Cysteine synthase

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Cysteine Synthase

Cysteine synthase is an enzyme that plays a crucial role in the biosynthesis of the amino acid cysteine. It is a key component in the sulfur metabolism pathway and is essential for the production of sulfur-containing compounds in organisms.

Structure[edit | edit source]

Cysteine synthase is a protein complex that typically consists of two subunits: the O-acetylserine sulfhydrylase (OASS) and the serine acetyltransferase (SAT). These subunits work together to catalyze the formation of cysteine from O-acetylserine and hydrogen sulfide.

O-acetylserine Sulfhydrylase (OASS)[edit | edit source]

OASS is responsible for the conversion of O-acetylserine to cysteine. It is a pyridoxal phosphate-dependent enzyme that facilitates the transfer of a sulfhydryl group to O-acetylserine, forming cysteine.

Serine Acetyltransferase (SAT)[edit | edit source]

SAT catalyzes the acetylation of serine to form O-acetylserine, which is the substrate for OASS. This reaction is crucial for the regulation of cysteine biosynthesis.

Function[edit | edit source]

Cysteine synthase is involved in the biosynthesis of cysteine, an amino acid that is vital for protein synthesis, detoxification, and the production of antioxidants such as glutathione. Cysteine is also a precursor for the synthesis of coenzyme A, biotin, and other important biomolecules.

Mechanism[edit | edit source]

The enzymatic reaction catalyzed by cysteine synthase involves two main steps:

  1. The acetylation of serine by SAT to form O-acetylserine.
  2. The transfer of a sulfhydryl group from hydrogen sulfide to O-acetylserine by OASS, resulting in the formation of cysteine and the release of acetate.

Regulation[edit | edit source]

Cysteine synthase activity is regulated by the availability of its substrates and by feedback inhibition from cysteine itself. High levels of cysteine can inhibit the activity of SAT, thereby reducing the production of O-acetylserine and subsequently cysteine.

Clinical Significance[edit | edit source]

Deficiencies or malfunctions in cysteine synthase can lead to disorders in sulfur metabolism, affecting the synthesis of important sulfur-containing compounds. This can result in various metabolic disorders and impact the body's ability to detoxify harmful substances.

Applications[edit | edit source]

Understanding the function and regulation of cysteine synthase is important in biotechnology and medicine. It can be targeted for the development of drugs that modulate sulfur metabolism, and it is also of interest in the study of antibiotic resistance in certain bacteria.

See Also[edit | edit source]


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Contributors: Prab R. Tumpati, MD