2001
DOI: 10.1016/s0167-4781(01)00290-1
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Cloning and characterization of a novel gene encoding ?-ribose isomerase from Acinetobacter sp. strain DL-28 in Escherichia coli

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Cited by 38 publications
(34 citation statements)
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“…The deduced amino acid sequence of CLLI exhibited no significant homology to any other sugar isomerase, including the RI from Acinetobacter sp. (30). However, a BLAST search with lyxA revealed that CLLI exhibited significant levels of sequence homology (Ն60%) with proteins from Bacillus species (Fig.…”
Section: Resultsmentioning
confidence: 97%
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“…The deduced amino acid sequence of CLLI exhibited no significant homology to any other sugar isomerase, including the RI from Acinetobacter sp. (30). However, a BLAST search with lyxA revealed that CLLI exhibited significant levels of sequence homology (Ն60%) with proteins from Bacillus species (Fig.…”
Section: Resultsmentioning
confidence: 97%
“…This enzyme is the first genetically identified isomerase that can catalyze the interconversion of D-lyxose to Dxylulose with a high specific activity. Although CLLI also converted D-mannose and L-ribose to D-fructose and L-ribulose, respectively, the amino acid sequence of the enzyme does not exhibit significant homology to MIs or RIs that can also isomerize D-lyxose (18,30). In addition, the substrate specificity of CLLI is different from the substrate specificities of MIs and RIs, suggesting that the enzyme is a novel LI.…”
Section: Discussionmentioning
confidence: 94%
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