Tryptophan tryptophylquinone
Names | |
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IUPAC name 2-Amino-3-[2-[2-amino-3-(2-carboxyethyl)-6,7-dioxo-1H-indol-4-yl]-1H-indol-3-yl]propanoic acid | |
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3D model (JSmol) |
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MeSH | Tryptophan+tryptophylquinone |
PubChem CID |
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Properties | |
Chemical formula | C22H20N4O6 |
Molar mass | 436.424 g·mol−1 |
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa). Y verify (what is YN ?) Infobox references |
Chemical compound
Tryptophan tryptophylquinone (TTQ)[1] is an enzyme cofactor, generated by posttranslational modification of amino acids within the protein. Methylamine dehydrogenase (MADH), an amine dehydrogenase, requires TTQ for its catalytic function.[2]
See also
- Amicyanin
References
- ^ Davidson, V. L.; Liu, A. (2012). "Tryptophan tryptophylquinone biosynthesis: A radical approach to posttranslational modification, by Victor L. Davidson1 and Aimin Liu2, on National Center for Biotechnology Information, U.S. National Library of Medicine, published 2012 Jan 28. doi: 10.1016/j.bbapap.2012.01.008". Biochimica et Biophysica Acta. 1824 (11): 1299–1305. doi:10.1016/j.bbapap.2012.01.008. PMC 3432176. PMID 22314272.
- ^ Davidson VL, Liu A (2009). "Uncovering novel biochemistry in the mechanism of tryptophan tryptophylquinone cofactor biosynthesis". Curr. Opin. Chem. Biol. 13 (4): 469–474. doi:10.1016/j.cbpa.2009.06.026. PMC 2749888. PMID 19648051.
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Protein primary structure and posttranslational modifications
- Peptide bond
- Protein biosynthesis
- Proteolysis
- Racemization
- N–O acyl shift
- Amidation
- Glycosyl phosphatidylinositol (GPI)
- O-methylation
- Detyrosination
Cysteine–Cysteine | |
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Methionine–Hydroxylysine | |
Lysine–Tyrosine |
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Tryptophan–Tryptophan |
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Serine–Tyrosine–Glycine |
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Histidine–Tyrosine–Glycine |
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Alanine–Serine–Glycine |
Allysine–Allysine–Allysine–Lysine |
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