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PLP-dependent H(2)S biogenesis.

Sangita Singh1, Ruma Banerjee

  • 1Department of Biological Chemistry, University of Michigan Medical Center, Ann Arbor, MI 48109-5606, USA.

Biochimica Et Biophysica Acta
|February 15, 2011
PubMed
Summary
This summary is machine-generated.

Hydrogen sulfide (H(2)S) plays key physiological roles, but its signaling mechanisms and regulation remain unclear. This review details H(2)S biogenesis pathways and pyridoxal phosphate-dependent enzymes involved.

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Area of Science:

  • Biochemistry
  • Physiology
  • Enzymology

Background:

  • Endogenously produced hydrogen sulfide (H(2)S) mediates diverse physiological effects in mammals.
  • Significant knowledge gaps exist regarding H(2)S biological targets, mechanisms of action, and regulation of its biogenesis and clearance.

Purpose of the Study:

  • To review the kinetics of H(2)S-generating reactions.
  • To compare the structures of pyridoxal 5'-phosphate-dependent (PLP) enzymes involved in H(2)S biogenesis.
  • To discuss strategies for regulating these PLP enzymes.

Main Methods:

  • Review of sulfur metabolic pathways involved in H(2)S production.
  • Comparative analysis of PLP-enzyme structures.
  • Discussion of regulatory strategies.

Main Results:

  • H(2)S is produced via two main pathways: reverse transsulfuration and cysteine catabolism.
  • Key PLP-dependent enzymes include cystathionine β-synthase, cystathionine γ-lyase, and cysteine aminotransferase.
  • These enzymes catalyze the conversion of homocysteine and cysteine to intermediates leading to H(2)S liberation.

Conclusions:

  • Understanding H(2)S biogenesis and the involved PLP enzymes is crucial for its pharmacological potential.
  • Further research into H(2)S signaling, targets, and regulation is warranted.
  • This review provides insights into H(2)S-generating reactions and enzyme regulation within the context of PLP enzymology.