Transient-state kinetic analysis of Synechococcus glutamate 1-semialdehyde aminotransferase

Biochemistry
M A SmithB Grimm

Abstract

We report a transient-state kinetic analysis relating to the mechanism of glutamate 1-semialdehyde aminotransferase (GSAT). Multiple-wavelength spectral kinetic data were collected by micro-stopped-flow spectrophotometry. Time resolved spectral sketches resulting from reactions with glutamate 1-semialdehyde (GSA), 4,5-diaminovalerate (DAVA), and 5-aminolevulinate (ALA) indicated various transient chromophoric intermediates. On the basis of the generally accepted mechanism of other aminotransferases and absorbance characteristics of associated intermediates, these transient chromophores are likely associated with Schiff base formation, ketimine/aldimine tautomerization, and transimidation etc. Spectral kinetic changes associated with these putative intermediates were, in general, concentration dependent. Various experimental evidence, including reactions with the GSAT lys272ile mutant, suggested rapid equilibrium of isomeric aldimines and geminal diamines. With this and related simplifying assumptions, a minimal mechanism was derived which provided a means for transient-state spectral kinetic analysis of reactions with GSA, DAVA, and ALA, all of which lead to the formation of the same putative central enzyme complex. Resulting k...Continue Reading

Citations

May 10, 2006·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Xinhuai LvLiwen Niu
May 28, 2010·Protein Science : a Publication of the Protein Society·Gunhild LayerDirk W Heinz
Jan 27, 2017·Microbiology and Molecular Biology Reviews : MMBR·Harry A DaileyMartin J Warren
Jul 25, 2003·The Journal of Biological Chemistry·Simona D'AguannoRobert A John

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