type	Journal Article
authors	Stolz, M.; Dornemann, D.
title	Purification, characterization and N-terminal sequence of phosphoserine aminotransferase from the green alga Scenedesmus obliquus, mutant C-2 A'
journal	Z Naturforsch [C]
Activity	2.6.1.52
Family	2.6.1.52.a
ui	94197860
year	(1994)
volume	49
number	1-2
pages	63-9.
keywords	Algae, Green/*enzymology
abstract	Phosphoserine aminotransferase (EC 2.6.1.52), an enzyme of the "phosphorylated pathway" leading to the formation of serine, was purified from Scenedesmus obliquus, mutant C-2 A'. Purification started from the soluble supernatant of a crude cell homogenate and included different affinity and DEAE chromatographic techniques, as well as gel filtration. The purified phosphoserine aminotransferase was enriched 1537-fold and identified to be a homodimer with subunit molecular masses of 40 kDa, each. The absorption spectrum is consistent with the presence of pyridoxal-5-phosphate as cofactor. From the purified enzyme 18 amino acids of the N-terminus could be determined, showing at least 67% homology with the serC gene encoding phosphoserine aminotransferases from bacterial organisms.
last changed	2020/02/20 10:46