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Related Concept Videos

ATP Synthase: Mechanism01:48

ATP Synthase: Mechanism

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 ATP...

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Evaluation of Vascular Control Mechanisms Utilizing Video Microscopy of Isolated Resistance Arteries of Rats
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Functional studies of rat hydroxymethylbilane synthase.

Nan Li1, Xiusheng Chu, Long Wu

  • 1Department of Biology and Chemistry, City University of Hong Kong, 83 Tat Chee Avenue, Kowloon, Hong Kong SAR, PR China.

Bioorganic Chemistry
|September 2, 2008
PubMed
Summary

This study reveals hydroxymethylbilane synthase

Area of Science:

  • Biochemistry
  • Enzymology
  • Natural Products Chemistry

Background:

  • Tetrapyrrolic pigments are vital natural products in biological processes.
  • Hydroxymethylbilane synthase is a key enzyme in tetrapyrrole biosynthesis.

Purpose of the Study:

  • To investigate rat hydroxymethylbilane synthase.
  • To characterize enzyme mutants and substrate analogs.

Main Methods:

  • Enzyme kinetics assays
  • Site-directed mutagenesis
  • Enzyme purification and characterization
  • Synthesis and incubation of substrate analogs

Main Results:

  • Enzymatic reaction rate of holoenzyme is lower than enzyme-intermediate complexes.

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  • Mutant D44 is crucial for enzyme-intermediate complex disassembly.
  • Mutants E63 and H78 maintain enzyme activity at high temperatures.
  • Three synthesized analogs are weak substrates; all four can prepare uroporphyrin I analogs.

    • Conclusions:

    • Corrected previous theoretical analysis of hydroxymethylbilane synthase kinetics.
    • Identified key residues for enzyme function and stability.
    • Demonstrated potential of synthesized analogs for uroporphyrin I analog preparation.