One-pot four-enzyme synthesis of ketoses with fructose 1,6-bisphosphate aldolases from Staphylococcus carnosus and rabbit muscle

Li, Zijie; Cai, Li; Wei, Mohui; Wang, Peng George

doi:10.1016/j.carres.2012.05.007

Cited by 23 publications

(13 citation statements)

References 18 publications

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“…Myrcene also participated in homoallylation with N,O-acetal to produce the corresponding hydroxylamine 1n as a single product ( Table 2, entry 7). Glyceraldehyde is a triose monosaccharide generally used for the enzymatic synthesis of D-fructose and L-sorbose with aldolases [12]. The glyceraldehyde can serve as an important electrophilic component for coupling reactions to form a physiologically active molecules.…”

Section: Resultsmentioning

confidence: 99%

Ni-Catalyzed Homoallylation of Polyhydroxy N,O-Acetals with Conjugated Dienes Promoted by Triethylborane

et al. 2014

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Abstract:In the presence of Ni-catalyst and triethylborane, N,O-acetals prepared from glycolaldehyde and glyceraldehyde with primary amines in situ underwent homoallylation with conjugated dienes to provide 2-amino-5-hexenols in high regio-and stereoselectivity. Under similar reaction conditions, N,O-acetals from carbohydrates with primary amines provided the corresponding polyhydroxy-bishomoallylamines in good to reasonable yields.

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Section: Resultsmentioning

confidence: 99%

Ni-Catalyzed Homoallylation of Polyhydroxy N,O-Acetals with Conjugated Dienes Promoted by Triethylborane

et al. 2014

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“…For example, RhaD aldolase was used to catalyze the aldol reaction of DHAP to L-glyceraldehyde to form L-fructose-1-phosphate; the latter could remove the phosphate group by acid phosphatase (AP) to produce L-fructose (8). By using a similar strategy, L-tagatose could be synthesized with FucA aldolase and L-sorbose through FruA from rabbit muscle aldolase (RAMA) (6,17). However, another important rare ketohexose, L-psicose (3S, 4S), was scarcely produced in previous research by using aldolases.…”

Section: Dhap-dependent Aldolases Create Two New Stereogenic Centers mentioning

confidence: 99%

Biosynthesis of l -Sorbose and l -Psicose Based on C—C Bond Formation Catalyzed by Aldolases in an Engineered Corynebacterium glutamicum Strain

