Isolation and Purification to Apparent Homogeneity of 4,5-Dioxovalerate Aminotransferase from Scenedesmus obliquus Mutant
نویسنده
چکیده
A . Kah, D . Dörnemann, and H . Senger Fachbereich Biologie/Botanik der Philipps-Universität Marburg, Lahnberge, D-3550 Marburg/L. , Bundesrepublik Deutschland Z . Naturforsch. 43c , 563-571 (1988); received March 3/Apr i l 12, 1988 C-5-Pathway, 4,5-Dioxovalerate, 5-Aminolevul inic Ac id , 4,5-Dioxovalerate Aminotransferase, Scenedesmus In the present paper the purif ication of a specific 4,5-dioxovalerate transaminase f rom pigment mutant C-2 A ' of the unicellular green alga Scenedesmus obliquus to apparent homogeneity is described. The newly isolated enzyme L-glutamate: 4,5-dioxovalerate aminotransferase is not identical wi th L-alanine: 4,5-dioxovalerate aminotransferase (EC 2.6.1.43) and L-alanine: glyoxylate aminotransferase (EC 2.6.1.44). A procedure for the purif ication is described and the resulting homogeneous protein is characterized by its A^-values for oxo-substrates and amino donors, its pyr idoxal phosphate requirement, reversability of the catalysis, pH-opt imum, isoelectric point and its molecular weight.
منابع مشابه
Kinetic Characteristics, Substrate Specificity and Catalytic Properties of Phosphoserine Aminotransferase from the Green Alga Scenedesmus obliquus, Mutant C-2A'
Phosphoserine am inotransferase (EC 2.6.1.52) has been purified from Scenedesmus obliquus. m utant C -2A ', as reported previously (Stolz and D örnem ann, 1994). The current studies on its catalytic properties, involving initial reaction velocities as a function of the phosphoserine concentration at various fixed concentrations of 2-oxoglutarate as aminoacceptor, indicate a bi-bi ping pong mech...
متن کاملPurification, characterization and N-terminal sequence of phosphoserine aminotransferase from the green alga Scenedesmus obliquus, mutant C-2 A'.
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 w...
متن کاملIsolation and Characterization of 3 Protochlorophyllides from Pigment Mutant C-2 A' of Scenedesmus obliquus
Kiriakos Kotzabasis and Horst Senger Fachbereich Biologie/Botanik, Philipps-Universität, Lahnberge, D-3550 Marburg, Bundesrepublik Deutschland Z. Naturforsch. 41c, 1001 — 1003 (1986); received July 1, 1986 Scenedesmus obliquus, Protochlorophyllide, Monovinyl Protochlorophyllide, Divinyl Protochlorophyllide Three Protrochlorophyllides (protochlorophyllide) were separated from mutant C-2 A' of th...
متن کاملCharging of Both, Plastidal tRNAg,n and tRNAglu with Glutamate and Subsequent Amidation of the Misacylated tRNAg,n by a Glutamyl-tRNA Amidotransferase in the Unicellular Green Alga Scenedesmus obliquus, Mutant C-2A’
U. C. Vothknecht* and D. Dörnemann Fachbereich Biologie/Botanik, Philipps-Universität Marburg, Karl-v.-Frisch-Straße, D-35032 Marburg, Bundesrepublik Deutschland Z. Naturforsch. 50c, 789-795 (1995); received June 16/August 28, 1995 C5-Pathway, Glutamyl-tRNAglu-Synthetase (E.C.6.1.1.17), Misacylation of tRNAglu, Amidotransferase, Scenedesmus obliquus In a previous paper we described the purifica...
متن کاملPurification and characterization of cytochrome c6 from the unicellular green alga Scenedesmus obliquus.
Purification of a soluble cytochrome c6 from the unicellular green alga Scenedesmus obliquus by a simple and rapid method is described. The purification procedure includes ammonium sulfate precipitation and non-denaturating PAGE. The N-terminal sequence of the first 20 amino acids was determined and shows 85% similarity and 75% identity to the sequence of cytochrome c6 from the green alga Monor...
متن کامل