Prephenate Dehydrogenase (NADP )
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Prephenate Dehydrogenase (NADP )
Prephenate dehydrogenase is an enzyme found in the shikimate pathway, and helps catalyze the reaction from prephenate to tyrosine. Nomenclature Gene: (Saccharomyces cerevisiae, Saccharomyces Cerevisiae) TYR1 Shikimate pathway: Arogenate/Prephenate (ADH/PDH). Although in the shikimate pathway Arogenate dehydrogenase, arogenate and prephenate dehydrogenase catalyze different reactions, they can at times be used interchangeably. * TyrA (tyrosine A: within the tyrosine pathway) * Prephenate dehydrogenase * Prephenate (Nicotinamide adenine dinucleotide phosphate) dehydrogenase * Prephenate dehydrogenase (NADP) * NADP+ oxidoreductase Homology (biology), Homology This enzyme so far has been found in sixteen different organisms; twelve different kinds of bacteria (mostly cyanobacteria) and four different kinds of plants (mostly different kinds of beans). Bacteria organisms (examples): Acenitobacter calcoaceticus, Fischerella sp., Flavobacterium so., Comamonas testosteroni, and nost ...
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Saccharomyces Cerevisiae
''Saccharomyces cerevisiae'' () (brewer's yeast or baker's yeast) is a species of yeast (single-celled fungal microorganisms). The species has been instrumental in winemaking, baking, and brewing since ancient times. It is believed to have been originally isolated from the skin of grapes. It is one of the most intensively studied eukaryotic model organisms in molecular and cell biology, much like '' Escherichia coli'' as the model bacterium. It is the microorganism which causes many common types of fermentation. ''S. cerevisiae'' cells are round to ovoid, 5–10  μm in diameter. It reproduces by budding. Many proteins important in human biology were first discovered by studying their homologs in yeast; these proteins include cell cycle proteins, signaling proteins, and protein-processing enzymes. ''S. cerevisiae'' is currently the only yeast cell known to have Berkeley bodies present, which are involved in particular secretory pathways. Antibodies again ...
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