Characterization of a Novel
            <scp>d</scp>
            -Lyxose Isomerase from
            <i>Cohnella laevoribosii</i>
            RI-39 sp. nov

Cho, Eun Ah; Lee, Dong Woo; Hwan, Yun; Lee, Sang Jae; Jung, Heung-Chae; Pan, Jae-Gu; Pyun, Yu‐Ryang

doi:10.1128/jb.01568-06

Cited by 50 publications

(51 citation statements)

References 51 publications

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“…The specific activity of L-ribose isomerase from an Acinetobacter sp. followed the order L-ribose Ͼ D-lyxose Ͼ D-mannose, whereas the specific activity of D-lyxose isomerase from C. laeviribosi followed the order D-lyxose Ͼ D-mannose Ͼ L-ribose (3,9). No activity was found from the two enzymes for D-talose, L-allose, D-ribose, L-talose, D-allose, L-lyxose, and L-mannose, demonstrating the different substrate specificities of the B. subtilis mannose-6-phosphate isomerase.…”

Section: Resultsmentioning

confidence: 96%

“…L-Ribulose has been biochemically converted from L-ribose using an Lribose isomerase from an Acinetobacter sp. (9), an L-arabinose isomerase mutant from Escherichia coli (4), a D-xylose isomerase mutant from Actinoplanes missouriensis (14), and a D-lyxose isomerase from Cohnella laeviribosi (3), indicating that L-ribose can be produced from L-ribulose by these enzymes. However, the enzymatic production of L-ribulose is slow, and the enzymatic production of L-ribose from L-ribulose has been not reported.…”

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confidence: 99%

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Substrate Specificity of a Mannose-6-Phosphate Isomerase from Bacillus subtilis and Its Application in the Production of l -Ribose

Yeom

Kim

et al. 2009

Appl Environ Microbiol

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The uncharacterized gene previously proposed as a mannose-6-phosphate isomerase from Bacillus subtilis was cloned and expressed in Escherichia coli. The maximal activity of the recombinant enzyme was observed at pH 7.5 and 40°C in the presence of 0.5 mM Co 2؉ . The isomerization activity was specific for aldose substrates possessing hydroxyl groups oriented in the same direction at the C-2 and C-3 positions, such as the D and L forms of ribose, lyxose, talose, mannose, and allose. The enzyme exhibited the highest activity for L-ribulose among all pentoses and hexoses. Thus, L-ribose, as a potential starting material for many L-nucleoside-based pharmaceutical compounds, was produced at 213 g/liter from 300-g/liter L-ribulose by mannose-6-phosphate isomerase at 40°C for 3 h, with a conversion yield of 71% and a volumetric productivity of 71 g liter ؊1 h ؊1 .L-Ribose is a potential starting material for the synthesis of many L-nucleoside-based pharmaceutical compounds, and it is not abundant in nature (5, 19). L-Ribose has been produced mainly by chemical synthesis from L-arabinose, L-xylose, Dglucose, D-galactose, D-ribose, or D-mannono-1,4-lactone (2,17,23). Biological L-ribose manufacture has been investigated using ribitol or L-ribulose. Recently, L-ribose was produced from ribitol by a recombinant Escherichia coli containing an NAD-dependent mannitol-1-dehydrogenase (MDH) with a 55% conversion yield when 100 g/liter ribitol was used in a 72-h fermentation (18). However, the volumetric productivity of L-ribose in the fermentation is 28-fold lower than that of the chemical method synthesized from L-arabinose (8). L-Ribulose has been biochemically converted from L-ribose using an Lribose isomerase from an Acinetobacter sp. (9), an L-arabinose isomerase mutant from Escherichia coli (4), a D-xylose isomerase mutant from Actinoplanes missouriensis (14), and a D-lyxose isomerase from Cohnella laeviribosi (3), indicating that L-ribose can be produced from L-ribulose by these enzymes. However, the enzymatic production of L-ribulose is slow, and the enzymatic production of L-ribose from L-ribulose has been not reported.Sugar phosphate isomerases, such as ribose-5-phosphate isomerase, glucose-6-phosphate isomerase, and galactose-6-phosphate isomerase, work as general aldose-ketose isomerases and are useful tools for producing rare sugars, because they convert the substrate sugar phosphates and the substrate sugars without phosphate to have a similar configuration (11,12,21,22). L-Ribose isomerase from an Acinetobacter sp. (9) and D-lyxose isomerase from C. laeviribosi (3) had activity with L-ribose, D-lyxose, and D-mannose. Thus, we can apply mannose-6-phosphate (EC 5.3.1.8) isomerase to the production of L-ribose, because there are no sugar phosphate isomerases relating to L-ribose and D-lyxose. The production of the expensive sugar L-ribose (bulk price, $1,000/kg) from the rare sugar L-ribulose by mannose-6-phosphate isomerase may prove to be a valuable industrial process, because we have produced Lribulose from the ch...

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Section: Resultsmentioning

confidence: 96%

mentioning

confidence: 99%

Substrate Specificity of a Mannose-6-Phosphate Isomerase from Bacillus subtilis and Its Application in the Production of l -Ribose

Yeom

Kim

et al. 2009

Appl Environ Microbiol

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“…It is possible that YdaE BL uses the same mechanism of action, but its true function needs to be confirmed. YdaE BL shows 58 and 76% similarity, respectively, to the characterized lyxose isomerase of C. laevoribosii (8) and an uncharacterized probable D-lyxose isomerase of Bacillus subtilis (GenBank accession no. BAA19258).…”

Section: Discussionmentioning

confidence: 99%

“…(5,8,23,25). Mannose isomerases of Agrobacterium radiobacter and Mycobacterium smegmatis have been proposed for the catalysis of lyxose and mannose to xylulose and fructose, respectively, but their efficiency with lyxose is lower than that with mannose (14,15).…”

mentioning

confidence: 99%

“…The uncharacterized hypothetical protein ydaE (GenBank accession no. AAU22106) of Bacillus licheniformis shows 58% amino acid similarity to the thermophilic C. laevoribosii lyxose isomerase (8). Bacillus licheniformis, a nonpathogenic, sporeforming organism that has been utilized extensively in biotechnological applications (30), has an efficient extracellular polysaccharide-digesting capacity and is able to survive on a variety of carbon sources (36).…”

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confidence: 99%

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Substrate Specificity of the Bacillus licheniformis Lyxose Isomerase YdaE and Its Application in In Vitro Catalysis for Bioproduction of Lyxose and Glucose by Two-Step Isomerization

Patel

Lee

et al. 2011

Appl Environ Microbiol

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Production of d‐mannose from d‐glucose by co‐expression of d‐glucose isomerase and d‐lyxose isomerase in Escherichia coli

Huang

Zhang

et al. 2018

J Sci Food Agric

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Characterization of a Novel d -Lyxose Isomerase from Cohnella laevoribosii RI-39 sp. nov

Cited by 50 publications

References 51 publications

Substrate Specificity of a Mannose-6-Phosphate Isomerase from Bacillus subtilis and Its Application in the Production of l -Ribose

Substrate Specificity of a Mannose-6-Phosphate Isomerase from Bacillus subtilis and Its Application in the Production of l -Ribose

Substrate Specificity of the Bacillus licheniformis Lyxose Isomerase YdaE and Its Application in In Vitro Catalysis for Bioproduction of Lyxose and Glucose by Two-Step Isomerization

Production of d‐mannose from d‐glucose by co‐expression of d‐glucose isomerase and d‐lyxose isomerase in Escherichia coli

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