ChemInform Abstract: Glycerol Kinase: Synthesis of Dihydroxyacetone Phosphate, sn‐Glycerol‐3‐phosphate, and Chiral Analogues.

Crans, Debbie C.; Whitesides, G. M.

doi:10.1002/chin.198612286

Cited by 5 publications

(9 citation statements)

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“…This route has been pioneered by Wong and Whitesides (1983) who exploited the relaxed substrate specificity of glycerol kinases to produce DHAP from dihydroxyacetone and ATP (Crans and Whitesides 1985a). For example, glycerol kinase from Saccharomyces cerevisiae was used to produce DHAP on mole scale from dihydroxyacetone and ATP (Crans and Whitesides 1985b). Alternatively, dihydroxyacetone kinases have been employed as a substitute (Yanase et al 1995;Itoh et al 1999;Sanchez-Moreno et al 2004).…”

Section: From Dihydroxyacetone To Dhapmentioning

confidence: 99%

Chemical and enzymatic routes to dihydroxyacetone phosphate

Schümperli

Pellaux

Panke

2007

Appl Microbiol Biotechnol

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Stereoselective carbon-carbon bond formation with aldolases has become an indispensable tool in preparative synthetic chemistry. In particular, the dihydroxyacetone phosphate (DHAP)-dependent aldolases are attractive because four different types are available that allow access to a complete set of diastereomers of vicinal diols from achiral aldehyde acceptors and the DHAP donor substrate. While the substrate specificity for the acceptor is rather relaxed, these enzymes show only very limited tolerance for substituting the donor. Therefore, access to DHAP is instrumental for the preparative exploitation of these enzymes, and several routes for its synthesis have become available. DHAP is unstable, so chemical synthetic routes have concentrated on producing a storable precursor that can easily be converted to DHAP immediately before its use. Enzymatic routes have concentrated on integrating the DHAP formation with upstream or downstream catalytic steps, leading to multi-enzyme arrangements with up to seven enzymes operating simultaneously. While the various chemical routes suffer from either low yields, complicated work-up, or toxic reagents or catalysts, the enzymatic routes suffer from complex product mixtures and the need to assemble multiple enzymes into one reaction scheme. Both types of routes will require further improvement to serve as a basis for a scalable route to DHAP.

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Section: From Dihydroxyacetone To Dhapmentioning

confidence: 99%

Chemical and enzymatic routes to dihydroxyacetone phosphate

Schümperli

Pellaux

Panke

2007

Appl Microbiol Biotechnol

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“…Disadvantages of both systems relate to the stability, expense, or requisite chemical syntheses (for large-scale application) of the high-energy phosphoryl donors and product inhibition, in the case of PK, by pyruvate. Despite minor drawbacks, these enzymatic ATP regeneration systems have facilitated the study of numerous kinase and synthetase reactions and led to improved chemoenzymatic synthesis of valuable phosphorylated compounds (5,6,9,11,12,19,21).ATP regeneration from ADP using polyphosphate/polyphosphate kinase (polyP/PPK) has also been demonstrated (13) and was recently applied in a practical synthesis of the oligosaccharide, N-acetyllactosamine (14). The latter work showed PPK from Escherichia coli to phosphorylate not only ADP but also other nucleoside diphosphates to their corresponding triphosphates using polyP as a phosphoryl donor.…”

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confidence: 99%

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confidence: 99%

In Vitro ATP Regeneration from Polyphosphate and AMP by Polyphosphate:AMP Phosphotransferase and Adenylate Kinase from Acinetobacter johnsonii 210A

