Structural study of a single-point mutant of Sulfolobus solfataricus alcohol dehydrogenase with enhanced activity(395 views) Esposito L, Bruno I, Sica F, Raia CA, Giordano A, Rossi M, Mazzarella L, Zagari A
Febs Lett (ISSN: 0014-5793, 0014-5793print, 1873-3468electronic), 2003 Mar 27; 539(1-3): 14-18.
Keywords: Alcohol Dehydrogenase, Coenzyme Binding, Crystal Structure, Enzyme Activation, Single Mutation, Reduced Nicotinamide Adenine Dinucleotide, Archaebacterium, Binding Affinity, Catalysis, Conference Paper, Controlled Study, Nonhuman, Priority Journal, Protein Structure, Sulfolobus Solfataricus, Wild Type, Crystallography, X-Ray, Models, Molecular, Point Mutation, Protein Conformation,
Affiliations: *** IBB - CNR ***
Ist. di Biostrutture e Bioimmagini, CNR, via Mezzocannone 6-8, I-80134 Napoli, Italy
Dipartimento di Chimica, Univ. Studi di Napoli 'Federico II', via Cinthia, I-80126 Napoli, Italy
Ist. di Biochimica delle Proteine, CNR, via Marconi 10, I-80125 Napoli, Italy
References: Not available.
Structural study of a single-point mutant of Sulfolobus solfataricus alcohol dehydrogenase with enhanced activity
Alcohol dehydrogenase from Sulfolobus solfataricus (SsADH) is the only enzyme from Archaea among the structurally studied members of the medium-chain ADH family described so far. Here, we present the three-dimensional structure of the apo form of the mutant N249Y which exhibits increased catalytic activity when compared to the wild-type enzyme. The substitution, located in the coenzyme binding domain, decreases the affinity for NAD(H) cofactor. The rearrangement of segments 248-250 and 270-275, induced by the mutation, suggests an explanation for the lower coenzyme affinity. This study also highlights the role in SsADH catalysis of the flexible loops located at the interface between the catalytic and the coenzyme domains. (C) 2003 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.
Structural study of a single-point mutant of Sulfolobus solfataricus alcohol dehydrogenase with enhanced activity
Santulli G, Cipolletta E, Sorriento D, Del Giudice C, Anastasio A, Monaco S, Maione AS, Condorelli G, Puca A, Trimarco B, Illario M, Iaccarino G * CaMK4 gene deletion induces hypertension(409 views) J Am Heart Assoc Journal Of The American Heart Association (ISSN: 2047-9980), 2012; 1(4): N/D-N/D. Impact Factor:2.882 ViewExport to BibTeXExport to EndNote