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Phosphoribulokinase : ウィキペディア英語版 | Phosphoribulokinase
In enzymology, a phosphoribulokinase () is an enzyme that catalyzes the chemical reaction :ATP + D-ribulose 5-phosphate ADP + D-ribulose 1,5-bisphosphate Thus, the two substrates of this enzyme are ATP and D-ribulose 5-phosphate, whereas its two products are ADP and D-ribulose 1,5-bisphosphate. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:D-ribulose-5-phosphate 1-phosphotransferase. Other names in common use include phosphopentokinase, ribulose-5-phosphate kinase, phosphopentokinase, phosphoribulokinase (phosphorylating), 5-phosphoribulose kinase, ribulose phosphate kinase, PKK, PRuK, and PRK. This enzyme participates in carbon fixation. ==Structural studies==
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
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