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• W2037312982 abstract "Abstract The 2‐keto‐3‐deoxygluconate aldolases (KDGAs) isolated from Sulfolobus species convert pyruvate and glyceraldehyde reversibly into 2‐keto‐3‐deoxygluconate and ‐galactonate. As a result of their high thermostability and activity on nonphosphorylated substrates, KDGA enzymes have potential as biocatalysts for the production of building blocks for fine chemical and pharmaceutical applications. Up to now, wild‐type enzymes have only shown moderate stereocontrol for their natural reaction. However, if a set of azido‐functionalized aldehydes were applied as alternative acceptors in the reaction with pyruvate, the stereoselectivity was strongly increased to give enantiomeric or diastereomeric excess values up to 97 %. The Sulfolobus acidocaldarius KDGA displayed a higher stereoselectivity than Sulfolobus solfataricus KDGA for all tested reactions. The azido‐containing products are useful chiral intermediates in the synthesis of nitrogen heterocycles." @default.
• W2037312982 created "2016-06-24" @default.
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• W2037312982 date "2014-03-05" @default.
• W2037312982 modified "2023-10-16" @default.
• W2037312982 title "Substrate Specificity and Stereoselectivity of Two <i>Sulfolobus</i> 2‐Keto‐3‐deoxygluconate Aldolases towards Azido‐Substituted Aldehydes" @default.
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• W2037312982 doi "https://doi.org/10.1002/cctc.201300785" @default.
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