37C, pH 6.4
4.25
-
mutant L175A, 37C, pH 6.4
4.46
-
mutant L175D, 37C, pH 6.4
4.5
-
partially purified Phe-sensitive isozyme
7.1
-
purified enzyme
7.7
-
purified Trp-sensitive isozyme
7.8
-
purified enzyme
8.1
-
purified Trp-sensitive isozyme
8.24
-
purified recombinant Tyr-sensitive isozyme
8.33
-
purified Trp-sensitive isozyme
10.75
-
purified enzyme
11.02
-
purified Trp-sensitive isozyme
16.4
-
purified enzyme
18.8
-
partially purified cytosolic isozyme, + 10 mM Mg2+
22
-
purified recombinant Tyr-sensitive isozyme, with Cd2+
30 - 40
-
purified Tyr-sensitive isozyme, wild-type and mutant N8K
56
-
purified enzyme
67
-
purified enzyme
82.6
-
purified enzyme
139.3
-
recombinant wild-type
additional information
-
-
additional information
-
-
additional information
-
mutants, influence of aromatic amino acids on activity
additional information
P0AB91
metal ions are removed form the buffer solution via Chelex 100
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.7
Q9YEJ7
at 60C
6.2
-
Tris-HCl buffer
6.5 - 7
-
-
6.5
-
wild-type and mutants
6.8 - 7.2
-
DAHP synthase-phe
6.8
-
DAHP synthase-tyr
6.8
-
wild-type Phe-sensitive isozyme
7 - 7.4
-
Trp-sensitive isozyme
7 - 7.5
-
recombinant Tyr-sensitive isozyme
7
-
assay at
7
-
DAHP synthase-tyr
7
-
isoenzyme DS-Mn
7
-
assay at
7.2 - 8.2
-
-
7.2
-
DAHP synthase-trp
7.2
-
phosphate buffer, Trp-sensitive isozyme
7.3
-
tryptophan-sensitive isozyme
7.4
-
assay at
7.5 - 8
-
chloroplastic isoenzyme DS-Mn
7.5
-
assay at; mutant enzyme I181D
7.6
-
assay at
8
-
above, Phe-sensitive iaozyme mutant C61G
8.2 - 8.5
-
native enzyme
8.6
-
assay at
8.8
-
isoenzyme DS-Co
9
-
cytosolic isozyme
9.2
-
cytosolic isoenzyme DS-Co
additional information
-
2 forms with pIs of pH 8.4 and pH 7.8
additional information
-
Tyr-sensitive isozyme, pIs: 6.1 and 8.9
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1.5 - 8.5
-
wild-type and mutants
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
-
more than 90% of maximum 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
-
at pH 9.0 the activity is about 60% of the activity at pH 6.0, wid-type enzyme; pH 6.0: about 55% of maximal activity, pH 9.0: about 35% of maximal activity, mutant enzyme I181D
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
7
Q9YEJ7
60C, 40% of maximum activity
8.5 - 9.5
-
more than 85% of maximum activity
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 50
-
wild-type and mutants
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
O68903
predicted
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
chloroplastidic isoenzyme DS-Mn
Manually annotated by BRENDA team
-
chloroplastidic isoenzyme DS-Mn
Manually annotated by BRENDA team
-
chloroplastidic isoenzyme DS-Mn
Manually annotated by BRENDA team
-
cytosolic isoenzyme DS-Co
Manually annotated by BRENDA team
-
cytosolic isoenzyme DS-Co
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Neisseria meningitidis serogroup B (strain MC58)
Neisseria meningitidis serogroup B (strain MC58)
Neisseria meningitidis serogroup B (strain MC58)
Neisseria meningitidis serogroup B (strain MC58)
Neisseria meningitidis serogroup B (strain MC58)
Neisseria meningitidis serogroup B (strain MC58)
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5700
-
gel filtration
660428
40000
-
isozyme NCgl0950 DAHP synthase, SDS-PAGE
684585
51830
-
expected mass, calculated from the 472 amino acids; observed by ESI-MS
701494
51830
-
ESI-MS; expected mass by calculation
703449
53000
-
gel filtration
639770
55400
Q9YEJ7
gel filtration
721793
58450
-
ESI-MS
660428
66000
-
gel filtration
639747
67000
-
DAHP synthase-phe, gel filtration
639759
69000
-
gel filtration
639768
71000
-
Tyr-sensitive isozyme, mutant N8K, gel filtration
639792
75000
-
Tyr-sensitive isozyme, wild-type, gel filtration
639792
84000
-
native NCgl0950 DAHP synthase, gel filtration
684585
97000
-
gel filtration
639742
100000
-
gel fitlration
657871
103000
-
gel filtration
639758
105000
-
strain JP401, gel filtration
639748
107000
-
Trp-sensitive isozyme, gel filtration
639779
109000
-
sedimentation equilibrium experiments, tetrameric enzyme
725725
110000
-
gel filtration; strain JP1525
639748
110000
-
gel filtration
639756
111000
-
gel filtration, tetrameric enzyme
725725
120000
-
gel filtration
639781
134000
-
gel filtration
659228
135000
-
Trp-sensitive isozyme, gel filtration
639769
136000
-
equilibrium sedimentation
639753
137000
-
