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Literature summary 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

Protein Variants

EC Number Protein Variants Comment Organism
4.1.2.48 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
4.1.2.48 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

EC Number Organism UniProt Comment Textmining
4.1.2.48 Escherichia coli P75823
-
-

Substrates and Products (Substrate)

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

Synonyms

EC Number Synonyms Comment Organism
4.1.2.48 low specificity threonine aldolase
-
 Escherichia coli
4.1.2.48 LtaE
-
 Escherichia coli