Heterocyclic β-hydroxy-α-amino acids as substrates for a novel aldolase from Streptomyces amakusaensis; preparation of (2R,3R)-3-(2-thienyl)serine and (2R,3R)-3-(2-furyl)serine from racemic threo material
Author:
Publisher
Royal Society of Chemistry (RSC)
Link
http://pubs.rsc.org/en/content/articlepdf/1996/P1/P19960002439
Reference17 articles.
1. The biosynthesis of tuberin from tyrosine and glycine; observations on the stereochemistry associated with the conversion of glycine through methylenetetrahydrofolate into methenyltetrahydrofolate
2. Stereospecific lysis of a range of β-hydroxy-α-amino acids catalysed by a novel aldolase from Streptomyces amakusaensis
3. Preparation of (2R,3S)-β-hydroxy-α-amino acids by use of a novel Streptomyces aldolase as a resolving agent for racemic material
4. The biosynthesis of nikkomycin X from histidine in Streptomyces tendae
5. Purification and characterization of pyridoxal 5'-phosphate dependent serine hydroxymethylase from lamb liver and its action upon β-phenylserines
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1. Aldol Reactions;Enzyme Catalysis in Organic Synthesis;2012-04-20
2. ChemInform Abstract: Heterocyclic β-Hydroxy-α-amino Acids as Substrates for a Novel Aldolase from Streptomyces amakusaensis: Preparation of (2R,3R)- 3-(2-Thienyl)serine and (2R,3R)-3-(2-Furyl)serine from Racemic threo Material.;ChemInform;2010-08-04
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