The Synthesis of Dihydroxyacetone Phosphate

Ballou, Clinton E.; Fischer, Hermann O. L.

doi:10.1021/ja01589a045

Cited by 79 publications

(23 citation statements)

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“…Dihydroxyacetone phosphate dimethyl ketal. This was prepared as the bis-monocyclohexylamine salt as described by Ballou & Fischer (1956). It had m.p.…”

Section: Methodsmentioning

confidence: 99%

pH-dependence of the triose phosphate isomerase reaction

Plaut

Knowles

1972

Biochemical Journal

162

152

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The pH-dependences of the kinetic parameters k(cat.) and K(m) for the triose phosphate isomerase reaction were determined in each direction. Apparent pK(a) values of 6.0 and 9.0 are observed in the dependences of k(cat.)/K(m). The pH-dependences of k(cat.) are sigmoid, with apparent pK(a) values of about 6.0. The results are interpreted in terms of a single base on the enzyme providing an efficient proton-shuttling mechanism for the isomerization.

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“…Dihydroxyacetone phosphate dimethyl ketal. This was prepared as the bis-monocyclohexylamine salt as described by Ballou & Fischer (1956). It had m.p.…”

Section: Methodsmentioning

confidence: 99%

pH-dependence of the triose phosphate isomerase reaction

Plaut

Knowles

1972

Biochemical Journal

162

152

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“…(Mannheim, Germany). DHAP was prepared from the ketal by the method of Ballou & Fischer (1956). Bovine serum albumin (fraction V) was obtained from the Armour Pharmaceutical Co. Ltd. (Eastbourne, Sussex).…”

Section: Methodsmentioning

confidence: 99%

The active chemical state of d-glyceraldehyde 3-phosphate in its reactions with d-glyceraldehyde 3-phosphate dehydrogenase, aldolase and triose phosphate isomerase

Trentham

McMurray

Pogson

1969

Biochemical Journal

151

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Glyceraldehyde 3-phosphate exists as the geminal diol and the free aldehyde in the molar ratio 29:1 in aqueous solution. The rate constant of the conversion of diol into aldehyde is 8.7x10(-2)sec.(-1) in the pH range 7.3-8.6 at 20 degrees . The free aldehyde is the substrate for d-glyceraldehyde 3-phosphate dehydrogenase. Over a wide concentration range of enzyme the rate of conversion of diol into aldehyde is the rate-limiting process in the catalytic oxidation of d-glyceraldehyde 3-phosphate by NAD(+). Aldolase and triose phosphate isomerase both liberate d-glyceraldehyde 3-phosphate as the aldehyde. This suggests that the relatively slow diol-aldehyde interconversion does not restrict the rate of glycolysis.

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“…The monomeric phosphorylated ketals ( Fig. 3b) are available by multi-step reactions from 3-chloro-1,2-propanediol (Ballou and Fischer 1956), acetone (Valentin and Bolte 1995), 1,3-dibromoacetone (available by acidic bromination of acetone; Gefflaut et al 1997), or dihydroxyacetone dimer (Ferroni et al 1999;Charmantray et al 2004). Again, the step from the precursor to DHAP can be made by acidic treatment.…”

Section: Chemical Routes 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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The Synthesis of Dihydroxyacetone Phosphate

Abstract: The carbanilides with substituents in the 2 and 5 positions lides require prolonged drying under vacuum since they rewere markedly more insoluble than the corresponding 3,4-tain solvent tenaciously, substituted compounds. The amino-substituted carbani-Wilmington, Delaware

Cited by 79 publications

References 0 publications

pH-dependence of the triose phosphate isomerase reaction

pH-dependence of the triose phosphate isomerase reaction

The active chemical state of d-glyceraldehyde 3-phosphate in its reactions with d-glyceraldehyde 3-phosphate dehydrogenase, aldolase and triose phosphate isomerase

Chemical and enzymatic routes to dihydroxyacetone phosphate

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