Solvent Isotope Effects in Reactions of Human Medium-Chain Acyl-CoA Dehydrogenase Active Site Mutants
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
-
Online-Ressource
- Language
-
Englisch
- Bibliographic citation
-
In: Biochemistry ; 46 (2007), 9. - S. 2497-2509. - ISSN 0006-2960. - eISSN 1520-4995
- Classification
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Biowissenschaften, Biologie
- Event
-
Veröffentlichung
- (where)
-
Konstanz
- (who)
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Bibliothek der Universität Konstanz
- (when)
-
2008
- Creator
- URN
-
urn:nbn:de:bsz:352-opus-51407
- Rights
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
25.03.2025, 1:49 PM CET
Data provider
This object is provided by:
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Gradinaru, Vasile Robert
- Schowen, Richard
- Ghisla, Sandro
- Bibliothek der Universität Konstanz
Time of origin
- 2008
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Probing the electron transfer properties of human medium-chain acyl-CoA dehydrogenase and site-directed mutants
Reaction of General Acyl-CoA Dehydrogenase with 3,4-Pentadienoyl-CoA
Inactivation of medium-chain acyl-CoA dehydrogenase from pig kidney by methylenecyclopropyl-acetyl-CoA : identification of a new flavin-inhibitor adduct
Molecular evolution and substrate specificity of acyl-CoA dehydrogenases : chimaeric 'medium/long' chain-specific enzyme from medium-chain acyl-CoA dehydrogenase
Protonic equilibria in the reductive half-reaction of the medium-chain acyl-CoA dehydrogenase
Substrate chain length specificity of acyl-CoA dehydrogenases : studies on different mutants
Acyl-CoA dehydrogenases - a mechanistic overview
Inactivation of General Acyl-CoA Dehydrogenase from Pig Kidney by a Metabolite of Hypoglycin A*
Inactivation of general acyl-CoA dehydrogenase from pig kidney by the suicide substrate methylenecyclopropylacetyl-CoA : structure of one of the covalent flavin-inhibitor adducts
On the Inactivation of General Acyl-CoA-Dehydrogenase from Pig Kidney by Methylenecyclopropyl-Acetyl-CoA, a Metabolite of Hypoglycin : Studies with flavin modified enzymes
Mechanistic studies with general acyl-CoA dehydrogenase and butyryl-CoA dehydrogenase : evidence for the transfer of the beta-hydrogen to the flavin N(5)-position as a hydride
Medium chain Acyl-CoA dehydrogenase genetic defects : identification and partial characterisation of two new patient mutants
Probing the electron transfer properties of human medium-chain acyl-CoA dehydrogenase and site-directed mutants
Reaction of General Acyl-CoA Dehydrogenase with 3,4-Pentadienoyl-CoA
Inactivation of medium-chain acyl-CoA dehydrogenase from pig kidney by methylenecyclopropyl-acetyl-CoA : identification of a new flavin-inhibitor adduct
Molecular evolution and substrate specificity of acyl-CoA dehydrogenases : chimaeric 'medium/long' chain-specific enzyme from medium-chain acyl-CoA dehydrogenase
Protonic equilibria in the reductive half-reaction of the medium-chain acyl-CoA dehydrogenase
Substrate chain length specificity of acyl-CoA dehydrogenases : studies on different mutants
Acyl-CoA dehydrogenases - a mechanistic overview
Inactivation of General Acyl-CoA Dehydrogenase from Pig Kidney by a Metabolite of Hypoglycin A*
Inactivation of general acyl-CoA dehydrogenase from pig kidney by the suicide substrate methylenecyclopropylacetyl-CoA : structure of one of the covalent flavin-inhibitor adducts
On the Inactivation of General Acyl-CoA-Dehydrogenase from Pig Kidney by Methylenecyclopropyl-Acetyl-CoA, a Metabolite of Hypoglycin : Studies with flavin modified enzymes
Mechanistic studies with general acyl-CoA dehydrogenase and butyryl-CoA dehydrogenase : evidence for the transfer of the beta-hydrogen to the flavin N(5)-position as a hydride
Medium chain Acyl-CoA dehydrogenase genetic defects : identification and partial characterisation of two new patient mutants
Probing the electron transfer properties of human medium-chain acyl-CoA dehydrogenase and site-directed mutants
Reaction of General Acyl-CoA Dehydrogenase with 3,4-Pentadienoyl-CoA
Inactivation of medium-chain acyl-CoA dehydrogenase from pig kidney by methylenecyclopropyl-acetyl-CoA : identification of a new flavin-inhibitor adduct
Molecular evolution and substrate specificity of acyl-CoA dehydrogenases : chimaeric 'medium/long' chain-specific enzyme from medium-chain acyl-CoA dehydrogenase
Protonic equilibria in the reductive half-reaction of the medium-chain acyl-CoA dehydrogenase
Substrate chain length specificity of acyl-CoA dehydrogenases : studies on different mutants
Acyl-CoA dehydrogenases - a mechanistic overview
Inactivation of General Acyl-CoA Dehydrogenase from Pig Kidney by a Metabolite of Hypoglycin A*
Inactivation of general acyl-CoA dehydrogenase from pig kidney by the suicide substrate methylenecyclopropylacetyl-CoA : structure of one of the covalent flavin-inhibitor adducts
On the Inactivation of General Acyl-CoA-Dehydrogenase from Pig Kidney by Methylenecyclopropyl-Acetyl-CoA, a Metabolite of Hypoglycin : Studies with flavin modified enzymes