Pub. Date : 2003 Nov 1
PMID : 12877657
7 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Putative NADPH-dependent GDH (L-glycerate dehydrogenase) of the protozoan parasite Entamoeba histolytica (EhGDH) has been characterized. | NADP | hexose-6-phosphate dehydrogenase/glucose 1-dehydrogenase | Homo sapiens |
| 2 | In contrast with the implications from protein alignment and phylogenetic analysis, kinetic studies revealed that the amoebic GDH showed biochemical properties similar to those of mammalian GDH, i.e. a preference for NADPH as cofactor and higher affinities towards NADPH and beta-hydroxypyruvate than towards NADP+ and L-glycerate. | NADP | hexose-6-phosphate dehydrogenase/glucose 1-dehydrogenase | Homo sapiens |
| 3 | In contrast with the implications from protein alignment and phylogenetic analysis, kinetic studies revealed that the amoebic GDH showed biochemical properties similar to those of mammalian GDH, i.e. a preference for NADPH as cofactor and higher affinities towards NADPH and beta-hydroxypyruvate than towards NADP+ and L-glycerate. | NADP | hexose-6-phosphate dehydrogenase/glucose 1-dehydrogenase | Homo sapiens |
| 4 | In contrast with the implications from protein alignment and phylogenetic analysis, kinetic studies revealed that the amoebic GDH showed biochemical properties similar to those of mammalian GDH, i.e. a preference for NADPH as cofactor and higher affinities towards NADPH and beta-hydroxypyruvate than towards NADP+ and L-glycerate. | NADP | hexose-6-phosphate dehydrogenase/glucose 1-dehydrogenase | Homo sapiens |
| 5 | In contrast with the implications from protein alignment and phylogenetic analysis, kinetic studies revealed that the amoebic GDH showed biochemical properties similar to those of mammalian GDH, i.e. a preference for NADPH as cofactor and higher affinities towards NADPH and beta-hydroxypyruvate than towards NADP+ and L-glycerate. | NADP | hexose-6-phosphate dehydrogenase/glucose 1-dehydrogenase | Homo sapiens |
| 6 | In contrast with the implications from protein alignment and phylogenetic analysis, kinetic studies revealed that the amoebic GDH showed biochemical properties similar to those of mammalian GDH, i.e. a preference for NADPH as cofactor and higher affinities towards NADPH and beta-hydroxypyruvate than towards NADP+ and L-glycerate. | NADP | hexose-6-phosphate dehydrogenase/glucose 1-dehydrogenase | Homo sapiens |
| 7 | In contrast with the implications from protein alignment and phylogenetic analysis, kinetic studies revealed that the amoebic GDH showed biochemical properties similar to those of mammalian GDH, i.e. a preference for NADPH as cofactor and higher affinities towards NADPH and beta-hydroxypyruvate than towards NADP+ and L-glycerate. | NADP | hexose-6-phosphate dehydrogenase/glucose 1-dehydrogenase | Homo sapiens |