Preparation of (2R,3S)-β-hydroxy-α-amino acids by use of a novel Streptomyces aldolase as a resolving agent for racemic material

Abstract

A unique aldolase, which was isolated from Streptomyces a~nakusaensis, is used to catalyse a reverse aldol reaction on representative racemic B-hydroxy-a-amino acids (3-6) to give samples of the (2R,3S)-(D-threo)-enantiomers with excellent enantiomeric purity.

Characterization of an Inducible Phenylserine Aldolase from Pseudomonas putida 24-1

“…Site-directed mutagenesis experiments showed that replacement of K213 with Q resulted in a loss of the enzyme activity, with a disappearance of the absorption maximum at 420 nm. Thus, K213 of the enzyme probably functions as an essential catalytic residue, forming a Schiff base with pyridoxal 5-phosphate.Much attention has been paid to 3-hydroxy-2-amino acids as components of antibiotics and immunosuppressants (5-7, 9, 18, 19, 32-34) and as a drug for Parkinson's disease therapy (21), and enzymatic syntheses of 3-hydroxy-2-amino acids with L-and D-threonine aldolases have been done extensively (5,6,9,18,19,(32)(33)(34).Phenylserine aldolase (L-threo-3-phenylserine benzaldehydelyase, EC 4.1.2.26) catalyzes the reversible conversion of Lthreo-and L-erythro-3-phenylserine to benzaldehyde and glycine. Although the occurrence of phenylserine aldolase in animals has been reported previously (2), the enzyme has not been purified and characterized.…”

“…Much attention has been paid to 3-hydroxy-2-amino acids as components of antibiotics and immunosuppressants (5-7, 9, 18, 19, 32-34) and as a drug for Parkinson's disease therapy (21), and enzymatic syntheses of 3-hydroxy-2-amino acids with L-and D-threonine aldolases have been done extensively (5,6,9,18,19,(32)(33)(34).…”

A Novel Metal-activated Pyridoxal Enzyme with a Unique Primary Structure, Low Specificity d-Threonine Aldolase fromArthrobacter sp. Strain DK-38

“…Threonine aldolase (TA) (EC 4.1.2.5), which catalyzes the reversible interconversion of certain ␤-hydroxy-␣-amino acids and glycine plus aldehydes, has been shown to be useful for the biosynthesis of ␤-hydroxy-␣-amino acids (1)(2)(3)(4)(5). The enzyme appears to fall into two types, L-type and D-type, on the basis of its stereospecificity of the cleavage reaction toward the ␣-carbon of threonine.…”

L-allo-threonine aldolase from Aeromonas jandaei DK-39: gene cloning, nucleotide sequencing, and identification of the pyridoxal 5'-phosphate-binding lysine residue by site-directed mutagenesis

“…The purified mutant enzymes, K51A and K224A, showed properties similar to those of the wild type, while the mutant enzyme K199A was catalytically inactive, with corresponding disappearance of the absorption maximum at 420 nm. Thus, Lys199 of L-allo-TA probably functions as an essential catalytic residue forming an internal Schiff base with PLP of the enzyme to catalyze the reversible aldol reaction.The bioorganic synthesis of ␤-hydroxy-␣-amino acids is attracting a great deal of attention because of their potential application as chiral building blocks for the synthesis of biologically active molecules (6,7,24,32,33). A variety of ␤-hydroxy-␣-amino acids are present in complex natural compounds with interesting biological properties.…”

“…The bioorganic synthesis of ␤-hydroxy-␣-amino acids is attracting a great deal of attention because of their potential application as chiral building blocks for the synthesis of biologically active molecules (6,7,24,32,33). A variety of ␤-hydroxy-␣-amino acids are present in complex natural compounds with interesting biological properties.…”