Re-engineering the discrimination between the oxidized coenzymes NAD+ and NADP+ in clostridial glutamate dehydrogenase and a thorough reappraisal of the coenzyme specificity of the wild-type enzyme.

Capone, Marina; Scanlon, David; Griffin, Joanna; Engel, Paul C

Capone, Marina; Scanlon, David; Griffin, Joanna; Engel, Paul C.

Affiliation

Capone M; School of Biomolecular and Biomedical Science, Conway Institute, University College Dublin, Dublin, Ireland.

FEBS J ; 278(14): 2460-8, 2011 Jul.

Article in En | MEDLINE | ID: mdl-21564547

Subject(s)

Bacterial Proteins/metabolism; Clostridium symbiosum/enzymology; Glutamate Dehydrogenase/metabolism; Mutant Proteins/metabolism; NADP/metabolism; NAD/metabolism; Amino Acid Substitution; Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Clostridium symbiosum/genetics; Drug Contamination; Glutamate Dehydrogenase/chemistry; Glutamate Dehydrogenase/genetics; Hydrogen-Ion Concentration; Indicators and Reagents/chemistry; Kinetics; Mutant Proteins/chemistry; NAD/analysis; NADP/analysis; NADP/isolation & purification; Osmolar Concentration; Oxidation-Reduction; Recombinant Proteins/chemistry; Recombinant Proteins/metabolism; Reproducibility of Results; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Bacterial Proteins / Clostridium symbiosum / Mutant Proteins / Glutamate Dehydrogenase / NAD / NADP Type of study: Prognostic_studies Language: En Journal: FEBS J Journal subject: BIOQUIMICA Year: 2011 Document type: Article Affiliation country: Ireland

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