Disease relevance of araA

• The constructed plasmids were named pTC101, pTC105 and pTC106, containing araA from E. coli, B. subtilis and S. typhimurium respectively [1].
• The araA gene encoding L-arabinose isomerase from Bacillus stearothermophilus US100 strain was cloned, sequenced and over-expressed in E. coli [2].
• Cloning and characterization of araA, araB, and araD, the structural genes for L-arabinose utilization in Bacillus subtilis [3].
• Cloning, expression and characterization of L-arabinose isomerase from Thermotoga neapolitana: bioconversion of D-galactose to D-tagatose using the enzyme [4].
• The deduced amino acid sequence has 94.8% identical amino acids compared with the residues in a putative L-arabinose isomerase of Thermotoga maritima [4].

High impact information on araA

• Escherichia coli L-arabinose isomerase (ECAI; EC 5.3.1.4) catalyzes the isomerization of L-arabinose to L-ribulose in vivo [5].
• Expression of the ara operon is directed by a strong sigma A-like promoter identified within a 150 bp DNA fragment upstream from the translation start site of araA [6].
• Cyclic AMP partially reversed the inhibitory effect on L-arabinose isomerase induction produced immediately after irradiation by all gamma-ray doses (up to 30 krad), but the enhanced inhibitory effect caused by induction in cells irradiated at higher doses could not be reversed by the nucleotide [7].
• Characterization of a mutated Geobacillus stearothermophilus L-arabinose isomerase that increases the production rate of D-tagatose [8].
• SIGNIFICANCE AND IMPACT OF THE STUDY: This work contributes knowledge on the characterization of a mutated L-arabinose isomerase, and allows an increased production rate for D-tagatose from D-galactose using the mutated enzyme [8].

Chemical compound and disease context of araA

• An L-arabinose isomerase of Escherichia coli was immobilized using covalent binding to agarose to produce D-tagatose, a bulking sweetener that can be economically used as a sugar substitute [9].
• Production of tagatose by a recombinant thermostable L-arabinose isomerase from Thermus sp. IM6501 [10].

Associations of araA with chemical compounds

• L-Arabinose isomerase (EC 5.3.1.4) catalyzes the isomerization of L-arabinose to L-ribulose [11].
• D-Tagatose production using an immobilized L-arabinose isomerase has a high potential for commercial application [9].
• Bioconversion of D-galactose into D-tagatose by expression of L-arabinose isomerase [1].
• Hyperinduction of L-arabinose isomerase was due to exogenous sodium chloride and the resulting alteration in the balance of the L-arabinose-metabolizing enzymes resulted in accumulation of L-Ru5P [12].

Analytical, diagnostic and therapeutic context of araA

• METHODS AND RESULTS: A mutated gene was obtained by an error-prone polymerase chain reaction using L-arabinose isomerase gene from G. stearothermophilus as a template and the gene was expressed in Escherichia coli [8].
• A feasible enzymatic process for D-tagatose production by an immobilized thermostable L-arabinose isomerase in a packed-bed bioreactor [13].

References