DAHP synthase-tyr, gel filtration
639760
140000
-
gel filtration and sedimentation equilibrium analysis
639753
156000
-
gel filtration
657873
175000
-
DAHP synthase-trp, gel filtration
639760
200000
-
tryptophan-sensitive isozyme, sedimentation equilibrium centrifugation
639763
251000
-
DAHP synthase-tyr, gel filtration
639759
253000
-
gel filtration
660444
385000 - 443000
-
gel filtration
639780
400000
-
gel filtration
639765
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 33000, SDS-PAGE
?
-
x * 42000, Tyr-sensitive isozyme, SDS-PAGE
?
-
x * 115000, cytosolic isozyme, SDS-PAGE
?
P0AB91
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
?
Escherichia coli K12
-
x * 33000, SDS-PAGE
-
dimer
-
2 * 53000, SDS-PAGE
dimer
-
2 * 59000, SDS-PAGE
dimer
-
2 * 54000, SDS-PAGE
dimer
-
2 * 54000, SDS-PAGE
dimer
-
x * 51000, SDS-PAGE
dimer
-
2 * 39000, recombinant Trp-sensitive isozyme, SDS-PAGE
dimer
-
2 * 29226, ESI-MS, 2 * 29224, calculated
dimer
-
mutant E24Q, crystallization data
dimer
-
wild-type, 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
dimer
-
2 * 54000, SDS-PAGE
-
dimer
Salmonella enterica subsp. enterica serovar Typhimurium SG12
-
2 * 40000, SDS-PAGE
-
homodimer
-
2 * 42000, native isozyme NCgl0950 DAHP synthase, gel filtration, 2 * 50000, native isozyme NCgl2098 DAHP synthase, gel filtration
homodimer
Q9YEJ7
2 * 30000, SDS-PAGE, 2 * 29159, calculated
pentamer
-
5 * 50511, ESI-MS, 5 * 50640, calculated
pentamer
-
5 * 50511, ESI-MS, 5 * 50640, calculated
-
tetramer
-
4 * 38000, SDS-PAGE
tetramer
-
crystallization data
tetramer
-
4 * 35000, Trp-sensitive isozyme
tetramer
-
4 * 52000, tryptophan-sensitive isozyme, SDS-PAGE
tetramer
-
4 * 35000, Phe-sensitive isozyme, SDS-PAGE
tetramer
-
4 * 4000, SDS-PAGE
tetramer
-
wild-type, crystallization data
tetramer
-
at pH 7.5 and 20C, 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
tetramer
Escherichia coli HE 401
-
4 * 35000, Phe-sensitive isozyme, SDS-PAGE
-
tetramer
Amycolatopsis mediterranei U-32
-
4 * 35000, Trp-sensitive isozyme
-
tetramer
Neurospora crassa 74-OR23-1A
-
4 * 52000, tryptophan-sensitive isozyme, SDS-PAGE
-
tetramer
Escherichia coli K12
-
4 * 35000, Phe-sensitive isozyme, SDS-PAGE
-
monomer
-
1 * 42130, calculation from nucleotide sequence
additional information
-
N-terminal amino acid sequence
additional information
-
active site structure
additional information
P0AB91
subunit structure
additional information
-
N-terminal amino acid sequence
-
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
Q9YEJ7
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
P29976
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
P0AB91
Phe-sensitive isozyme, hanging drop vapour diffusion method, 22C, 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 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
-
hanging-drop vapor diffusion, ctystal structure of wild-type enzyme and mutant enzyme I181D
-
recombinant enzyme, in complex with phosphoenolpyruvate
-
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
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8
-
30C, stable for at least 2 h
639742
7 - 7.5
-
maximal stability
639742
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
639771
25
-
1 h, in 1,3-bis[tris(hydroxymethyl)methylamino]propane buffer, 10% loss of activity; 2 h, in 3(N-morpholono)propane-sulfonic acid buffer, 50% loss of activity
639747
25
-
t1/2: 5 h in absence of DTT
639798
30
-
pH 6.0-8.0, stable for at least 2 h
639742
37
-
isoenzyme Ds-Co, 95% loss of activity in absence of phosphoenolpyruvate, 1.1 mM phosphoenolpyruvate almost completely protects from inactivation
639780
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
639792
50
-
inactivation above
639742
50
-
inactivation above
639745
60
-
86h, 50% residual activty
659228
60
-
30 min, presence of phosphoenolpyruvate, stable
660428
70
-
21h, 50% residual activity
659228
70
-
30 min, presence of phosphoenolpyruvate, stable
660428
80
-
5h, 50% residual activity
659228
90
Q9YEJ7
1 h, 50% residual activity
721793
95
-
presence of 0.1 mM Mn2+, 130 min, 50% residual activity, absence of Mn2+, 3 min, 50% residual activity
660428
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
725725
additional information
-
D-erythrose 4-phosphate, erythrose and ribose 5-phosphate increase rate of inactivation; phosphoenolpyruvate protects against inactivation
639742
additional information
-
