Fructose-1,6 bisphosphatase (FBPase) is a ubiquitous enzyme controlling a key reaction. In non-photosynthetic tissues, it regulates the rate of gluconeogenesis. In photosynthetic tissues, two FBPase isozymes (chloroplastic and cytosolic) play key roles in carbon assimilation and metabolism. The cytosolic FBPase is one of the regulatory enzymes in the sucrose biosynthetic pathway - its activity is regulated by both fine and coarse control mechanisms. Kinetic and allosteric properties of the plant cytosolic FBPase are remarkably similar to the mammalian and yeast FBPase, but differ greatly from those of the chloroplastic FBPase. Cytosolic FBPase is relatively conserved among various organisms both at amino acid and nucleotide sequence levels. There is slightly higher similarity between mammalian FBPase and plant cytosolic FBPase than there is between the two plant FBPases. Expression of plant cytosolic FBPase gene is developmentally regulated and appears to be coordinated with the expression of Rubisco and other carbon metabolism enzymes. Similar to the gluconeogenic FBPase, relatively rapid end product repression of FBPase gene occurs in plant. However, unlike the gluconeogenic FBPase, a concurrent decline in plant FBPase activity does not occur in response to increased end product levels. The physiological significance of FBPase gene repression, therefore, remains unclear in plants. Both expression and activity of the cytosolic FBPase are regulated by environmental factors such as light and drought conditions. Light-dependent modulation of FBPase activity in plants appears to involve some type of posttranslational modification. In addition to elucidating the exact nature of the presumed posttranslational modification, cloning of genomic and upstream sequences is needed before we fully understand the molecular regulation of the cytosolic FBPase in plants. Use of transgenic plants with altered rates of FBPase activity offers potential for enhanced crop productivity.
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