Enzymes
| UniProtKB help_outline | 3,138 proteins |
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- Name help_outline D-lyxose Identifier CHEBI:16789 (CAS: 1114-34-7) help_outline Charge 0 Formula C5H10O5 InChIKeyhelp_outline PYMYPHUHKUWMLA-UOWFLXDJSA-N SMILEShelp_outline OC[C@@H](O)[C@H](O)[C@H](O)C=O 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline D-xylulose Identifier CHEBI:17140 (CAS: 551-84-8) help_outline Charge 0 Formula C5H10O5 InChIKeyhelp_outline ZAQJHHRNXZUBTE-WUJLRWPWSA-N SMILEShelp_outline C(O)C(=O)[C@@H](O)[C@H](O)CO 2D coordinates Mol file for the small molecule Search links Involved in 6 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:14201 | RHEA:14202 | RHEA:14203 | RHEA:14204 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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PURIFICATION AND CHARACTERIZATION OF D-LYXOSE ISOMERASE.
ANDERSON R.L., ALLISON D.P.
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Characterization of a novel D-lyxose isomerase from Cohnella laevoribosii RI-39 sp. nov.
Cho E.-A., Lee D.-W., Cha Y.-H., Lee S.-J., Jung H.-C., Pan J.-G., Pyun Y.-R.
A newly isolated bacterium, Cohnella laevoribosii RI-39, could grow in a defined medium with L-ribose as the sole carbon source. A 21-kDa protein isomerizing L-ribose to L-ribulose, as well as D-lyxose to D-xylulose, was purified to homogeneity from this bacterium. Based on the N-terminal and inte ... >> More
A newly isolated bacterium, Cohnella laevoribosii RI-39, could grow in a defined medium with L-ribose as the sole carbon source. A 21-kDa protein isomerizing L-ribose to L-ribulose, as well as D-lyxose to D-xylulose, was purified to homogeneity from this bacterium. Based on the N-terminal and internal amino acid sequences of the purified enzyme obtained by N-terminal sequencing and quantitative time of flight mass spectrometry-mass spectrometry analyses, a 549-bp gene (lyxA) encoding D-lyxose (L-ribose) isomerase was cloned and expressed in Escherichia coli. The purified endogenous enzyme and the recombinant enzyme formed homodimers that were activated by Mn(2+). C. laevoribosii D-lyxose (L-ribose) isomerase (CLLI) exhibits maximal activity at pH 6.5 and 70 degrees C in the presence of Mn(2+) for D-lyxose and L-ribose, and its isoelectric point (pI) is 4.2 (calculated pI, 4.9). The enzyme is specific for D-lyxose, L-ribose, and D-mannose, with apparent K(m) values of 22.4 +/- 1.5 mM, 121.7 +/-10.8 mM, and 34.0 +/-1.1 mM, respectively. The catalytic efficiencies (k(cat)/K(m)) of CLLI were 84.9 +/-5.8 mM(-1) s(-1) for D-lyxose (V(max), 5,434.8 U mg(-1)), 0.2 mM(-1) s(-1) for L-ribose (V(max), 75.5 +/- 6.0 U mg(-1)), and 1.4 +/-0.1 mM(-1) s(-1) for D-mannose (V(max), 131.8 +/-7.4 U mg(-1)). The ability of lyxA to permit E. coli cells to grow on D-lyxose and L-ribose and homology searches of other sugar-related enzymes, as well as previously described sugar isomerases, suggest that CLLI is a novel type of rare sugar isomerase. << Less