|
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 |
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