Isolation and Purification to Apparent Homogeneity of 4,5-Dioxovalerate Aminotransferase from Scenedesmus obliquus Mutant C-2 A′

A. Kah; D. Dörnemann; H. Senger

doi:10.1515/znc-1988-7-813

Open Access Published by De Gruyter June 2, 2014

Isolation and Purification to Apparent Homogeneity of 4,5-Dioxovalerate Aminotransferase from Scenedesmus obliquus Mutant C-2 A′

A. Kah , D. Dörnemann and H. Senger

From the journal Zeitschrift für Naturforschung C

https://doi.org/10.1515/znc-1988-7-813

In the present paper the purification of a specific 4,5-dioxovalerate transaminase from pigment mutant C-2 A′ of the unicellular green alga Scenedesmus obliquus to apparent homogeneity is described. The newly isolated enzyme ʟ-glutamate: 4,5-dioxovalerate aminotransferase is not identical with ʟ-alanine: 4,5-dioxovalerate aminotransferase (EC 2.6.1.43) and ʟ-alanine: glyoxylate aminotransferase (EC 2.6.1.44). A procedure for the purification is described and the resulting homogeneous protein is characterized by its K_ᴍ-values for oxo-substrates and amino donors, its pyridoxal phosphate requirement, reversability of the catalysis, pH-optimum, isoelectric point and its molecular weight.

: C-5-Pathway; 4,5-Dioxovalerate; 5-Aminolevulinic Acid; 4,5-Dioxovalerate Aminotransferase; Scenedesmus

Received: 1988-4-12

Revised: 1988-3-3

Published Online: 2014-6-2

Published in Print: 1988-8-1

This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 3.0 License.

Isolation and Purification to Apparent Homogeneity of 4,5-Dioxovalerate Aminotransferase from Scenedesmus obliquus Mutant C-2 A′

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