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Literature summary extracted from

  • Uhl, M.K.; Oberdorfer, G.; Steinkellner, G.; Riegler-Berket, L.; Mink, D.; van Assema, F.; Schuermann, M.; Gruber, K.
    The crystal structure of D-threonine aldolase from Alcaligenes xylosoxidans provides insight into a metal ion assisted PLP-dependent mechanism (2015), PLoS ONE, 10, e0124056 .
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
4.1.2.42 pharmacology the enzyme has a considerable potential in biocatalysis for the stereospecific synthesis of various beta-hydroxy amino acids, which are valuable building blocks for the production of pharmaceuticals Achromobacter xylosoxidans
4.1.2.42 synthesis the enzyme has a considerable potential in biocatalysis for the stereospecific synthesis of various beta-hydroxy amino acids, which are valuable building blocks for the production of pharmaceuticals Achromobacter xylosoxidans

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.2.42 expression in Escherichia coli BL21 Star (DE3) cells Achromobacter xylosoxidans

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.1.2.42 determination of the crystal structure at 1.5 A resolution Achromobacter xylosoxidans

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.1.2.42 Mn2+ the role of the essential metal (manganese) ion is most likely to activate the beta-hydroxy group of the substrate for deprotonation by His193 Achromobacter xylosoxidans

Organism

EC Number Organism UniProt Comment Textmining
4.1.2.42 Achromobacter xylosoxidans A0A0J9X243 IFO 12669
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.2.42
-
 Achromobacter xylosoxidans

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.2.42 D-threonine
-
 Achromobacter xylosoxidans glycine + acetaldehyde
-
 ?

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.2.42 pyridoxal 5'-phosphate pyridoxal 5'-phosphate dependent enzyme. The metal binding siteis close to the pyridoxal 5'-phosphate cofactor in the active site of the enzyme. Metal ion assisted pyridoxal 5'-phosphate-dependent mechanism Achromobacter xylosoxidans

General Information

EC Number General Information Comment Organism
4.1.2.42 physiological function the enzyme plays a major role in degradation of D-threonine Achromobacter xylosoxidans