Enzymatic aldol reaction/isomerization as a route to unusual sugars

Durrwachter, J. R.; Sweers, H. M.; Nozaki, Kenji; Wong, Chi‐Huey

doi:10.1016/s0040-4039(00)84233-1

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1986

2012

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Cited by 33 publications

(6 citation statements)

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“…Previous studies of the application of RAMA as a catalyst in organic synthesis by us,37"39 Jones,40 Wong,41,[42][43][44][45] have focused mainly on the synthesis of carbohydrates. The qualitative conclusion of these and other biochemical studies30 is that RAMA accepts a broad range of aldehydes as the electrophilic component of the aldol reaction, but accepts only DHAP or close analogues of DHAP as the nucleophilic component.…”

mentioning

confidence: 99%

Rabbit muscle aldolase as a catalyst in organic synthesis

Bednarski¹,

Simon²,

Bischofberger³

et al. 1989

J. Am. Chem. Soc.

221

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mentioning

confidence: 99%

Rabbit muscle aldolase as a catalyst in organic synthesis

Bednarski¹,

Simon²,

Bischofberger³

et al. 1989

J. Am. Chem. Soc.

221

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“…It has been shown that aldolase-catalysed condensations provide a practical route to a wide variety of simple sugars and sugar derivatives (Durrwachter et al 1986). Wong and Whitesides (1983) established the use of rabbit muscle aldolase in the organic synthesis of unnatural sugar phosphates.…”

Section: Discussionmentioning

confidence: 99%

Purification and characterization of a class I fructose 1,6-bisphosphate aldolase from Staphylococcus carnosus

Brockamp

Kula

1990

Appl Microbiol Biotechnol

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A fructose 1,6-bisphosphate aldolase (E.C.4.1.2.13) from Staphylococcus carnosus DSM 20501 was purified for the first time. The enzymatic activity was insensitive to high levels of E D T A indicating that the enzyme is a class I aldolase. This enzyme exhibits good stability at high temperatures and extreme stability over a wide p H range. The Km for fructose 1,6-bisphosphate as substrate was 0.022 mM. The S. carnosus aldolase is a monomeric enzyme with a molecular mass of about 33 kDa. It exhibits a relatively broad p H optimum between pH 6.5 and 9.0. Furthermore, the aldolase accepts other aldehydes in place of its natural substrate, glyceraldehyde 3-phosphate, allowing the synthesis of various sugar phosphates.

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“…Xylose isomerase requires divalent metal cations, usually Mg2', Mn2+, or Co2+ for the maximum activity and thermal stability. The enzyme has a wide substrate specificity [223]: glucose and fructose derivatives modified at the 3-, 5-or 6-position are isomerized by the enzyme as will be described later.…”

Section: Lsomerizationsmentioning

confidence: 99%