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Cellular respiration produces 30 - 32 ATP per glucose molecule. Although most of the ATP results from oxidative phosphorylation and the electron transport chain (ETC), 4 ATP are gained beforehand (2 from glycolysis and 2 from the citric acid cycle).
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The bonds of adenosine triphosphate (ATP) can be broken through the addition of water, releasing one or two phosphate groups in an exergonic process called hydrolysis. This reaction liberates the energy in the bonds for use in the cell—for instance, to synthesize proteins from amino acids.
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In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased...
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Related Experiment Video

Updated: Jan 31, 2026

Author Spotlight: Advancing Structural and Biochemical Studies of Proteins Through Thermal Shift Assays
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Pseudokinases: Flipping the ATP for AMPylation.

Lee Bardwell1

  • 1Department of Developmental & Cell Biology, University of California, Irvine, CA 92697, USA.

Current Biology : CB
|January 9, 2019
PubMed
Summary

Researchers discovered that SelO, a pseudokinase, has unexpected catalytic activity. Its ATP cofactor binds in a unique orientation, revealing a new function for this ancient enzyme.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Pseudokinases were historically considered catalytically inactive enzymes.
  • SelO is an ancient enzyme belonging to the pseudokinase family.
  • Understanding pseudokinase function is crucial for various biological processes.

Purpose of the Study:

  • To elucidate the structural basis of SelO function.
  • To investigate the potential catalytic activity of SelO.
  • To understand the role of ATP cofactor binding in SelO's mechanism.

Main Methods:

  • X-ray crystallography was used to determine the crystal structure of SelO.
  • Structural analysis focused on the active site and cofactor interactions.
  • Biochemical assays were employed to assess catalytic activity.

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Main Results:

  • The crystal structure of SelO revealed an ATP cofactor bound in the active site.
  • The ATP cofactor adopted a non-canonical, flipped orientation compared to typical kinases.
  • This unique binding mode enabled SelO to exhibit unexpected catalytic activity.

Conclusions:

  • SelO is not an inactive pseudokinase but possesses catalytic activity.
  • The flipped orientation of the ATP cofactor is key to SelO's enzymatic function.
  • This finding redefines our understanding of pseudokinase capabilities and ancient enzyme evolution.