Disease relevance of dl-Lyxose

• Chemistry of the lyxose-containing mycobacteriophage receptors of Mycobacterium phlei/Mycobacterium smegmatis [1].
• Results are presented which show that the D-xylose isomerases present in Streptomyces olivaceus and Streptomyces phaeochromogenes NRRL B-3559 are incapable of utilizing D-lyxose as a substrate [2].
• Growth on D-lyxose of a mutant strain of Escherichia coli K12 using a novel isomerase and enzymes related to D-xylase metabolism [3].
• The isomerization of L-erythrulose to L-erythrose was carried out using constitutively produced L-ribose isomerase (l-RI) from the mutant strain Acinetobacter sp. DL-28 grown on D-lyxose mineral salt medium [4].

High impact information on dl-Lyxose

• Glucokinase exhibited an ATPase activity which was 1/2000th that of the rate of the kinase reaction, and unlike yeast hexokinase, it was not affected by the addition of lyxose [5].
• This glucose-induced conformational state had an increased ability to bind metal-ATP ligands; however, the relative changes in the dissociation constants for the various metal-ATP ligands differ from those observed with hexokinase in the presence of lyxose [6].
• Adaptation of yeast torulopsis candida to D-arabinose, D-lyxose and L-oxylose is shown to be due to the appearance of a new enzyme which catalyzes the reduction of these pentoses to D-arabitol and xylitol, respectively [7].
• Acid hydrolysis afforded D-lyxose [8].
• The purified enzyme had an optimum pH at 8.0, an optimum temperature at 60 degrees C, a pI of 5.2 and a Km of 20 mM, and specifically converted D-mannose and D-lyxose to ketose [9].

Associations of dl-Lyxose with other chemical compounds

• Yeast hexokinase A(ATP:D-hexose 6-phosphotransferase) is inactivated when incubated in the presence of xylose and ATPMg, or in the presence of D-lyxose in a reaction medium in which ATPMg is being continuously regenerated (phosphoenolpyruvate and pyruvate kinase) [10].

Gene context of dl-Lyxose

• The binding of five-carbon sugar inhibitors such as lyxose induced a conformational state of hexokinase that demonstrated a small quenching of 2,6-TNS fluorescence but an increased ability to bind metal-ligands when compared to free enzyme [6].
• A second-stage mutant of Escherichia coli K12 designated as strain 806 grew faster on D-lyxose than the mutant strain 805 previously described [11].

Analytical, diagnostic and therapeutic context of dl-Lyxose

• The product was crystallized and was confirmed to be D-lyxose by HPLC, 13C-NMR spectra, IR spectra analysis, and optical rotation measurement [12].

References