An Investigation of the Active Site of Lactate Dehydrogenase with NAD+ Analogues
| العنوان: | An Investigation of the Active Site of Lactate Dehydrogenase with NAD+ Analogues |
|---|---|
| المؤلفون: | Jean-Pierre Samama, Michael G. Rossmann, Nicole Marchal-Rosenheimer, Jean-Francois Beiellmann |
| المصدر: | European Journal of Biochemistry. 120:563-569 |
| بيانات النشر: | Wiley, 1981. |
| سنة النشر: | 1981 |
| مصطلحات موضوعية: | chemistry.chemical_classification, Binding Sites, L-Lactate Dehydrogenase, Nicotinamide, biology, Stereochemistry, Coenzymes, Active site, NAD, Biochemistry, Cofactor, Kinetics, chemistry.chemical_compound, Species Specificity, chemistry, Dogfish, Lactate dehydrogenase, biology.protein, Animals, Moiety, Cattle, Rabbits, Pyridinium, NAD+ kinase, Thioamide |
| الوصف: | The kinetic properties of 18 NAD+ analogues, with alterations to the nicotinamide moiety, have been studied with respect to dogfish M4, rabbit M4 and beef H4 lactate dehydrogenases. The size of the groups present at C-3 of the pyridinium can be increased quite extensively without loss of coenzyme activity. Groups tested were thioamide, methyl, ethyl, diazoketone and chloroacetyl. Substitutions at positions C-4 and C-5 prevent proper positioning for hydride transfer and can hinder binding to the enzyme. The kinetic properties of pyridine-adenine dinucleotide and its 3-iodo derivative reveal the bidning role of the amide at C-3 whereas 3-cyanopyridine-adenine dinculeotide is a strong inhibitor. |
| تدمد: | 1432-1033 0014-2956 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fd7a6e8cbdc59bfc1de9ee6a417bafa3Test https://doi.org/10.1111/j.1432-1033.1981.tb05737.xTest |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....fd7a6e8cbdc59bfc1de9ee6a417bafa3 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 14321033 00142956 |
|---|