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Literature summary for 1.11.2.2 extracted from
- Human neutrophils employ the myeloperoxidase-hydrogen peroxide-chloride system to oxidize alpha-amino acids to a family of reactive aldehydes. Mechanistic studies identifying labile intermediates along the reaction pathway (1998), J. Biol. Chem., 273, 4997-5005.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| neutrophil | - |
Homo sapiens | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Cl- + H2O2 + H+ | - |
Homo sapiens | HClO + H2O | - |
? |  |
| additional information | only amino acids with free amino and carboxylic acid groups on the alpha-carbon yield aldehydes when oxidized by the myeloperoxidase-H2O2-Cl- system. Incubation of the alpha-amino blocked analog Nalpha-acetyllysine with the complete myeloperoxidase system fails to generate detectable aldehyde | Homo sapiens | ? | - |
? | |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| heme | - |
Homo sapiens | |
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Release 2023.1 (January 2023)
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