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B6db references: 94197860

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
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 2002/11/12 16:17

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