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  2. Sulfur metabolism - Wikipedia

    en.wikipedia.org/wiki/Sulfur_metabolism

    From the sulfide they form the amino acids cysteine and methionine, sulfolipids, and other sulfur compounds. Animals obtain sulfur from cysteine and methionine in the protein that they consume. Sulfur is the third most abundant mineral element in the body. [21] The amino acids cysteine and methionine are used by the body to make glutathione.

  3. Sulfur assimilation - Wikipedia

    en.wikipedia.org/wiki/Sulfur_assimilation

    Furthermore, the reduced sulfur is incorporated into cysteine, [2] an amino acid that is a precursor to many other sulfur-containing compounds. In animals, sulfur assimilation occurs primarily through the diet, as animals cannot produce sulfur-containing compounds directly.

  4. Cystathionine beta synthase - Wikipedia

    en.wikipedia.org/wiki/Cystathionine_beta_synthase

    CBS occupies a pivotal position in mammalian sulfur metabolism at the homocysteine junction where the decision to conserve methionine or to convert it to cysteine via the transsulfuration pathway, is made. Moreover, the transsulfuration pathway is the only pathway capable of removing sulfur-containing amino acids under conditions of excess. [9]

  5. Microbial metabolism - Wikipedia

    en.wikipedia.org/wiki/Microbial_metabolism

    Sulfur oxidation involves the oxidation of reduced sulfur compounds (such as sulfide H 2 S), inorganic sulfur (S), and thiosulfate (S 2 O 2− 3) to form sulfuric acid (H 2 SO 4). A classic example of a sulfur-oxidizing bacterium is Beggiatoa, a microbe originally described by Sergei Winogradsky, one of the founders of environmental microbiology.

  6. Sulfur-reducing bacteria - Wikipedia

    en.wikipedia.org/wiki/Sulfur-reducing_bacteria

    Desulfuromusa genus includes bacteria obligately anaerobic that use sulfur as an electron acceptor and short-chain fatty acids, dicarboxylic acids, and amino acids, as electron donors that are oxidized completely to CO 2. They are gram negative and complete oxidizer bacteria; their cells are motile and slightly curved or rod shaped.

  7. Adenylyl-sulfate reductase (thioredoxin) - Wikipedia

    en.wikipedia.org/wiki/Adenylyl-sulfate_reductase...

    The thioredoxin dependent adenylyl-sulfate reductase's cleaved disulfuric ions are incorporated into the molecular structure of the proto-proteins in the formation of the aforementioned amino acids. In studies such as one published in the Journal of Biological Chemistry experimentally observed the use of this enzyme type and thioredoxin in the ...

  8. Biosynthesis - Wikipedia

    en.wikipedia.org/wiki/Biosynthesis

    The different amino acids are identified by the functional group. As a result of the three different groups attached to the α-carbon, amino acids are asymmetrical molecules. For all standard amino acids, except glycine, the α-carbon is a chiral center. In the case of glycine, the α-carbon has two hydrogen atoms, thus adding symmetry to this ...

  9. Sulfur - Wikipedia

    en.wikipedia.org/wiki/Sulfur

    This is an accepted version of this page This is the latest accepted revision, reviewed on 1 February 2025. This article is about the chemical element. For other uses, see Sulfur (disambiguation). Chemical element with atomic number 16 (S) Sulfur, 16 S Sulfur Alternative name Sulphur (pre-1992 British spelling) Allotropes see Allotropes of sulfur Appearance Lemon yellow sintered microcrystals ...