Document Detail

Threonine aldolases-screening, properties and applications in the synthesis of non-proteinogenic beta-hydroxy-alpha-amino acids.
MedLine Citation:
PMID:  20683718     Owner:  NLM     Status:  MEDLINE    
Threonine aldolases (TAs) constitute a powerful tool for catalyzing carbon-carbon bond formations in synthetic organic chemistry, thus enabling an enantio- and diastereoselective synthesis of beta-hydroxy-alpha-amino acids. Starting from the achiral precursors glycine and an aldehyde, two new stereogenic centres are formed in this catalytic step. The resulting chiral beta-hydroxy-alpha-amino acid products are important precursors for pharmaceuticals such as thiamphenicol, a L: -threo-phenylserine derivative or L: -threo-3,4-dihydroxyphenylserine. TAs are pyridoxal-5-phosphate-dependent enzymes, which, in nature, catalyze the cleavage of L: -threonine or L: -allo-threonine to glycine and acetaldehyde in a glycine biosynthetic pathway. TAs from a broad number of species of bacteria and fungi have been isolated and characterised as biocatalysts for the synthesis of beta-hydroxy-alpha-amino acids. In this review, screening methods to obtain novel TAs, their biological function, biochemical characterisation and preparative biotransformations with TAs are described.
Nina Dückers; Katrin Baer; Sabine Simon; Harald Gröger; Werner Hummel
Related Documents :
2805178 - Reductive biotransformation of 3-oxo bile acids in human blood.
7216718 - Synthesis and chromatographic properties of 1,3-thiazane-2-carboxylic acid (beta-homoth...
2582318 - Beta-carboline analogues of n-methyl-4-phenyl-1,2,5,6-tetrahydropyridine (mptp): endoge...
1633888 - Barley (1----3,1----4)-beta-glucanase isoenzyme ei gene expression is mediated by auxin...
24425478 - Sugar and malic acid utilization and acetic acid formation byleuconostoc oenos.
6721888 - The lubricating activity of human synovial fluids.
Publication Detail:
Type:  Journal Article; Review     Date:  2010-08-04
Journal Detail:
Title:  Applied microbiology and biotechnology     Volume:  88     ISSN:  1432-0614     ISO Abbreviation:  Appl. Microbiol. Biotechnol.     Publication Date:  2010 Sep 
Date Detail:
Created Date:  2010-08-23     Completed Date:  2011-01-25     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  8406612     Medline TA:  Appl Microbiol Biotechnol     Country:  Germany    
Other Details:
Languages:  eng     Pagination:  409-24     Citation Subset:  IM    
evocatal GmbH, Düsseldorf, Germany.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Aldehydes / metabolism
Amino Acids / biosynthesis,  chemical synthesis*,  chemistry
Glycine / metabolism
Glycine Hydroxymethyltransferase / chemistry*,  classification,  isolation & purification*
Recombinant Proteins / biosynthesis
Threonine / metabolism
Reg. No./Substance:
0/Aldehydes; 0/Amino Acids; 0/Recombinant Proteins; 56-40-6/Glycine; 72-19-5/Threonine; EC Hydroxymethyltransferase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Previous Document:  Arbuscular mycorrhizal fungus enhances P acquisition of wheat (Triticum aestivum L.) in a sandy loam...
Next Document:  Photoinactivation effects of hematoporphyrin monomethyl ether on Gram-positive and -negative bacteri...