2.5.1.54: 3-deoxy-7-phosphoheptulonate synthase
This is an abbreviated version!
For detailed information about 3-deoxy-7-phosphoheptulonate synthase, go to the full flat file.
Word Map on EC 2.5.1.54
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2.5.1.54
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shikimate
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chorismate
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mutase
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4.1.2.15
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prephenate
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l-phenylalanine
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feedback-resistant
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feedback-insensitive
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l-tyrosine
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phenylalanine-sensitive
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kdo8ps
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8-phosphate
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tyrosine-sensitive
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tryptophan-sensitive
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feedback-inhibited
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3-deoxy-d-manno-octulosonate
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3-dehydroshikimate
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arogfbr
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l-tyr
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3-deoxy-d-manno-octulosonate-8-phosphate
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arogenate
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synthesis
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agriculture
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biotechnology
- 2.5.1.54
- shikimate
- chorismate
- mutase
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4.1.2.15
- prephenate
- l-phenylalanine
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feedback-resistant
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feedback-insensitive
- l-tyrosine
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phenylalanine-sensitive
- kdo8ps
- 8-phosphate
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tyrosine-sensitive
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tryptophan-sensitive
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feedback-inhibited
- 3-deoxy-d-manno-octulosonate
- 3-dehydroshikimate
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arogfbr
- l-tyr
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3-deoxy-d-manno-octulosonate-8-phosphate
- arogenate
- synthesis
- agriculture
- biotechnology
Reaction
Synonyms
2-dehydro-3-deoxy-D-arabino-heptonate-7-phosphate D-erythrose-4-phosphate-lyase (pyruvate-phosphorylating), 2-dehydro-3-deoxy-phosphoheptanoate aldolase, 2-dehydro-3-deoxy-phosphoheptonate aldolase, 2-keto-3-deoxy-D-arabino-heptonic acid 7-phosphate synthetase, 3-deoxy-7-phosphoheptulonate synthase, 3-deoxy-D-arabino heptulosonate 7-phosphate synthase, 3-deoxy-D-arabino-2-heptulosonic acid 7-phosphate synthetase, 3-deoxy-D-arabino-heptolosonate-7-phosphate synthetase, 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase, 3-deoxy-D-arabino-heptulosonate 7-phosphate synthetase, 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase, 3-deoxy-D-arabino-heptulosonic acid 7-phosphate synthase, 3-deoxy-D-arabinoheptulosonate 7-phosphate synthase, 3-deoxy-D-arabinoheptulosonate-7-phosphate synthetase, 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate D-erythrose-4-phosphate-lyase (pyruvate-phosphorylating), 7-phospho-2-keto-3-deoxy-D-arabino-heptonate D-erythrose-4-phosphate lyase (pyruvate-phosphorylating), aldolase, phospho-2-keto-3-deoxyheptanoate, Aro1A, Aro4, Aro4p, AroA, AroA(Q), aroF, AroFFR, AroG, D-erythrose-4-phosphate-lyase, D-erythrose-4-phosphate-lyase (pyruvate-phosphorylating), DAH7-P synthase, DAH7-P synthase (phe), DAH7P, DAH7P synthase, DAH7PS, DAHP synthase, DAHP synthase-phe, DAHP synthase-trp, DAHP synthase-tyr, DAHP(Phe), DAHPS, DAHPS(Tyr), Dax1, deoxy-D-arabino-heptulosonate-7-phosphate synthetase, DHS, DHS1, DS-Co, DS-Mn, EC 4.1.2.15, KDPH synthase, KDPH synthetase, More, mtDAH7Ps, MtDS, NCgl0950 DAHP synthase, NCgl2098 DAHP synthase, Nme-DAH7PS, OsDAHPS, PF1690, 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, phzC, TmaDAH7PS
ECTree
2.5.1.54 3-deoxy-7-phosphoheptulonate synthaseAdvanced search results
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results (Engineering
Engineering on EC 2.5.1.54 - 3-deoxy-7-phosphoheptulonate synthase
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PROTEIN VARIANTS 
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
C67L
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site-directed mutagenesis, highly reduced activity, insensitive to inhibition by divalent metal ions
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
H207G
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site-directed mutagenesis, reduced activity, increased Km values for the substrates, reduced kcat
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
I213P
overexpression of variant leads to less decrease in the accumulation of phenylalanine than overexpression of wild-type
L175Q
N5K
N8A
overexpression of variant leads to less decrease in the accumulation of phenylalanine than overexpression of wild-type
N8K
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similar activity and substrate affinities like the wild-type, but insensitive against inhibition by tyrosine, decreased thermostability
P148A
overexpression of variant leads to less decrease in the accumulation of phenylalanine than overexpression of wild-type
Q152A
overexpression of variant leads to higher accumulation of phenylalanine
S181A
overexpression of variant leads to higher accumulation of phenylalanine
I213P
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overexpression of variant leads to less decrease in the accumulation of phenylalanine than overexpression of wild-type
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N8A
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overexpression of variant leads to less decrease in the accumulation of phenylalanine than overexpression of wild-type
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P148A
