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Investigation of mechanism of pyruvate phosphate dikinase

Thesis/Dissertation ·
OSTI ID:5265395
The kinetic mechanism of pyruvate phosphate dikinase (PPDK) from Bacteroides symbiosus was investigated with several different kinetic diagnostics. Initial velocity patterns were intersecting for AMP/PPi and ATP/Pi substrate pairs and parallel for all other substrate pairs. PPDK was shown to catalyze ({sup 14}C)-pyruvate: PEP exchange in the absence of cosubstrates, ({sup 14}C)-AMP:ATP exchange in the presence of Pi/PPi and the ({sup 32}P)-Pi:PPi exchange in the presence of ATP/AMP. The enzyme was also shown by using ({alpha},{beta}-{sup 18}O, {beta}-{sup 18}O{sub 2})-ATP and ({beta},{gamma}-{sup 18}O,{gamma}-{sup 18}O{sub 3})-ATP and {sup 31}P-NMR techniques, to catalyze exchange in ATP between the {beta}, {gamma}-bridge oxygen and the {alpha}-P nonbridge oxygen and also between the {beta},{gamma}-bridge oxygen and the {beta}-P nonbridge oxygen. The exchanges were catalyzed by PPDK in the presence of Pi. AMP and Pi binding order was examined by carrying-out dead-end inhibition studies.
Research Organization:
Maryland Univ., College Park, MD (USA)
OSTI ID:
5265395
Country of Publication:
United States
Language:
English

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Related Subjects

550201* -- Biochemistry-- Tracer Techniques
59 BASIC BIOLOGICAL SCIENCES
AMP
ATP
BACTERIA
BETA DECAY RADIOISOTOPES
BETA-MINUS DECAY RADIOISOTOPES
BIOCHEMICAL REACTION KINETICS
CARBON 14 COMPOUNDS
DAYS LIVING RADIOISOTOPES
ENZYMES
EVEN-EVEN NUCLEI
ISOTOPE APPLICATIONS
ISOTOPES
KINETICS
LABELLED COMPOUNDS
LIGHT NUCLEI
MICROORGANISMS
NMR SPECTRA
NUCLEI
NUCLEOTIDES
ODD-ODD NUCLEI
ORGANIC COMPOUNDS
OXYGEN 18
OXYGEN COMPOUNDS
OXYGEN ISOTOPES
PHOSPHATES
PHOSPHORUS 32
PHOSPHORUS COMPOUNDS
PHOSPHORUS ISOTOPES
PHOSPHORUS-GROUP TRANSFERASES
PHOSPHOTRANSFERASES
RADIOISOTOPES
REACTION KINETICS
SPECTRA
STABLE ISOTOPES
SUBSTRATES
TRACER TECHNIQUES
TRANSFERASES