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Role of tryptophan residues of lipoxygenase-1 in activity, structure and stability: Chemical modification studies with N-bromosuccinimide

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Relation http://ir.cftri.com/8/
http://www.elsevier.com/locate/foodchem
FC-70-199-204-2000
 
Title Role of tryptophan residues of lipoxygenase-1 in activity,
structure and stability: Chemical modification studies with
N-bromosuccinimide
 
Creator Srinivasulu, Sonati
Appu Rao, A. G.
 
Subject 29 Protein Chemistry
 
Description The tryptophan residues of lipoxygenase-1 (LOX1) from soybeans (Glycine max) were modi®ed using N-bromosuccinimide under both native and denaturing conditions. The accessibility of tryptophan residues was pH-dependent. Only one tryptophan residue was accessible at the optimum pH of enzyme activity and with a decrease in pH from 9 to 2, the accessibility increased. Modification of the accessible four tryptophan residues at pH 4.0 under non-denaturing conditions resulted in complete loss of enzyme
activity; one tryptophan residue was critical for enzyme activity. Modification of the tryptophan residues did not alter the substrate binding affinity; the presence of the substrate during modification did not alter the extent of modi®cation. Modification of the surface-exposed tryptophans did not affect (i) the conformation or structural integrity but (ii) decreased the stability.
 
Date 2000
 
Type Article
NonPeerReviewed
 
Format application/pdf
 
Language en
 
Rights —
 
Identifier http://ir.cftri.com/8/1/Food_Chemistry_70_%282000%29_199-204.pdf
Srinivasulu, Sonati and Appu Rao, A. G. (2000) Role of tryptophan residues of lipoxygenase-1 in activity, structure and stability: Chemical modification studies with N-bromosuccinimide. Food Chemistry, 70. pp. 199-204. ISSN 0308-8146