MPST: Key Enzyme in Citric Acid Cycle (G4357)

Target Name: MPST

NCBI ID: G4357

MPST

MPST: Key Enzyme in Citric Acid Cycle

Mercaptopyruvate sulfur transferase (MPST) is a protein that plays a crucial role in the citric acid cycle, also known as the Krebs cycle or tricarboxylic acid (TCA) cycle, in eukaryotic cells. The MPST enzyme is involved in the transfer of sulfur from the amino acid cysteine to the amino acid tryptophan, which is the last step in the TCA cycle. This process is essential for the production of energy in the form of ATP from the energy-rich chemical bonds formed by the transfer of sulfur.

MPST is a key enzyme in the citric acid cycle, and its activity is regulated by various factors, including oxygen availability, nutrient availability, and pH levels. It is also a target for several drugs, including thiopurine drugs, which are used to treat autoimmune and inflammatory disorders.

One of the key features of MPST is its catalytic mechanism. MPST is a single-chain protein with 215 amino acid residues. It has a highly conserved active site, which is located at the intersection of its amino acid sequence. The active site is responsible for the transfer of sulfur from cysteine to tryptophan, and it is the site of the enzyme's catalytic power.

The catalytic mechanism of MPST is driven by a Michaelis-Menten-type mechanism, which means that the rate of the reaction increases as the concentration of the reactants increases. This is achieved through a combination of factors, including the presence of multiple active site sub-structures, which allow for the efficient binding and activation of different substrate molecules.

One of the key features of MPST is its role in the production of ATP from the TCA cycle. The TCA cycle is a central metabolic pathway that is involved in the production of energy in the form of ATP, as well as the synthesis of amino acids, nucleotides, and other molecules. MPST is a key enzyme in this pathway, and its activity is regulated by various factors, including oxygen availability and nutrient availability.

In addition to its role in the TCA cycle, MPST is also involved in the regulation of cellular processes that are critical for cell survival. For example, MPST is involved in the production of cysteine, which is a critical precursor for the synthesis of proteins and other molecules. It is also involved in the regulation of pH levels, which is critical for the proper functioning of many cellular processes.

The use of thiopurine drugs to treat autoimmune and inflammatory disorders is based on the inhibition of MPST activity. These drugs work by inhibiting the activity of MPST and preventing the formation of cysteine, which is a critical precursor for the synthesis of proteins and other molecules. The inhibition of MPST activity can lead to the inhibition of the production of ATP from the TCA cycle, which can result in the inhibition of cellular processes that are critical for cell survival.

In conclusion, MPST is a key enzyme involved in the citric acid cycle and the production of ATP from the TCA cycle. Its activity is regulated by various factors, including oxygen availability, nutrient availability, and pH levels. The inhibition of MPST activity has been shown to be effective in the treatment of autoimmune and inflammatory disorders. Further research is needed to fully understand the role of MPST in cellular processes and its potential as a drug target.

Protein Name: Mercaptopyruvate Sulfurtransferase

Functions: Transfer of a sulfur ion to cyanide or to other thiol compounds. Also has weak rhodanese activity. Detoxifies cyanide and is required for thiosulfate biosynthesis. Acts as an antioxidant. In combination with cysteine aminotransferase (CAT), contributes to the catabolism of cysteine and is an important producer of hydrogen sulfide in the brain, retina and vascular endothelial cells. Hydrogen sulfide H(2)S is an important synaptic modulator, signaling molecule, smooth muscle contractor and neuroprotectant. Its production by the 3MST/CAT pathway is regulated by calcium ions

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