Enzymes from Pseudomonas sp. strain NCIB 11097 participating in biotransformation of acetaldehyde and glycine to threonine isomers.
Enzyme activities involved in L-threonine bioconversions present in cells of Pseudomonas sp. strain NCIB 11097 were separated by phenyl-Sepharose hydrophobic chromatography. The separation of the two main activity components was monitored by discontinuous polyacrylamide gel electrophoresis. Threonine aldolase catalyzed the conversion of glycine and acetaldehyde to a mixture of isomers, L-threonine and L-allothreonine, in a biotransformation reaction having pH and temperature optima of 7.5 and 25-30 degrees C, respectively. The fraction containing serine hydroxymethyltransferase converted acetaldehyde and glycine specifically to L-allothreonine in a biotransformation reaction having pH and temperature optima of 7.4 and 37 degrees C, respectively.
Diaz-Diaz
M
M
Department of Biology, University of Waterloo, ON, Canada.
Ward
O P
OP
Honek
J
J
Lajoie
G
G
D000079:Acetaldehyde / Q000378:metabolism*; D001426:Bacterial Proteins / Q000302:isolation & purification* / Q000378:metabolism; D002853:Chromatography, Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D005998:Glycine / Q000378:metabolism*; D012696:Glycine Hydroxymethyltransferase / Q000302:isolation & purification / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D011549:Pseudomonas / Q000201:enzymology*; D013237:Stereoisomerism; D013696:Temperature; D013912:Threonine / Q000096:biosynthesis*
D001426:Bacterial Proteins; D013912:Threonine; D012696:Glycine Hydroxymethyltransferase; D000079:Acetaldehyde; D005998:Glycine