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Phosphoenolpyruvate (2-phosphoenolpyruvate, PEP) is the carboxylic acid derived from the enol of pyruvate and phosphate. It exists as an anion. PEP is an important intermediate in biochemistry. It has the highest-energy phosphate bond found (−61.9 kJ/mol) in organisms, and is involved in glycolysis and gluconeogenesis.
The reaction is similar to the reaction catalysed by pyruvate kinase, which also converts pyruvate to PEP. [3] However, pyruvate kinase catalyses an irreversible reaction, and does not consume ATP. By contrast, PPDK catalyses a reversible reaction, and consumes 1 molecule of ATP for each molecule of pyruvate converted.
d -Glucose + 2 [NAD] + + 2 [ADP] + 2 [P] i 2 × Pyruvate 2 × + 2 [NADH] + 2 H + + 2 [ATP] + 2 H 2 O Glycolysis pathway overview The use of symbols in this equation makes it appear unbalanced with respect to oxygen atoms, hydrogen atoms, and charges. Atom balance is maintained by the two phosphate (P i) groups: Each exists in the form of a hydrogen phosphate anion, dissociating to contribute ...
Pyruvate, the conjugate base, CH 3 COCOO −, is an intermediate in several metabolic pathways throughout the cell. Pyruvic acid can be made from glucose through glycolysis, converted back to carbohydrates (such as glucose) via gluconeogenesis, or converted to fatty acids through a reaction with acetyl-CoA. [3]
When pyruvate kinase – the enzyme that normally catalyzes the reaction that converts PEP to pyruvate – is knocked out in mutants of Bacillus subtilis, PEPCK participates in one of the replacement anaplerotic reactions, working in the reverse direction of its normal function, converting PEP to OAA. [13] Although this reaction is possible ...
The hyperthermostable pyruvate, water dikinase enzyme in Pyrococcus furiosus is encoded by the mlrA gene, which was found to be regulated by at least in part by maltose at a transcription level. [4] Pyruvate, water dikinase catalyzes the reaction that converts phosphoenolpyruvate, AMP, and phosphate to pyruvate, ATP, and water.
Many Enterobacteriaceae, including E. coli, have two isoforms of pyruvate kinase, PykA and PykF, which are 37% identical in E. coli (Uniprot: PykA, PykF).They catalyze the same reaction as in eukaryotes, namely the generation of ATP from ADP and PEP, the last step in glycolysis, a step that is irreversible under physiological conditions.
Enolase is a member of the large enolase superfamily.It has a molecular weight of 82,000–100,000 daltons depending on the isoform. [3] [4] In human alpha enolase, the two subunits are antiparallel in orientation so that Glu 20 of one subunit forms an ionic bond with Arg 414 of the other subunit. [3]