- Tytuł:
- Preliminary crystallographic studies of Y25F mutant of periplasmic Escherichia coli L-asparaginase.
- Autorzy:
-
Kozak, Maciej
Jaskólski, Mariusz
Röhm, Klaus - Powiązania:
- https://bibliotekanauki.pl/articles/1044330.pdf
- Data publikacji:
- 2000
- Wydawca:
- Polskie Towarzystwo Biochemiczne
- Tematy:
-
protein crystallography
mutagenesis
leukemia
amidohydrolase - Opis:
- Periplasmic Escherichia coli L-asparaginase II with Y25F mutation in the active-site cavity has been obtained by recombinant techniques. The protein was crystallized in a new hexagonal form (P6522). Single crystals of this polymorph, suitable for X-ray diffraction, were obtained by vapor diffusion using 2-methyl-2,4-pentanediol as precipitant (pH 4.8). The crystals are characterized by a = 81.0, c = 341.1 Å and diffract to 2.45 Å resolution. The asymmetric unit contains two protein molecules arranged into an AB dimer. The physiologically relevant ABA'B' homotetramer is generated by the action of the crystallographic 2-fold axis along [1, -1, 0]. Kinetic studies show that the loss of the phenolic hydroxyl group at position 25 brought about by the replacement of Y with F strongly impairs kcat without significantly affecting Km.
- Źródło:
-
Acta Biochimica Polonica; 2000, 47, 3; 807-814
0001-527X - Pojawia się w:
- Acta Biochimica Polonica
- Dostawca treści:
- Biblioteka Nauki
Artykuł