Disease relevance of C02022

• Thermotolerant Gluconobacter frateurii CHM 43 was selected for L-erythrulose production from mesoerythritol at higher temperatures [1].

High impact information on C02022

• In vivo, ATP is apparently consumed with the accumulation of D-erythrulose 1-phosphate (D-glycero-2-tetrulose 1-phosphate) and no substrate level phosphorylation [2].
• As a result, the one-substrate transketolase reaction product, erythrulose, is formed [3].
• The phylogenic analysis of D-erythrulose reductase and the other related proteins suggests that the protein described as a carbonyl reductase D-erythrulose reductase [4].
• Enzymatic determination of D-erythrulose made use of the D-erythrulose reductase purified from beef or chicken liver, which catalyzes specifically the reduction of D-erythrulose with concomitant conversion of NADH to NAD+ [5].
• After dephosphorylation, the presence of D-erythrulose and D-threose was confirmed by thin-layer chromatography, gas-liquid chromatography and an enzymatic method depending upon D-erythrulose reductase [6].

Biological context of C02022

• Modeling of reaction kinetics for reactor selection in the case of L-erythrulose synthesis [7].
• The research of the substrate specificity in the reductive reaction demonstrated that L-erythrulose and dihydroxyacetone were better substrates, that D-acetoin was inactive and L-erythrose (aldose) was slightly active [8].
• The degradation of vitamin C in mammals is initiated by the hydrolysis of dehydroascorbate to 2,3-diketo-l-gulonate, which is spontaneously degraded to oxalate, CO(2) and l-erythrulose [9].

Associations of C02022 with other chemical compounds

• The first reaction in the pathway was the phosphorylation of mesoerythritol with an ATP-dependent kinase which formed d-erythritol 1-phosphate (d-erythro-tetritol 1-phosphate). d-Erythritol 1-phosphate was oxidized by an NAD-dependent dehydrogenase to d-erythrulose 1-phosphate (d-glycero-2-tetrulose 1-phosphate) [10].

Gene context of C02022

• With the example of the transketolase catalyzed L-erythrulose synthesis we demonstrate how the most effective reactor mode can be determined by kinetic simulations [7].

Analytical, diagnostic and therapeutic context of C02022

• From the gas chromatography/mas spectrometry analyses of the enzymatic reaction products, it appeared that about 90% of the total amount of tetrose 4-phosphate was present as D-erythrulose 4-phosphate after equilibration [11].
• Studies on D-tetrose metabolism. VI. Crystallization and some properties of D-erythrulose reducatase from beef liver [12].

References