Catalyses an early step in the biosynthesis of petrobactin, a siderophore produced by many bacteria, including the human pathogen Bacillus anthracis. Requires divalent ions, with a preference for Mn2+.
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SYSTEMATIC NAME
IUBMB Comments
3-dehydroshikimate hydro-lyase
Catalyses an early step in the biosynthesis of petrobactin, a siderophore produced by many bacteria, including the human pathogen Bacillus anthracis. Requires divalent ions, with a preference for Mn2+.
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
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
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
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
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
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
three-dimensional structure comparisons, superimposition of the QuiC1 N-terminal (DSD) domain with Bacillus anthracis AsbF, and structure comparisons with Pseudomonas fluorescens 4-hydroxyphenylpyruvate dioxygenase (HPPD), overview
three-dimensional structure comparisons, superimposition of the QuiC1 N-terminal (DSD) domain with Bacillus anthracis AsbF, and structure comparisons with Pseudomonas fluorescens 4-hydroxyphenylpyruvate dioxygenase (HPPD), overview
three-dimensional structure comparisons, superimposition of the QuiC1 N-terminal (DSD) domain with Bacillus anthracis AsbF and structure comparisons with Pseudomonas fluorescens 4-hydroxyphenylpyruvate dioxygenase (HPPD), overview
three-dimensional structure comparisons, superimposition of the QuiC1 N-terminal (DSD) domain with Bacillus anthracis AsbF and structure comparisons with Pseudomonas fluorescens 4-hydroxyphenylpyruvate dioxygenase (HPPD), overview
random mutagenesis, triple AsbF mutant Mut1, half-life of Mut1 at 37°C is over 10fold higher compared to wild-type AsbF. The second-order rate constants for both wild-type AsbF and Mut1 are approximately equal, thus demonstrating protein thermostability does not come at the expense of enzyme thermophilicity
gene asbF is unstable at 37°C, structure-based design to identify stabilizing mutations and creation a combinatorial library based upon predicted mutations at specific locations on the enzyme surface. A diversified asbF library (with about 2000 variants) is expressed in Escherichiaxa0coli harboring a GFP reporter system linked to the product of AsbF activity (3,4-dihydroxybenzoate, DHB)
quiC1 transposon quiC1 gene knockout in strain PAO1, recombinant plasmid-based expression of gene quiC1 from Pseudomonas putida QuiC1 in the Pseudomonas aeruginosa quiC1 knockout strain
native mDSD from strain IFO 3244 membrane fraction to homogeneity by solubilization with detergents n-dodecyl-beta-D-maltoside and n-octyl-beta-D-glucoside, anion exchange and hydroxyapatite chromatography. The cytosolic isozyme sDSD is purified from the cytosolic fraction after centrifugation at 62000 x g followed by anion echange chromatograohy, ammonium sulfate precipitation, and dialysis, the enzyme activity is lost during dialysis
gene qsuB, recombinant expression of the 3-dehydroshikimate dehydratase from Corynebacterium glutamicum in Arabidopsis thaliana transgenic C4H::qsuB lines, the enzyme is targeted to the plastids via plastid-targeting signal peptide (SCHL), reduces lignin content and improves biomass saccharification efficiency, reduction of lignin deposition. Compared to wild-type plants, lines expressing QsuB contain higher amount of protocatechuate, p-coumarate, p-coumaraldehyde and p-coumaryl alcohol, and lower amounts of coniferaldehyde, coniferyl alcohol, sinapaldehyde, and sinapyl alcohol. Metabolite analysis of C4H::qsuB lines, overview. Recombinant expression of YFP-tagged enzyme in plastids of transgenic Arabidopsis thaliana
gene quiC1, sequence comparisons and phylogenetic analysis, plasmid-based expression of Pseudomonas putida QuiC1 in the Pseudomonas aeruginosa quiC1 knockout strain, recombinant expression of wild-type and mutant enzymes
in vivo overexpression of enzyme mutant Mut1 in Escherichiaxa0coli results in a about 60fold increase in functional enzyme when compared to the wild-type enzyme under the identical expression conditions, and 80-120% increase in DHB accumulation in the media
introduction of both 3-dehydroshikimate dehydratase and protocatechuic acid decarboxylase into an Escherichia coli construct synthesizing elevated levles of 3-dehydroshikimic acid leads to production of up to 18.5 mM catechol from 56 mM D-glucose on 1 l-scale
production of vanillin by engineered pathway in Schizosaccharomyces pombe or Saccharomyces cerevisiae. Pathway involves incorporation of 3-dehydroshikimate dehydratase, an aromatic carboxylic acid reductase from a bacterium of the Nocardia genus, and an O-ethyltransferase from Homo sapiens. In Saccharomyces cerevisiae, the aromatic carboxylic acid reductase enzyme requires activation by phosphopantetheinylation, achieved by coexpression of a Corynebacterium glutamicum phosphopantetheinyl transferase. Prevention of reduction of vanillin to vanillyl alcohol is achieved by knockout of the host alcohol dehydrogenase ADH6. In Schizosaccharomyces pombe, the biosynthesis is further improved by introduction of an Arabidopsis thaliana family 1 UDPglycosyltransferase, converting vanillin into vanillin beta-D-glucoside, which is not toxic to the yeast cells and thus may be accumulated in larger amounts
Shinagawa, E.; Adachi, O.; Ano, Y.; Yakushi, T.; Matsushita, K.
Purification and characterization of membrane-bound 3-dehydroshikimate dehydratase from Gluconobacter oxydans IFO 3244, a new enzyme catalyzing extracellular protocatechuate formation
Rapid thermostabilization of Bacillus thuringiensis serovar Konkukian 97-27 dehydroshikimate dehydratase through a structure-based enzyme design and whole cell activity assay