phosphoenolpyruvate protects against inactivation
639745
additional information
-
phosphoenolpyruvate, D-erythrose 4-phosphate and inorganic phosphate protect the purified enzyme against heat denaturation
639764
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
DTT stabilizes the active protein, no influence on the alkylated enzyme
-
loss of 50% activity by freezing and thawing the cell extract
-
unstable during manipulations such as dialysis, dilution, ammonium sulfate fractionation, chromatography on DEAE-cellulose or Sephadex G-200
-
Mn2+ stabilizes during purification
-
37C, 65 min, 50% residual activity
-
Co2+ stabilizes
-
Cu2+ and Fe2+ accelerates subunit dissociation
-
metal-catalysed oxidation of the enzyme, the apoenzyme shows an exponentially decrease in activity with a half-life of about 1 day at 22C, Cu2+ and Fe2+ accelerated the rate of inactivation and subunit dissociation, phosphoenolpyruvate and EDTA stabilize, mutants are insensitive
-
phosphoenolpyruvate stabilizes
-
spontaneous inactivation with a net loss of two of the seven thiol groups per subunit is restored by dithiothreitol
-
-70C, presence of 1 mM dithiothreitol, stable
-
4C, presence of 1 mM dithiothreitol, stabel for at least 24 h
-
-80C, stable for at least 2 months
-
resistant to denaturation by sodium dodecyl sulfate
-
dithiothreitol stabilizes during incubation at 30C for 15 min
-
overnight dialysis against buffer containing 10 mM EDTA at 4C results in 85% inactivation
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15C, ammonium sulfate and acetone fractions, stable for at least several weeks
-
-20C, 0.1 M potassium phosphate, pH 6.5, 1 mM phosphoenolpyruvate, stable for at least 6 months
-
-20C, in phosphate buffer containing phosphoenolpyruvate, stable for several months
-
-20C, 50% glycerol, stable for at least 4 weeks
-
0.1 M potassium phosphate, pH 7.4, 1 mM phosphoenolpyruvate, 0.02% NaN3, purified enzyme, stable for 2-3 months
-
-80C, isoenzyme DS-Co, stable for at least several months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant protein
Q9YEJ7
Trp-sensitive isozyme, 130fold
-
recombinant from Escherichia coli, mature chloroplastic form, purified to homogeneity
-
partially, isozymes DS-Co and DS-Mn
-
His-Bind protein chromatography
-
recombinant His-tagged wild-type and mutants from Escherichia coli
-
cytosolic isozyme, 79.8fold to homogeneity
-
enzyme III
-
2fold; recombinant from overexpressing strain
-
5-6fold to homogeneity; recombinant from overexpressing strain
-
Phe-sensitive isozyme, recombinant wild-type from overexpressing strain and recombinant mutants
-
recombinant from overexpressing strain
-
strain JP1525
-
Tyr-sensitive isozyme, wild-type and mutants from strain AB3257
-
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
-
recombinant enzyme
-
2350fold purification of the tryptophan sensitive isozyme, partial purification of the tyrosine- and phenylalanine-sensitive isozyme
-
Trp-sensitive isozyme to homogeneity, 2000fold
-
partially, 2 isozymes
-
Phe-sensitive isozyme, 11fold to homogeneity from overproducing strain
-
recombinantly overexpresed Tyr-sensitive isozyme, 7.5fold
-
Tyr-sensitive isozyme
-
Trp-sensitive isozyme to homogeneity, 2380fold, large scale
-
Trp-sensitive isozyme to homogeneity, 3750fold
-
partial, isozyme DS-Co and isozyme DS-Mn
-
partial, 19fold, recombinant from Escherichia coli
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in soluble form by co-expression with chaperonins GroEL/GroES in Escherichia coli
O68903
expression in Escherichia coli
Q9YEJ7
DHS1 and DHS2, complementation of Saccharomyces cerevisiae mutant strain YBK7
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expression of mature chloroplastic form, without signal sequence, in Escherichia coli
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expressed in Escherichia coli
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expressed in Escherichia coli BL21(DE3) cells
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overexpression of His-tagged wild-type and mutants in Escherichia coli
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expressed in Escherichia coli strain NSTCSRA
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gene aroF, Tyr-sensitive isozyme, expression of wild-type and mutants in strain AB3257
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gene aroF, Tyr-sensitive isozyme, overexpression in strain BL21(DE3)
