Abstract:
:The mechanism of the maize pyruvate, phosphate dikinase-catalyzed conversion of adenosine 5'-triphosphate, orthophosphate and pyruvate to adenosine 5'-monophosphate, inorganic pyrophosphate and phosphoenolpyruvate, respectively, was determined by using transient kinetic techniques. The data obtained demonstrate that catalysis in the maize pyruvate, phosphate dikinase active site involves initial transfer of the P beta P-unit from adenosine 5'-trisphosphate to the enzyme to form a pyrophosphorylenzyme intermediate, followed by sequential phosphoryl group transfer to orthophosphate (to form pyrophosphate and a phosphoenzyme intermediate) and pyruvate (to form phosphoenolpyruvate and free enzyme).
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Carroll LJ,Dunaway-Mariano D,Smith CM,Chollet Rdoi
10.1016/0014-5793(90)81358-usubject
Has Abstractpub_date
1990-11-12 00:00:00pages
178-80issue
1-2eissn
0014-5793issn
1873-3468journal_volume
274pub_type
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