4.2.1.118: 3-dehydroshikimate dehydratase
This is an abbreviated version!
For detailed information about 3-dehydroshikimate dehydratase, go to the full flat file.
Word Map on EC 4.2.1.118
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4.2.1.118
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protocatechuate
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quinate
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glutamicum
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corynebacterium
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lignin
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crassa
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quinic
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saccharification
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nylon
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bioproducts
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adipic
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qa
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muconic
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7-phosphate
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polyurethan
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co-product
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petrochemicals
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3,4-dihydroxybenzoate
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terephthalic
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podospora
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feedback-resistant
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bioenergy
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3-dehydroquinate
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cis,cis-muconic
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synthesis
- 4.2.1.118
- protocatechuate
- quinate
- glutamicum
- corynebacterium
- lignin
- crassa
-
quinic
-
saccharification
-
nylon
-
bioproducts
-
adipic
- qa
-
muconic
- 7-phosphate
-
polyurethan
-
co-product
-
petrochemicals
- 3,4-dihydroxybenzoate
-
terephthalic
-
podospora
-
feedback-resistant
-
bioenergy
- 3-dehydroquinate
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cis,cis-muconic
- synthesis
Reaction
Synonyms
(-)-3-dehydroshikimate dehydratase, 3-dehydroshikimate dehydratase, AroZ, AsbF, BT246_21860, dehydroshikimate dehydratase, DHSase, DSD, mDSD, membrane-bound 3-dehydroshikimate dehydratase, Qa-1, QsuB, Qui1, quiC1, quiC_1, QutC
ECTree
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General Information
General Information on EC 4.2.1.118 - 3-dehydroshikimate dehydratase
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evolution
metabolism
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lignin biosynthetic pathway and heterologous expression of bacterial 3-dehydroshikimate dehydratase
physiological function
additional information
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the QuiC1 protein is not related by sequence with previously identified DSDs from the Gram-negative genus, Acinetobacter, but instead shows limited sequence identity in its N-terminal half with fungal DSDs
evolution
the QuiC1 protein is not related by sequence with previously identified DSDs from the Gram-negative genus, Acinetobacter, but instead shows limited sequence identity in its N-terminal half with fungal DSDs
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constitutve overexpression leads to impaired growth in minimal medium which can be alleviated by the addition of aromatic amino acids to the medium. Overexpression of the qutC gene in mutant strains lacking protocatechuic acid oxygenase leads to the build up of protocatechuic acid in the medium. The metabolites 3-dehydroquinate and dehydroshikimate leak from the pentafunctional AROM protein at a rate comparable with the extent of flux catalysed by the AROM protein. The AROM protein has a low level channelling function probably as a result of the close juxtaposition of five active sites and this channelling function is only physiologically significant under non-optimal conditions of nutrient supply and oxygenation, when the organism is in situ in its natural environment
physiological function
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3-dehydroshikimate dehydratase is the first enzyme known to catalyze the aromatization of dehydroshikimate to protocatechuate
physiological function
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3-dehydroshikimate dehydratase is the first enzyme known to catalyze the aromatization of dehydroshikimate to protocatechuate
physiological function
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enzyme Qui1 is important for growth on either quinate or shikimate
physiological function
enzyme Qui1 is important for growth on either quinate or shikimate
physiological function
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the enzyme converts 3-dehydroshikimate, an intermediate of the shikimate pathway, into protocatechuate
physiological function
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3-dehydroshikimate dehydratase is the first enzyme known to catalyze the aromatization of dehydroshikimate to protocatechuate
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additional information
superimposition of the active sites of the Pseudomonas putida QuiC1 N-terminal domain and Bacillus anthracis AsbF in complex with protocatechuate. AsbF residues occupying the same position as QuiC1 Arg207 and Arg210 are not observed. Enzyme structure-function analysis, overview
additional information
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superimposition of the active sites of the Pseudomonas putida QuiC1 N-terminal domain and Bacillus anthracis AsbF in complex with protocatechuate. AsbF residues occupying the same position as QuiC1 Arg207 and Arg210 are not observed. Enzyme structure-function analysis, overview
additional information
superimposition of the active sites of the Pseudomonas putida QuiC1 N-terminal domain and Bacillus anthracis AsbF in complex with protocatechuate. AsbF residues occupying the same position as QuiC1 Arg207 and Arg210 are not observed. Enzyme structure-function analysis, overview