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gene aroG, Phe-sensitive isozyme, overexpression in strain gene aroH, Trp-sensitive isozyme, overexpression in deficient strain AB3248
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overexpression in BL21(DE3)
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overexpression of 3 isozymes
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Phe-sensitive isozyme, wild-type and mutants, expression in Escherichia coli strain BL21(DE3)
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expression in Escherichia coli
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expression of enzyme with affinity purification tagwith plasmid pKTDS-HN in Escherichia coli KA13
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N-terminally histidine-tagged enzyme is expressed in Escherichia coli KA13
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expressed in Escherichia coli
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ARO3 gene, expression in deficient strain and in Escherichia coli strain JA196
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ARO4 gene, tyrosine-sensitive isozyme, overexpression from plasmid in strain RH1326
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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
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C145S
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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
C334S
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site-directed mutagenesis, unaltered properties
C67L
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site-directed mutagenesis, highly reduced activity, insensitive to inhibition by divalent metal ions
C67S
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site-directed mutagenesis, inactive
S187A
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site-directed mutagenesis, slightly reduced activity
S187C
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site-directed mutagenesis, reduced activity, activation by tyrosine and phenylalanine instead of inhibition like the wild-type
S187F
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site-directed mutagenesis, highly reduced activity, activation by tyrosine and phenylalanine instead of inhibition like the wild-type
S187Y
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site-directed mutagenesis, highly reduced activity, activation by tyrosine and phenylalanine instead of inhibition like the wild-type
C328V
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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
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site-directed mutagenesis, highly reduced activity, highly increased Km for phosphoenolpyruvate, higher pH-optimum than the wild-type
C61V
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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
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N-terminal deletion of amino acids 1-15, no formation of dimeric form
E24Q
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unlike tetrameric enzyme, mutant is dimeric in solution
F144A
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inhibition by phenylalanine, 30% residual activity
F209A
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inhibition by phenylalanine, 79% residual activity
H172G
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site-directed mutagenesis, inactive
H207G
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site-directed mutagenesis, reduced activity, increased Km values for the substrates, reduced kcat
H268G
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site-directed mutagenesis, inactive
H304G
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site-directed mutagenesis, reduced activity, increased Km values for the substrates, increased kcat
H64G
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site-directed mutagenesis, reduced activity, increased Km values for the substrates, increased kcat
H64L
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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
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inhibition by phenylalanine, 95% residual activity
I10A
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kinetic parameter similar to wild-type, part of enzyme is monomer instead of dimer
