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Information on EC 2.5.1.54 - 3-deoxy-7-phosphoheptulonate synthase and Organism(s) Mycobacterium tuberculosis and UniProt Accession O53512

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This record set is specific for:
Mycobacterium tuberculosis
UNIPROT: O53512 not found.
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Word Map
The taxonomic range for the selected organisms is: Mycobacterium tuberculosis
The enzyme appears in selected viruses and cellular organisms
Synonyms
dahp synthase, dahps, dah7ps, 3-deoxy-d-arabino-heptulosonate-7-phosphate synthase, ds-co, ds-mn, dah7p synthase, dahp synthase-phe, dah7p, 3-deoxy-d-arabinoheptulosonate 7-phosphate synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3-deoxy-7-phosphoheptulonate synthase
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3-deoxy-D-arabino-heptulosonate 7-phosphate synthase
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2-dehydro-3-deoxy-D-arabino-heptonate-7-phosphate D-erythrose-4-phosphate-lyase (pyruvate-phosphorylating)
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-
-
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2-dehydro-3-deoxy-phosphoheptanoate aldolase
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-
-
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2-dehydro-3-deoxy-phosphoheptonate aldolase
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-
-
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2-keto-3-deoxy-D-arabino-heptonic acid 7-phosphate synthetase
-
-
-
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3-deoxy-D-arabino-2-heptulosonic acid 7-phosphate synthetase
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-
-
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3-deoxy-D-arabino-heptolosonate-7-phosphate synthetase
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-
-
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3-deoxy-D-arabino-heptulosonate 7-phosphate synthetase
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-
-
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3-deoxy-D-arabino-heptulosonate-7-phosphate synthase
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-
-
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7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate D-erythrose-4-phosphate-lyase (pyruvate-phosphorylating)
-
-
-
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7-phospho-2-keto-3-deoxy-D-arabino-heptonate D-erythrose-4-phosphate lyase (pyruvate-phosphorylating)
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-
-
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aldolase, phospho-2-keto-3-deoxyheptanoate
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-
-
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D-erythrose-4-phosphate-lyase
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-
-
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D-erythrose-4-phosphate-lyase (pyruvate-phosphorylating)
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-
-
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DAH7-P synthase
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-
-
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DAH7-P synthase (phe)
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-
-
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DAH7P synthase
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DAHP synthase
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-
-
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DAHP synthase-phe
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-
-
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DAHP synthase-trp
-
-
-
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DAHP synthase-tyr
-
-
-
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DAHP(Phe)
-
-
-
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deoxy-D-arabino-heptulosonate-7-phosphate synthetase
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-
-
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KDPH synthase
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-
-
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KDPH synthetase
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-
-
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phospho-2-dehydro-3-deoxyheptonate aldolase
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-
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phospho-2-keto-3-deoxyheptanoate aldolase
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-
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Phospho-2-keto-3-deoxyheptonate aldolase
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-
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phospho-2-keto-3-deoxyheptonic aldolase
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-
-
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phospho-2-oxo-3-deoxyheptonate aldolase
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
condensation
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
phosphoenolpyruvate:D-erythrose-4-phosphate C-(1-carboxyvinyl)transferase (phosphate-hydrolysing, 2-carboxy-2-oxoethyl-forming)
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CAS REGISTRY NUMBER
COMMENTARY hide
9026-94-2
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + 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 + erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + 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 + erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2S)-2,7-bis(phosphonooxy)heptanoic acid
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3-pyridine carboxyaldehyde
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4-allylpyrocatechol
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allylpyrocatechol-3,4-diacetate
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eupalitin-3-O-galactoside
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L-phenylalanine
allosteric feedback inhibition
L-tryptophan
allosteric feedback inhibition
L-tyrosine
allosteric feedback inhibition
phenylalanine
inhibition of the synthase-chorismate mutase complex, based on mutase activity measurements at 30°C, 50 mM BTP (1,3-bis[tris(hydroxymethyl)methylamino]propane), pH 7.5, 0.5 mM TCEP [tris(2-carboxyethyl)phosphine hydrochloride], 0.2 mM phosphoenolpyruvate, and 0.1 mM MnCl2
tyrosine
inhibition of the synthase-chorismate mutase complex, based on mutase activity measurements at 30°C, 50 mM BTP (1,3-bis[tris(hydroxymethyl)methylamino]propane), pH 7.5, 0.5 mM TCEP [tris(2-carboxyethyl)phosphine hydrochloride], 0.2 mM phosphoenolpyruvate, and 0.1 mM MnCl2
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
beta-mercaptoethanol
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
84
phosphoenolpyruvate
results within factor two of this otherwise published value, 30°C, 50 mM BTP (1,3-bis[tris(hydroxymethyl)methylamino]propane), pH 7.5 with 100 microM MnCl2, 240 microM D-erythrose-4-phosphate (saturating), less than 10 microM phosphoenolpyruvate, no influence of chorismate mutase concentration on activity
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.054
3-pyridine carboxyaldehyde
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.021
alpha-tocopherol
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.042
rutin
Mycobacterium tuberculosis
pH and temperature not specified in the publication
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
51830
253000
-
gel filtration
50511
-
5 * 50511, ESI-MS, 5 * 50640, calculated
50640
-
5 * 50511, ESI-MS, 5 * 50640, calculated
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pentamer
-
5 * 50511, ESI-MS, 5 * 50640, calculated
additional information
-
N-terminal amino acid sequence
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, stable for at least 2 months
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of enzyme with affinity purification tagwith plasmid pKTDS-HN in Escherichia coli KA13
N-terminally histidine-tagged enzyme is expressed in Escherichia coli KA13
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Webby, C.J.; Lott, J.S.; Baker, H.M.; Baker, E.N.; Parker, E.J.
Crystallization and preliminary X-ray crystallographic analysis of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Mycobacterium tuberculosis
Acta Crystallogr. Sect. F
F61
403-406
2005
Mycobacterium tuberculosis
Manually annotated by BRENDA team
Rizzi, C.; Frazzon, J.; Ely, F.; Weber, P.G.; da Fonseca, I.O.; Gallas, M.; Oliveira, J.S.; Mendes, M.A.; de Souza, B.M.; Palma, M.S.; Santos, D.S.; Basso, L.A.
DAHP synthase from Mycobacterium tuberculosis H37Rv: cloning, expression, and purification of functional enzyme
Protein Expr. Purif.
40
23-30
2005
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
Manually annotated by BRENDA team
Okvist, M.; Sasso, S.; Roderer, K.; Kast, P.; Krengel, U.
A novel noncovalent complex of chorismate mutase and DAHP synthase from Mycobacterium tuberculosis: protein purification, crystallization and X-ray diffraction analysis
Acta Crystallogr. Sect. F
65
1048-1052
2009
Mycobacterium tuberculosis (O53512), Mycobacterium tuberculosis
Manually annotated by BRENDA team
Sasso, S.; Okvist, M.; Roderer, K.; Gamper, M.; Codoni, G.; Krengel, U.; Kast, P.
Structure and function of a complex between chorismate mutase and DAHP synthase: efficiency boost for the junior partner
EMBO J.
28
2128-2142
2009
Mycobacterium tuberculosis (O53512), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (O53512)
Manually annotated by BRENDA team
Nirmal, C.R.; Rao, R.; Hopper, W.
Inhibition of 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase from Mycobacterium tuberculosis: in silico screening and in vitro validation
Eur. J. Med. Chem.
105
182-193
2015
Mycobacterium tuberculosis (O53512), Mycobacterium tuberculosis
Manually annotated by BRENDA team