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Research Article

Inactivation of Leuconostoc Mesenteroids NRRL B-512F Dextransucrase by Specific Modification of Lysine Residues with Pyridoxal-5′-Phosphate

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Pages 291-295 | Received 09 Jun 1994, Accepted 25 Oct 1994, Published online: 27 Sep 2008
 

Abstract

Dextransucrase from Leuconostoc mesentwoides NRRL B-512F was inactivated by pyridoxal-5′-phosphate (PLP). The inactivation was reversible in as much as the loss of enzyme activity was completely reversed by prolonged dialysis. PLP-modified dextransucrase after reduction with sodium borohydride showed a characteristic fluorescence emission maximum at 397 nm when excited at 325 nm. The stoichiometric results indicated that four lysine residues are modified by PLP under the experimental conditions. These results established for the first time that lysine residues are essential for the activity of dextransucrase.

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