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Gene Review:

araA - L-arabinose isomerase

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK0063, JW0061

Jørgensen, F. et al., Kim, H.J. et al., Heffernan, L. et al., Lee, D.W. et al., Wallace, L.J. et al., et al.

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Disease relevance of araA

The nucleotide sequence of gene araA of Salmonella typhimurium LT2 has been determined [1].
The araA gene encoding L-arabinose isomerase (AI) from the hyperthermophilic bacterium Thermotoga maritima was cloned and overexpressed in Escherichia coli as a fusion protein containing a C-terminal hexahistidine sequence [2].
Enzymatic conversion of D-galactose to D-tagatose: heterologous expression and characterisation of a thermostable L-arabinose isomerase from Thermoanaerobacter mathranii [3].

High impact information on araA

L-Arabinose isomerase, EC 5.3.1.4, catalyzes the conversion of L-arabinose to L-ribulose, the first step in the catabolism of L-arabinose by Escherichia coli B/r. Patrick and Lee (1969) J [4].
Escherichia coli L-arabinose isomerase (ECAI; EC 5.3.1.4) catalyzes the isomerization of L-arabinose to L-ribulose in vivo [5].
The araCi protein differs in stability from araC+ protein and alters the concentration of cyclic adenosine-3', 5'-monophosphate required to maximally stimulate L-arabinose isomerase synthesis in an in vitro protein-synthesizing system [6].
The initial differential rates of synthesis of L-arabinose isomerase, the product of the araA gene, were determined for the Ara+, plasmid containing strains [7].
Characterization of a mutated Geobacillus stearothermophilus L-arabinose isomerase that increases the production rate of D-tagatose [8].

Chemical compound and disease context of araA

Tagatose production by immobilized recombinant Escherichia coli cells containing Geobacillus stearothermophilus l-arabinose isomerase mutant in a packed-bed bioreactor [9].

Biological context of araA

Amino acid sequence comparisons indicated that this enzyme is only distantly related to the group of previously known araA sequences in which the sequence similarity is evident [3].
The substrate specificity and the Michaelis-Menten constants of the enzyme determined with L-arabinose, D-galactose and D-fucose also indicated that this enzyme is an unusual, versatile L-arabinose isomerase which is able to isomerise structurally related sugars [3].

Associations of araA with chemical compounds

The ability to convert D-galactose into D-tagatose was compared among a number of bacterial L-arabinose isomerases ( araA) [3].
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].
Direct conversion of lactose to D-tagatose in a single reactor was demonstrated using a thermostable beta-galactosidase together with the thermostable L-arabinose isomerase [3].

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].

References

The araBAD operon of Salmonella typhimurium LT2. II. Nucleotide sequence of araA and primary structure of its product, L-arabinose isomerase. Lin, H.C., Lei, S.P., Wilcox, G. Gene (1985) [Pubmed]
Characterization of a thermostable L-arabinose (D-galactose) isomerase from the hyperthermophilic eubacterium Thermotoga maritima. Lee, D.W., Jang, H.J., Choe, E.A., Kim, B.C., Lee, S.J., Kim, S.B., Hong, Y.H., Pyun, Y.R. Appl. Environ. Microbiol. (2004) [Pubmed]
Enzymatic conversion of D-galactose to D-tagatose: heterologous expression and characterisation of a thermostable L-arabinose isomerase from Thermoanaerobacter mathranii. Jørgensen, F., Hansen, O.C., Stougaard, P. Appl. Microbiol. Biotechnol. (2004) [Pubmed]
The shape of L-arabinose isomerase from Escherichia coli. Wallace, L.J., Eiserling, F.A., Wilcox, G. J. Biol. Chem. (1978) [Pubmed]
Crystal structure of Escherichia coli L-arabinose isomerase (ECAI), the putative target of biological tagatose production. Manjasetty, B.A., Chance, M.R. J. Mol. Biol. (2006) [Pubmed]
Effect of araC gene product on catabolite repression in the L-arabinose regulon. Heffernan, L., Wilcox, G. J. Bacteriol. (1976) [Pubmed]
Regulation of the L-arabinose operon in strains of Escherichia coli containing ColE1-ara hybrid plasmids. Wallace, L.J., Wilcox, G. Mol. Gen. Genet. (1979) [Pubmed]
Characterization of a mutated Geobacillus stearothermophilus L-arabinose isomerase that increases the production rate of D-tagatose. Kim, H.J., Kim, J.H., Oh, H.J., Oh, D.K. J. Appl. Microbiol. (2006) [Pubmed]
Tagatose production by immobilized recombinant Escherichia coli cells containing Geobacillus stearothermophilus l-arabinose isomerase mutant in a packed-bed bioreactor. Jung, E.S., Kim, H.J., Oh, D.K. Biotechnol. Prog. (2005) [Pubmed]

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