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B6db references: 4390206

type Journal Article
authors Rao, D. R.; Hariharan, K.; Vijayalakshmi, K. R.
title A study of the metabolism of L-alpha gamma-diaminobutyric acid in a Xanthomonas species
journal Biochem J
sel selected
ui 4390206
year (1969)
volume 114
number 1
pages 107-15
keywords Aminobutyric Acids/*metabolism
abstract 1. l-alphagamma-Diaminobutyric acid is metabolized in Xanthomonas sp. to aspartic beta-semialdehyde, aspartic acid and oxaloacetic acid. 2. Aspartic beta-semialdehyde is formed from diaminobutyric acid by a pyruvate-dependent gamma-transamination. 3. The transaminase has a pH optimum of 9 and exhibits a high degree of substrate specificity, as analogues of diaminobutyric acid and pyruvate are inert in the system. The transaminase is inhibited by carbonyl-binding agents such as hydroxylamine. 4. Aspartic acid is formed from aspartic beta-semialdehyde by an NAD(+)-dependent dehydrogenation. 5. The dehydrogenase has a pH optimum of 8.5 and is a thiol enzyme. It is specific for aspartic beta-semialdehyde but analogues of NAD(+) such as 3-acetylpyridine-adenine dinucleotide and deamino-NAD are partly active in the system. 6. The significance of these reactions is discussed in relation to diaminobutyric acid metabolism in plants and mammalian systems.
last changed 2009/05/06 09:33

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