Yang

Men

et al. 2015

Appl Environ Microbiol

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The property of loose stereochemical control at aldol products from aldolases helped to synthesize multiple polyhydroxylated compounds with nonnatural stereoconfiguration. In this study, we discovered for the first time that some fructose 1,6-diphosphate aldolases (FruA) and tagatose 1,6-diphosphate (TagA) aldolases lost their strict stereoselectivity when using L-glyceraldehyde and synthesized not only L-sorbose but also a high proportion of L-psicose. Among the aldolases tested, TagA A ldolases are remarkably useful and have been widely investigated for catalyzed COC bond formation (1). The ability to catalyze aldol addition reactions from small chiral polyfunctional molecules and generate up to two new stereogenic centers allows aldolases to synthesize a broad range of both natural and novel polyhydroxylated compounds. Among the aldolase families, dihydroxyacetone-phosphate (DHAP)-dependent aldolases, which utilize DHAP as the donor substrate and accept a broad range of acceptor aldehydes, are widely investigated. Well-known members of this class include fuculose 1-phosphate aldolase (FucA), rhamnulose 1-phosphate aldolase (RhaD), fructose 1,6-diphosphate aldolase (FruA), and tagatose 1,6-diphosphate aldolase (TagA) (2). These enzymes have been used to synthesize several new deoxy or phosphorylated sugars and iminocyclitols (3-5). DHAP-dependent aldolases create two new stereogenic centers at C atoms 3 and 4 ([3S,4R], [3S,4S], [3R,4S], [3R,4R]). FucA, FruA, RhaD, and TagA generally form (3R,4R), (3S,4R), (3R,4S), and (3S,4S) stereoconfigurations, respectively (1, 2). However, some aldolases sometimes lost their strict stereoselectivity at the C-4 stereocenter with some aldehydes as substrates. For example, RhaD aldolase from Escherichia coli catalyzed DHAP and L-glyceraldehyde to form L-fructose (3R,4S). However, D-sorbose (3R,4S) and D-psicose (3R,4R) were formed when using D-glyceraldehyde (6-8). Moreover, FucA aldolase from E. coli catalyzed DHAP and L-glyceraldehyde to form the single product L-tagatose (3R,4R). However, FucA from Thermus thermophilus HB8 generated L-tagatose (3R,4R) and L-fructose (3R,4S) simultaneously from the same substrates. This finding indicated that aldolases had a high level of stereocontrol at C-3; however, the configuration of the stereocenter at C-4 in some cases depended on the particular enzyme and acceptor structure. This aldolase property can be well utilized to synthesize various types of rare sugars. Thus far, no reports have shown this property for FruA aldolase. In addition, TagA aldolases form diastereomer mixtures of product, in which instead of the natural configuration (3S,4S), those of the configuration (3S,4R) predominated (Ͼ90%) (4).L-Sugars, which are one large group of rare sugars, often hold enormous potential for applications in the pharmaceutical industry (9-11). For example, several L-sugars can be used to produce L-nucleoside analogues, which showed increased antiviral activity, better metabolic stability, and more favorable toxicological profiles (12, 1...

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“…[6] Among the aldolase families, we have been focusing on dihydroxyacetone phosphate (DHAP)-dependent aldolases in recent years and investigating the stereochemistry of these enzymes in in vitro synthesis of rare sugars. [7][8][9][10][11] However, an important prerequisite for a suitable biocatalysis is that the substrate of the biocatalyst should be readily available in sufficient amount and relatively stable. Thus, the strict specificity for the donor substrate DHAP, a rather expensive and unstable compound, is disadvantageous for broad application of DHAPdependent aldolases.…”

Section: Introductionmentioning

confidence: 99%

Synthesis of D-Sorbose and D-Psicose by RecombinantEscherichia coli

Gao

et al. 2015

Journal of Carbohydrate Chemistry

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In the current work, the in vitro synthetic system for rare sugars was successfully transformed into an engineered Escherichia coli with a plasmid containing both the aldolase RhaD and phosphatase YqaB. By taking advantage of the inherent biosynthetic pathways in E. coli, this approach permits the use of simple and cheap glycerol for the synthesis of DHAP in vivo. Moreover, the introduction of the phosphatase into the E. coli system allows for the removal of the phosphate group on the synthetic intermediate to yield the neutral rare sugars, which can be readily secreted to the medium without accumulation in the cell.

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One-pot four-enzyme synthesis of ketoses with fructose 1,6-bisphosphate aldolases from Staphylococcus carnosus and rabbit muscle

Abstract: By the action of D-fructose 1,6-bisphosphate aldolases (FruA) from rabbit muscle and Staphylococcus carnosus, various ketoses were synthesized from glyceraldehydes or other aliphatic aldehydes as acceptors in a one-pot four-enzyme system.

Cited by 23 publications

References 18 publications

Ni-Catalyzed Homoallylation of Polyhydroxy N,O-Acetals with Conjugated Dienes Promoted by Triethylborane

Ni-Catalyzed Homoallylation of Polyhydroxy N,O-Acetals with Conjugated Dienes Promoted by Triethylborane

Biosynthesis of l -Sorbose and l -Psicose Based on C—C Bond Formation Catalyzed by Aldolases in an Engineered Corynebacterium glutamicum Strain

Synthesis of D-Sorbose and D-Psicose by RecombinantEscherichia coli

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