Abstract
Abstract δ-Aminovaleramide amidohydrolase (δ-aminovaleramidase) has been purified 400-fold from the soluble fraction of cell-free extracts of Pseudomonas putida P2 grown on l-lysine as sole source of carbon and nitrogen. The purified enzyme catalyzes hydrolysis of amides four to six carbon atoms in length which bear an ω-amino group. Gel filtration and density gradient centrifugation suggest a molecular weight of about 67,000. Optimum activity occurs at pH 7.5 to 8.5, and photoinactivation data implicate involvement of an essential histidyl residue.
Highlights
(d-aminovaleramidase) has been purified 400-fold from the soluble fraction of cell-free extracts of Pseudomonas pufida P2 grown on L
The enzyme preparation used had a specific activity of 130 units per mg
Induction by Lysine- extracts of cells grown on glucose, malate, glutamate, or valine catalyze the a-aminovaleramidase reaction, the activity of extracts of lysine-grown cells is at least 25.fold higher (Table II)
Summary
(d-aminovaleramidase) has been purified 400-fold from the soluble fraction of cell-free extracts of Pseudomonas pufida P2 grown on L-. While D-lysine may be degraded by yet other reactions [2]. Catabolism of D-lysine in mammals appears to involve conversion to pipecolate [3]. L-Lysine is degraded via saccharopine in mammals [4, 5], via acylated intermediates in the yeast Hunsenula saturnis [6, 7], via fl-lysine and 3,5-diaminohexanoate in Clostridia [8, 9], via transamination to Al-piperideine-6-carboxylate in Flavobacterium fuscorum [10, 11] and via the intermediates shown in Fig. 1 in Pseudomonas. A deamidase catalyzing Reaction 3 (Fig. 1) was purified 20.fold and reported to lack activity toward glutamine or asparagine [16]. We report here the purification and properties of Pseudomonas putida 6aminovaleramidel amidohydrolase (&aminovaleramidase) which catalyzes the reaction : COOH.
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