Disease relevance of aroD

• These E. coli transformants complement an aroD mutant [1].
• Construction of aromatic dependent Shigella flexneri 2a live vaccine candidate strains: deletion mutations in the aroA and the aroD genes [2].
• The aroD gene from Salmonella typhi, encoding 5-dehydroquinate hydrolyase (3-dehydroquinase), has been cloned into Escherichia coli and the DNA sequence determined [3].
• Bacteriophage P22 as a vehicle for transducing cosmid gene banks between smooth strains of Salmonella typhimurium: use in identifying a role for aroD in attenuating virulent Salmonella strains [4].
• An aroD gene of Escherichia coli K12 strain NK 5131, inactivated by insertion in it of the Tn 10 transposon, was transduced using phage P1 into a virulent S. flexneri serotype Y strain (Sfl 1) isolated from a patient with bacillary dysentery [5].

High impact information on aroD

• DNA from these transformants can be recovered by retransformation back into E. coli aroD recipients and selection for chloramphenicol resistance [1].
• The shikimate pathway enzyme 3-dehydroquinase is very susceptible to inactivation by the group-specific reagent diethyl pyrocarbonate (DEP) [6].
• These genes code for 3-dehydroquinase enzymes of type II, involved in the catabolism of quinic acid [7].
• All recombinant cosmids selected for their aroD complementation property carry this sequence [8].
• No DNA sequence homology has, however, been detected by Southern hybridization between the cloned fragment and the aroD gene of E. coli or the qa2 (catabolic dehydroquinase) gene of Neurospora crassa [8].

Chemical compound and disease context of aroD

• A virulent Shigella flexneri serotype Y strain, SFL1, was made auxotrophic for aromatic metabolites, including p-aminobenzoic acid, which is not available in mammalian tissues, by transduction of a Tn10-inactivated aroD gene from Escherichia coli K-12 NK5131 [9].
• 5. The enzymes quinate dehydrogenase and 3-dehydroquinase have previously been overproduced in Escherichia coli, and protocols for their purification published [10].

Biological context of aroD

• The presence of an aroD deletion does not interfere with expression of an invasive phenotype; however, in bacteria containing a functional kcpA gene, replication and spread by invading bacteria are limited, preventing development of the plaque-positive phenotype [11].
• Expression of hybrid lipopolysaccharide and deletion of aroD resulted in the attenuation of phenotypic characteristics associated with pathogenicity [11].
• Initial mapping experiments located the autolysin gene near aroD on the B. subtilis 168 chromosome [12].
• A 5.6-kb PstI fragment containing the structural gene (aroD) for 5-dehydroquinate hydrolyase (DHQase) of Escherichia coli K-12 has been cloned into recombinant plasmid pJKK12 [13].
• The overexpression and complete amino acid sequence of Escherichia coli 3-dehydroquinase [14].

Associations of aroD with chemical compounds

• The presence of shikimic acid in the growth medium restores the ability of an aroD mutant to synthesize cmo5U, while O-succinylbenzoate, which is an early intermediate in the synthesis of menaquinone, does not [15].
• The addition of an aroD deletion results in a requirement for an aromatic precursor of para-aminobenzoic acid (PABA), an essential bacterial metabolite not present in mammalian tissues [11].
• The tetracycline-sensitive derivatives of Tn10 mutants obtained were selected on Bochner's medium and checked by DNA-DNA hybridization using aroA and aroD gene specific probes [2].
• A stable mutation was introduced into the aroD gene of S. typhimurium C5 [4].
• Additionally we have overproduced and purified the qutB-encoded quinate dehydrogenase and overproduced the qa-2 encoded type II 3-dehydroquinase of Neurospora crassa [16].

Other interactions of aroD

• Subfragments of the Arom locus encoding EPSP synthase and 3-dehydroquinase have been expressed in appropriate E. coli aro mutants [17].

Analytical, diagnostic and therapeutic context of aroD

• Southern blot analysis of a cosmid library identified several potential clones, one of which complemented an Escherichia coli aroD point mutant strain deficient in host dehydroquinase [18].
• Crystallization of a type I 3-dehydroquinase from Salmonella typhi [19].
• Molecular cloning and characterization of the aroD gene encoding 3-dehydroquinase from Salmonella typhi [3].

References