Studies on Acetone-Glyceraldehyde. VII. Preparation of <i>l</i>-Glyceraldehyde and <i>l</i>(-)Acetone Glycerol

Baer, Erich; Fischer, Hermann O. L.

doi:10.1021/ja01873a001

Cited by 109 publications

(30 citation statements)

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“…Product was shown to be free from contaminants by HPLC and 1 H NMR spectroscopy, and its enantiomeric purity was assessed by polarimetry. The determined optical rotation, [␣] D 25 ϭ ϩ9.75°(c ϭ 2, H 2 O), was well within the reported range of ϩ7°to ϩ14° (34). The enantiomeric purity was further confirmed by derivatization with L-(Ϫ)-␣-methylbenzylamine, which yielded diastereometrically pure (S,S)-3-(1-phenylethylamine)propane-1,2-diol, as assessed by 1 H NMR spectroscopy.…”

Section: Resultssupporting

confidence: 68%

Metabolic Pathway Promiscuity in the Archaeon Sulfolobus solfataricus Revealed by Studies on Glucose Dehydrogenase and 2-Keto-3-deoxygluconate Aldolase

Lamble

Heyer

Bull

et al. 2003

Journal of Biological Chemistry

137

206

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The hyperthermophilic Archaeon Sulfolobus solfataricus metabolizes glucose by a non-phosphorylative variant of the Entner-Doudoroff pathway. In this pathway glucose dehydrogenase and gluconate dehydratase catalyze the oxidation of glucose to gluconate and the subsequent dehydration of gluconate to 2-keto-3-deoxygluconate. 2-Keto-3-deoxygluconate (KDG) aldolase then catalyzes the cleavage of 2-keto-3-deoxygluconate to glyceraldehyde and pyruvate. The gene encoding glucose dehydrogenase has been cloned and expressed in Escherichia coli to give a fully active enzyme, with properties indistinguishable from the enzyme purified from S. solfataricus cells. Kinetic analysis revealed the enzyme to have a high catalytic efficiency for both glucose and galactose. KDG aldolase from S. solfataricus has previously been cloned and expressed in E. coli. In the current work its stereoselectivity was investigated by aldol condensation reactions between D-glyceraldehyde and pyruvate; this revealed the enzyme to have an unexpected lack of facial selectivity, yielding approximately equal quantities of 2-keto-3-deoxygluconate and 2-keto-3-deoxygalactonate. The KDG aldolase-catalyzed cleavage reaction was also investigated, and a comparable catalytic efficiency was observed with both compounds. Our evidence suggests that the same enzymes are responsible for the catabolism of both glucose and galactose in this Archaeon. The physiological and evolutionary implications of this observation are discussed in terms of catalytic and metabolic promiscuity.The hyperthermophilic Archaeon Sulfolobus solfataricus grows optimally at 80 -85°C and pH 2-4, utilizing a wide range of carbon and energy sources (1). It has become one of the most comprehensively researched model organisms of archaeal metabolism and bioenergetics (2). Central metabolism in this organism involves a modified Entner-Doudoroff pathway (3), production of acetyl-CoA by pyruvate:ferredoxin oxidoreductase (4), and the citric acid cycle coupled to oxidative phosphorylation (5). The modified Entner-Doudoroff pathway is a nonphosphorylative variant of the classic pathway and proceeds with no net production of ATP (Fig. 1). An analogous pathway has also been detected in the thermoacidophilic Archaea Sulfolobus acidocaldarius (6), Thermoplasma acidophilum (7), and Thermoproteus tenax (8), as well as strains of Aspergillus fungi (9, 10).The first reaction of the non-phosphorylative Entner-Doudoroff pathway involves the NAD(P)-dependent oxidation of glucose to gluconate, catalyzed by glucose dehydrogenase. Gluconate is then dehydrated by gluconate dehydratase to 2-keto-3-deoxygluconate (KDG), 1 which undergoes an aldolate cleavage to pyruvate and glyceraldehyde, catalyzed by KDG aldolase. Glyceraldehyde dehydrogenase then oxidizes glyceraldehyde to glycerate, which is phosphorylated by glycerate kinase to give 2-phosphoglycerate. A second molecule of pyruvate is produced from this by the actions of enolase and pyruvate kinase.Glucose dehydrogenase has previously been purified to homogenei...

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Section: Resultssupporting

confidence: 68%

Metabolic Pathway Promiscuity in the Archaeon Sulfolobus solfataricus Revealed by Studies on Glucose Dehydrogenase and 2-Keto-3-deoxygluconate Aldolase

Lamble

Heyer

Bull

et al. 2003

Journal of Biological Chemistry

137

206

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“…Fischer and co-workers (Baer and Fischer, 1941;Baer et al, 1944) were the first to prepare batyl, chimyl and selachyl alcohols, and their antipodes, enantiomerically pure by using the chiral C 3 -synthons, (S)-1,2-O-isopropylidene-sn-glycerol obtained from D-mannitol, and (R)-2,3-O-isopropylidene-sn-glycerol prepared from L-arabinose (Baer and Fischer, 1939a). Knowing the predetermined stereochemistry of the synthetic compounds and their optical rotations, they were capable to determine the Sconfiguration of the naturally occurring 1-O-alkyl-sn-glycerols.…”

