Disease relevance of asd

• Nucleotide sequence of the asd gene of Escherichia coli: absence of a typical attenuation signal [1].
• The coding regions for the Escherichia coli gene for aspartokinase I/homoserine dehydrogenase I (thrA) and the Corynebacterium glutamicum gene for aspartic semialdehyde dehydrogenase (asd) have been subcloned into a Simian Virus 40 (SV40)-based mammalian expression vector [2].
• Cloning and characterization of the Neisseria meningitidis asd gene [3].
• An asd-complementing mini-Tn5 transposon was constructed for random insertion of the Escherichia coli LT enterotoxin genes (elt) into the genome of Deltaasd attenuated strains of Salmonella typhimurium [4].
• Aspartate beta-D-semialdehyde dehydrogenase genes (asd) were cloned and sequenced from a deep-sea-adapted strictly barophilic bacterium, Shewanella sp. strain DB6705, and a moderately barophilic bacterium, Shewanella sp. strain DSS12 [5].

High impact information on asd

• Hence the expression of the asd gene is probably not controlled in the same way as other multivalently repressed operons such as ilva and thr [1].
• The asd gene of escherichia coli encodes aspartic semialdehyde dehydrogenase, an enzyme involved in lysine, threonine, and methionine biosynthesis; its synthesis is controlled by a multivalent repression mechanism [1].
• Active site analysis of the potential antimicrobial target aspartate semialdehyde dehydrogenase [6].
• Malonyl-CoA reductase has 38% amino acid sequence identity to aspartate-semialdehyde dehydrogenase, suggesting a common ancestor for both proteins [7].
• Many different L. pneumophila loci are able to transform L. pneumophila after addition of plasmid DNA, including gspA, ppa, asd, and pilEL [8].

Chemical compound and disease context of asd

• The first two genes of the lysine pathway are closely linked forming a transcriptional operon in the cephamycin producer 'Amycolatopsis lactamdurans'. The asd gene, encoding the enzyme aspartic semialdehyde dehydrogenase, has been cloned by complementation of Escherichia coli asd mutants [9].
• The transport and phosphorylation of gluconate in E. coli occurs through two systems (GntI and GntII) which duplicate activities. bioH-asd deletion mutants do not grow on media with gluconate as sole carbon source because they lack the GntI system and do not express GntII [10].
• Cloning and nucleotide sequence of the Bacillus subtilis hom gene coding for homoserine dehydrogenase. Structural and evolutionary relationships with Escherichia coli aspartokinases-homoserine dehydrogenases I and II [11].
• With E. coli W7, a dap lys mutant generally used in this kind of studies, steady-state incorporation was reached only after about 0.75 of the doubling time [12].
• As part of an attempt to develop a semi-in vitro system of lysogenic induction, using spheroplasts of Escherichia coli K-12 lysogenic for prophage lambda, we prepared spheroplasts by depriving E. coli dap of diaminopimelic acid (DAP-spheroplasts) [13].

Biological context of asd

• The thrA and asd expression cassettes were combined into a single plasmid which, when transfected into 3T3 cells, enabled them to produce homoserine from aspartic acid [2].
• By subcloning and insertion mutagenesis, the N. meningitidis asd was localized to a 1.5-kb DNA fragment [3].
• The V. cholerae genome contains two asd genes [14].
• The amino acid sequence of the Asd protein exhibits significant homology to asd gene products from other microorganisms [15].
• Sequence analysis revealed that the homdr mutation is a single nucleotide (G1964) deletion in codon 429 within the hom reading frame [16].

Anatomical context of asd

• The asd mutants of Gram- and some Gram+ bacteria have an obligate requirement for diaminopimelic acid (DAP), an essential constituent of the cell wall of these organisms [3].
• To transfer genes into airway epithelial cells, we have generated auxotrophic dap Escherichia coli BM2710 mutant that expresses the invasin of Yersinia pseudotuberculosis and the listeriolysin of Listeria monocytogenes [17].

Associations of asd with chemical compounds

• Treatment with chloramphenicol (CAM) did not alter the size distributions of either rel+ or relA- strains except when they were rel+ dap-. CAM treatment of rel+ dap- strains resulted in an increase in cell size [18].

Other interactions of asd

• The aspartate semialdehyde dehydrogenase, dihydrodipicolinate synthase and dihydrodipicolinate reductase were not regulated by the end-products of the pathway [19].

References