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Simultaneous binding of coenzyme and two ligand molecules into the active siteof fungal trihydroxynaphthalene reductaseStojan, Jure, 1956- ; Brunskole Švegelj, Mojca ; Lanišnik-Rižner, TeaWe present here a kinetic characterization of the oxidation of the artificial substrate 2,3-dihydro-2,5-dihydroxy-4H-benzopyran-4-one in the presence of NADP(+) by trihydroxynaphthalene reductase ... from the filamentous fungus Curvularia lunata. Although the experimental data were gathered by conventional equipment and were only available for the reaction in one direction, the analysis confirms the bi-bi reaction mechanism and yields estimates of kinetic parameters of the intermediates. It is based on an independent estimation of coenzyme binding constants and on a sequential analysis of three portions of the progress curves, from the beginning of the reaction until equilibrium is reached. First, the plateaus are used to determine the overall equilibrium constant of the non-catalyzed reaction. Then, the dissociation constants of the oxidized and reduced cofactor are estimated by titration. Subsequently, the initial parts of the progress curvesare analyzed using the rate equation that is derived under combined assumptions of equilibrium and steady state. The macroscopic relations obtained are then fixed in the final progress curve analysis where the information for only two remaining rate constants is extracted from their curved portions by fitting numerically solved model-specific differential equations to the data. At pH 8, the overall equilibrium largely favours the oxidized substrate and reduced cofactor, and the activity of the holoenzyme isinhibited by high substrate concentrations. Substrate inhibition can be discriminated from true cooperativity through the effects of apigenin, a flavonoid inhibitor that is structurally similar, but larger, than the substrate used in the study.Source: Enzymology and molecular biology of carbonyl metabolism : [14th international workshop, Kranjska Gora, Slovenia, July 8 - 12, 2008] (Vol. 178, issues 1/3, 2009, str. 268-273)Type of material - conference contributionPublish date - 2009Language - englishCOBISS.SI-ID - 25390297
Author
Stojan, Jure, 1956- |
Brunskole Švegelj, Mojca |
Lanišnik-Rižner, Tea
Topics
Fungi |
Enzymology |
Coenzymes |
Oxidoreductases |
Binding Sites |
Nadp |
Nadph Dehydrogenase |
Glive |
NADP |
Koencimi |
Oksidoreduktaze |
Mesta vezave |
NADPH dehidrogenaza
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source: Enzymology and molecular biology of carbonyl metabolism : [14th international workshop, Kranjska Gora, Slovenia, July 8 - 12, 2008] (Vol. 178, issues 1/3, 2009, str. 268-273)
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Year | Impact factor | Edition | Category | Classification | ||||
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JCR | SNIP | JCR | SNIP | JCR | SNIP | JCR | SNIP |
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DRS, in which the journal is indexed
Database name | Field | Year |
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Links to authors' personal bibliographies | Links to information on researchers in the SICRIS system |
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Stojan, Jure, 1956- | 03723 |
Brunskole Švegelj, Mojca | 28343 |
Lanišnik-Rižner, Tea | 11699 |
Source: Personal bibliographies
and: SICRIS
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