Section: Chemical Synthesismentioning

confidence: 99%

“…They assumed that 1-O-alkylglycerol can be formed by chemical interconversion of 1-O-alkyl-D-glyceraldehyde, without severing the bonds to the stereogenic carbon atom, by reduction. Since, 1-O-alkyl-D-glyceraldehyde is in turn homofacial with D-(+)-glyceraldehyde, this implying that the naturally occurring 1-O-alkylglycerols belong to the D-series and therefore exhibit the configuration shown in Scheme 3 (Baer and Fischer, 1939b).…”

Section: Isolation Identification and Structural Elucidationmentioning

confidence: 99%

Ether lipids

Magnusson

Haraldsson

2011

Chemistry and Physics of Lipids

124

119

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The naturally occurring 1-O-alkyl-sn-glycerols and their methoxylated congeners, 1-O-(2'-methoxyalkyl)-sn-glycerols, are biologically active compounds, ubiquitously found in nature as diacyl glyceryl ether lipids and phosphoether lipids. The chief objective of this article is to provide a comprehensive and up to date review on such ether lipids. The occurrence and distribution of these compounds in nature are extensively reviewed, their chemical structure and molecular variety, their biosynthesis and chemical synthesis and, finally, their various biological effects are described and discussed. An unprecedented biosynthesis of the 2'-methoxylated alkylglycerols is proposed. The first synthesis of enantiopure (Z)-(2'R)-1-O-(2'-methoxyhexadec-4'-enyl)-sn-glycerol, the most prevalent 2'-methoxylated type alkylglycerol present in cartilaginous fish, is described. It was accomplished by a highly convergent five step process.

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“…Recently, it has been successfully used in the synthesis of, for example, enantiopure 4-(dihydroxyalkyl)-b-lactams (antibiotic) (Areces et al, 2007) or 8a-epi-swainsoine (anticancer drug; Bi and Aggarwal, 2008). Both glyceraldehyde enantiomers have been synthesized chemically by different approaches starting from chiral pool compounds (Andrews et al, 1981;Baer and Fischer, 1939;Hubschwerlen, 1986;Hubschwerlen et al, 1995;Jurczak et al, 1986;Schmid and Bryant, 1995). The step economy and accumulated waste streams of the existing procedures are however not very favourable for industrial applications despite the achieved yields of the individual steps.…”

Section: Introductionmentioning

confidence: 99%

Characterization of a whole‐cell catalyst co‐expressing glycerol dehydrogenase and glucose dehydrogenase and its application in the synthesis of L‐glyceraldehyde

Richter¹,

Neumann²,

Liese³

et al. 2010

Biotech & Bioengineering

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A whole-cell catalyst using Escherichia coli BL21(DE3) as a host, co-expressing glycerol dehydrogenase (GlyDH) from Gluconobacter oxydans and glucose dehydrogenase (GDH) from Bacillus subtilis for cofactor regeneration, has been successfully constructed and used for the reduction of aliphatic aldehydes, such as hexanal or glyceraldehyde to the corresponding alcohols. This catalyst was characterized in terms of growth conditions, temperature and pH dependency, and regarding the influence of external cofactor and permeabilization. In the case of external cofactor addition we found a 4.6-fold increase in reaction rate caused by the addition of 1 mM NADP(+). Due to the fact that pH and temperature are also factors which may affect the reaction rate, their effect on the whole-cell catalyst was studied as well. Comparative studies between the whole-cell catalyst and the cell-free system were investigated. Furthermore, the successful application of the whole-cell catalyst in repetitive batch conversions could be demonstrated in the present study. Since the GlyDH was recently characterized and successfully applied in the kinetic resolution of racemic glyceraldehyde, we were now able to transfer and establish the process to a whole-cell system, which facilitated the access to L-glyceraldehyde in high enantioselectivity at 54% conversion. All in all, the whole-cell catalyst shows several advantages over the cell-free system like a higher thermal, a similar operational stability and the ability to recycle the catalyst without any loss-of-activity. The results obtained making the described whole-cell catalyst an improved catalyst for a more efficient production of enantiopure L-glyceraldehyde.

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Studies on Acetone-Glyceraldehyde. VII. Preparation of l-Glyceraldehyde and l(-)Acetone Glycerol

Cited by 109 publications

References 0 publications

Metabolic Pathway Promiscuity in the Archaeon Sulfolobus solfataricus Revealed by Studies on Glucose Dehydrogenase and 2-Keto-3-deoxygluconate Aldolase

Metabolic Pathway Promiscuity in the Archaeon Sulfolobus solfataricus Revealed by Studies on Glucose Dehydrogenase and 2-Keto-3-deoxygluconate Aldolase

Ether lipids

Characterization of a whole‐cell catalyst co‐expressing glycerol dehydrogenase and glucose dehydrogenase and its application in the synthesis of L‐glyceraldehyde

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