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B6db references: 90167095

type Journal Article
authors Ueno, S.; Morino, H.; Sano, A.; Kakimoto, Y.
title Purification and characterization of D-3-aminoisobutyrate-pyruvate aminotransferase from rat liver
journal Biochim Biophys Acta
ui 90167095
year (1990)
volume 1033
number 2
pages 169-75.
keywords Animal
abstract D-3-Aminoisobutyrate-pyruvate aminotransferase (EC was purified 1900-fold from rat liver extract. The purified enzyme showed a molecular mass of 180 kDa by gel-permeation HPLC analysis using a TSK gel G3000SW column. Reductive polyacrylamide gel electrophoresis in sodium dodecyl sulfate resulted in identification of a single band of approx. 50 kDa, indicating that the native enzyme is probably a tetrametric protein. The specific activity of the purified enzyme was 1.14 mumol/min per mg protein. D-3-Aminoisobutyrate and beta-alanine were good amino donors. The Km value for L-3-aminoisobutyrate was 100- times larger than that for the D-isomer. The apparent Km values for D-3- aminoisobutyrate and beta-alanine were 35 and 282 microM, respectively. Pyruvate, glyoxylate, oxalacetate, 2-oxo-n-valerate, and 2-oxo-n- butyrate were good amino acceptors. The apparent Km values for pyruvate and glyoxylate were 32 and 44 microM, respectively.
last changed 2002/11/12 16:17

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