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overexpression of variant leads to less decrease in the accumulation of phenylalanine than overexpression of wild-type
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Q152A
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overexpression of variant leads to higher accumulation of phenylalanine
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S181A
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overexpression of variant leads to higher accumulation of phenylalanine
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N8K
Escherichia coli W3110 / ATCC 27325
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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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R126S
site-directed mutagenesis, mutation of the residue involved in the salt bridge formation of Arg126-Glu27 results in perturbation of the less extensive interface in the enzyme tetramer and formation of enzyme dimers in solution. The dimeric NmeDAH7PSR126S variant exhibits a slight reduction in thermal stability by differential scanning calorimetry experiments and a slow loss of activity over time compared to the wild-type enzyme. Although NmeDAH7PSR126S crystallised as a tetramer, like the wild-type enzyme, structural asymmetry at the less extensive interface was observed consistent with its destabilisation
S213G
I181D
mutant enzyme is catalytically more active than the wild type enzyme from 20 to 80°C, the mutation disrupts the tetrameric structure of the enzyme, the melting temperatures of the wild-type protein are significantly higher than the melting temperatures of mutant enzyme I181D at pH values greater than 6.5
H29A
site-directed mutagenesis, the mutant is inhibited by both L-Tyr and L-Phe
H29S/S31H
site-directed mutagenesis, the mutant is inhibited to a greater extent by L-Phe than L-Tyr
S31G
site-directed mutagenesis, the mutation severely reduces inhibition by L-Tyr
additional information
I10A
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kinetic parameter similar to wild-type, part of enzyme is monomer instead of dimer
S213G
site-directed mutagenesis, a single Ser residue at the bottom of the inhibitor-binding cavity is substituted to Gly, which alters inhibitor specificity from L-Phe to L-Tyr
S213G
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site-directed mutagenesis, a single Ser residue at the bottom of the inhibitor-binding cavity is substituted to Gly, which alters inhibitor specificity from L-Phe to L-Tyr
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additional information
random mutagenesis, the AroF variant with a deficiency in residue Ile11 is insensitive to L-tyrosine. Construction of feedback-resistant 3-deoxy-D-arabino-heptulosonate-7-phosphate synthases by engineering the N-terminal domain for L-phenylalanine synthesis, generation of nine AroF variants with truncation of different N-terminal fragments, the variants AroFD(1-9), AroFD(1-10), AroFD(1-12) and, in particular, AroFD(1-11) significantly lead to the accumulation of L-phenylalanine, overview. Mutant AroFDELTA(1-11) does not show any feedback inhibition by L-Phe, demonstrated in a strain that has a high L-Phe level through coexpression of L-Phe producing chorismate mutase-4-prephenate dehydratase
additional information
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random mutagenesis, the AroF variant with a deficiency in residue Ile11 is insensitive to L-tyrosine. Construction of feedback-resistant 3-deoxy-D-arabino-heptulosonate-7-phosphate synthases by engineering the N-terminal domain for L-phenylalanine synthesis, generation of nine AroF variants with truncation of different N-terminal fragments, the variants AroFD(1-9), AroFD(1-10), AroFD(1-12) and, in particular, AroFD(1-11) significantly lead to the accumulation of L-phenylalanine, overview. Mutant AroFDELTA(1-11) does not show any feedback inhibition by L-Phe, demonstrated in a strain that has a high L-Phe level through coexpression of L-Phe producing chorismate mutase-4-prephenate dehydratase
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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
additional information
recombinant expression of aroG in transgenic Solanum lycopersicum cv. 82 fruits results in ripe AroG-expressing tomato fruits that have a preferred floral aroma compare with fruits of the wild-type line. Plants expressing the bacterial gene exhibit enhanced levels of a number of aromatic specialized metabolites in a manner that is specific to the bacterial enzyme. Metabolic profiling of transgenic tomato plants expressing a bacterial feedback-insensitive AroG gene, overview
additional information
Escherichia coli W3110 / ATCC 27325
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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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additional information
overexpression of 3-deoxy-7-phosphoheptulonate synthase gene from Gossypium hirsutum enhances Arabidopsis resistance to infection by Verticillium dahliae and Verticillium wilt. GhDHS1 overexpression is associated with longer primary roots for Arabidopsis plants. GhDHS1 overexpression increases xylem lignification of Arabidopsis plants in response to Verticillium dahliae infection
additional information
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overexpression of 3-deoxy-7-phosphoheptulonate synthase gene from Gossypium hirsutum enhances Arabidopsis resistance to infection by Verticillium dahliae and Verticillium wilt. GhDHS1 overexpression is associated with longer primary roots for Arabidopsis plants. GhDHS1 overexpression increases xylem lignification of Arabidopsis plants in response to Verticillium dahliae infection
additional information
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loss of 81 N-terminal amino acid resiudes leads to more flexibility in global terms of structure and a higher degree of compaction. A strain carrying the mutant shows an increased 2-phenylethanol production
additional information
Kluyveromyces marxianus CCT 7735
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loss of 81 N-terminal amino acid resiudes leads to more flexibility in global terms of structure and a higher degree of compaction. A strain carrying the mutant shows an increased 2-phenylethanol production
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