Resnick

Zehnder

2000

Appl Environ Microbiol

116

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In vitro enzyme-based ATP regeneration systems are important for improving yields of ATP-dependent enzymatic reactions for preparative organic synthesis and biocatalysis. Several enzymatic ATP regeneration systems have been described but have some disadvantages. We report here on the use of polyphosphate:AMP phosphotransferase (PPT) from Acinetobacter johnsonii strain 210A in an ATP regeneration system based on the use of polyphosphate (polyP) and AMP as substrates. We have examined the substrate specificity of PPT and demonstrated ATP regeneration from AMP and polyP using firefly luciferase and hexokinase as model ATP-requiring enzymes. PPT catalyzes the reaction polyP n ؉ AMP 3 ADP ؉ polyP n؊1 . The ADP can be converted to ATP by adenylate kinase (AdK). Substrate specificity with nucleoside and 2-deoxynucleoside monophosphates was examined using partially purified PPT by measuring the formation of nucleoside diphosphates with high-pressure liquid chromatography. AMP and 2-dAMP were efficiently phosphorylated to ADP and 2-dADP, respectively. GMP, UMP, CMP, and IMP were not converted to the corresponding diphosphates at significant rates. Sufficient AdK and PPT activity in A. johnsonii 210A cell extract allowed demonstration of polyP-dependent ATP regeneration using a firefly luciferase-based ATP assay. Bioluminescence from the luciferase reaction, which normally decays very rapidly, was sustained in the presence of A. johnsonii 210A cell extract, MgCl 2 , polyP n‫53؍‬ , and AMP. Similar reaction mixtures containing strain 210A cell extract or partially purified PPT, polyP, AMP, glucose, and hexokinase formed glucose 6-phosphate. The results indicate that PPT from A. johnsonii is specific for AMP and 2-dAMP and catalyzes a key reaction in the cell-free regeneration of ATP from AMP and polyP. The PPT/AdK system provides an alternative to existing enzymatic ATP regeneration systems in which phosphoenolpyruvate and acetylphosphate serve as phosphoryl donors and has the advantage that AMP and polyP are stabile, inexpensive substrates.Enzyme-catalyzed phosphoryl transfer reactions (i.e., those which form or cleave P-O bonds) represent a viable alternative to multistep chemical phosphorylations in preparative organic synthesis (7,10,20). Many useful phosphorylating enzymes require nucleoside triphosphates as cofactors. ATP is the most important biological phosphate donor and is a required cofactor for numerous enzymatic reactions in both anabolic and catabolic metabolism, specifically in the formation of P-O bonds. Cofactor provision for ATP-dependent enzymes can be accomplished by their direct addition in stoichiometric amounts or by the inclusion of a cofactor regeneration system. Direct cofactor addition is not only costly but can unfavorably alter reaction equilibrium, lead to an accumulation of inhibitory cofactor by-products, and complicate recovery of end products (20). For preparative-scale organic synthesis, these problems have been overcome by the development of enzymatic systems for ATP regeneration.Whitesi...

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“…Numerous papers have been published on DHAP production (Crans and Whitesides 1985;Fessner 1997;Itoh et al 1999;Kramer and Steckhan 1997), but this is the first to describe immobilization of a microorganism for this purpose.…”

Section: Discussionmentioning

confidence: 98%

“…Enzymatic phosphorylation of dihydroxyacetone by glycerokinase-ATP yields a DHAP that is characterized by a high degree of acetate and phosphate contamination, since the acetyl phosphate used for cofactor regeneration is hydrolytically unstable (Crans and Whitesides 1985).…”

Section: Introductionmentioning

confidence: 99%

Microencapsulation of Aerococcus viridans with catalase and its application for the synthesis of dihydroxyacetone phosphate

Streitenberger

Villaverde

Sánchez‐Ferrer

et al. 2002

Applied Microbiology and Biotechnology

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Dihydroxyacetone phosphate is essential for the synthesis of polyhydroxylated compounds used as components or precursors of active pharmaceutical substances, such as antibiotics or glycosidase inhibitors. Dihydroxyacetone phosphate was produced by enzymatic oxidation of L-alpha-glycerophosphate in the presence of glycerophosphate oxidase or Aerococcus viridans coimmobilized with a hydrogen peroxide-decomposing enzyme. The microencapsulation of A. viridans with catalase in sodium alginate showed a conversion of 98.5%; the conversion percentage remained constant in all five runs. Liquid chromatography of the product revealed that the product peak corresponded to that of the dihydroxyacetone phosphate internal standard. This indicated a high degree of product purity.

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ChemInform Abstract: Glycerol Kinase: Synthesis of Dihydroxyacetone Phosphate, sn‐Glycerol‐3‐phosphate, and Chiral Analogues.

Abstract: Glycerol kinase (E.C.

Cited by 5 publications

References 1 publication

Chemical and enzymatic routes to dihydroxyacetone phosphate

Chemical and enzymatic routes to dihydroxyacetone phosphate

In Vitro ATP Regeneration from Polyphosphate and AMP by Polyphosphate:AMP Phosphotransferase and Adenylate Kinase from Acinetobacter johnsonii 210A

Microencapsulation of Aerococcus viridans with catalase and its application for the synthesis of dihydroxyacetone phosphate

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