L175A
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inhibition by phenylalanine, 18% residual activity
L175D
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inhibition by phenylalanine, 83% residual activity
L175Q
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inhibition by phenylalanine, 44% residual activity
L175Q
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phenylalanine-feedback-insensitive mutant
N5K
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inhibition by phenylalanine, 33% residual activity
N5K
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kinetic parameter similar to wild-type
N8K
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similar activity and substrate affinities like the wild-type, but insensitive against inhibition by tyrosine, decreased thermostability
P150L
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inhibition by phenylalanine, no inhibition by phenylalanine
V221A
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inhibition by phenylalanine, 95% residual activity
N8K
Escherichia coli W3110
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similar activity and substrate affinities like the wild-type, but insensitive against inhibition by tyrosine, decreased thermostability
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I181D
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mutant enzyme is catalytically more active than the wild type enzyme from 20 to 80C, 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
K229L
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the mutation eliminates the L-tyrosine sensitivity
P165G
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inhibited by tryptophan
Q302R
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inhibited by tryptophan
S195A
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inhibited by tryptophan
L179A
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inhibition by phenylalanine, 82% residual activity
additional information
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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
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N-terminal deletion mutant, no inhibition by phenylalanine
additional information
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KDPGal aldolase mutant EC03-1 (F33I/D58N/Q72H/A75V/V85A/V154F) develops increased DAHP synthase activity
W215A
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inhibition by phenylalanine, 58% residual activity
additional information
Escherichia coli K12
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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
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N8K
Escherichia coli K12
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similar activity and substrate affinities like the wild-type, but insensitive against inhibition by tyrosine, decreased thermostability
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additional information
Escherichia coli W3110
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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
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Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
reactivation of dipicolinic acid-inactivated enzyme by divalent cations
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reactivation of EDTA-treated enzyme by divalent metyl ions, in decreasing order: Co2+, Mn2+, Ca2+, Mg2+, Cu2+, Zn2+
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EDTA-inactivated enzyme, restoration in decreasing order of effectiveness by Zn2+, Cd2+, Mn2+, Co2+, Ni2+, Ca2+, Hg2+, Cu2+
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reactivation of EDTA-inactivated enzyme in decreasing order by Zn2+, Cd2+, Mn2+, Cu2+, Co2+, Ni2+
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
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isozyme DS-Co is a possible target for the herbicide glyphosate, i.e. N-[phosphomonomethyl]glycine
agriculture
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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
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increased production of aromatic amino acids in E. coli mutants with modified phosphoenolpyruvate metabolism and enhanced transketolase activity, 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