Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 4.1.2.48 extracted from

  • Kurjatschij, S.; Katzberg, M.; Bertau, M.
    Production and properties of threonine aldolase immobilisates (2014), J. Mol. Catal. B, 103, 3-9 .
No PubMed abstract available
Search for more literature for 4.1.2.48

Protein Variants

Protein Variants Comment Organism
industry biocatalysis using threonine aldolases opens up a way to synthesise beta-hydroxy-alpha-amino acids in one step. Dichiral beta-hydroxy-alpha-amino acids are a highly valuable class of compounds from which pharmaceutically active intermediates for the synthesis of e.g. beta-sympathomimetic drugs. Methods to immobilise the L-low specificity threonine aldolase of Escherichia coli are studied. The entrapment of the enzyme into a porous network of orthosilicate appears to be the most promising method Escherichia coli
synthesis biocatalysis using threonine aldolases opens up a way to synthesise beta-hydroxy-alpha-amino acids in one step. Dichiral beta-hydroxy-alpha-amino acids are a highly valuable class of compounds from which pharmaceutically active intermediates for the synthesis of e.g. beta-sympathomimetic drugs. Methods to immobilise the L-low specificity threonine aldolase of Escherichia coli are studied. The entrapment of the enzyme into a porous network of orthosilicate appears to be the most promising method Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P75823
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-threonine
-
 Escherichia coli glycine + acetaldehyde
-
 ?

Synonyms

Synonyms Comment Organism
low specificity threonine aldolase
-
 Escherichia coli
LtaE
-
 Escherichia coli