Aspartic Acid 413 Is Important for the Normal Allosteric Functioning of ADP-Glucose Pyrophosphorylase
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چکیده
منابع مشابه
Aspartic Acid 413 1 s lmportant for the Normal Allosteric
As part of a structure-function analysis of the higher-plant ADPglucose pyrophosphorylase (ACP), we used a random mutagenesis approach in combination with a nove1 bacterial complementation system to isolate over 100 mutants that were defective in glycogen production (T.W. Creene, S.E. Chantler, M.L. Khan, C.F. Barry, j. Preiss, T.W. Okita [1996] Proc Natl Acad Sci USA 93: 1509-1513). One mutant...
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The substrate specificity of enzymes is crucial to control the fate of metabolites to different pathways. However, there is growing evidence that many enzymes can catalyze alternative reactions. This promiscuous behavior has important implications in protein evolution and the acquisition of new functions. The question is how the undesirable outcomes of in vivo promiscuity can be prevented. ADP-...
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ADP-glucose (Glc) pyrophosphorylase (AGPase), a key regulatory enzyme in starch biosynthesis, is highly regulated. Transgenic approaches in four plant species showed that alterations in either thermal stability or allosteric modulation increase starch synthesis. Here, we show that the classic regulators 3-phosphoglyceric acid (3-PGA) and inorganic phosphate (Pi) stabilize maize (Zea mays) endos...
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ADP-glucose pyrophosphorylase catalyzes a rate-limiting reaction in prokaryotic glycogen and plant starch biosynthesis. Despite sharing similar molecular size and catalytic and allosteric regulatory properties, the prokaryotic and higher plant enzymes differ in higher-order protein structure. The bacterial enzyme is encoded by a single gene whose product of ca. 50,000 Da assembles into a homote...
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ژورنال
عنوان ژورنال: Plant Physiology
سال: 1996
ISSN: 1532-2548,0032-0889
DOI: 10.1104/pp.112.3.1315