tryptophan tryptophylquinone
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| verifiedrevid = 434501491
| ImageFile=Tryptophan tryptophylquinone.svg
| ImageSize=200px
| IUPACName=2-Amino-3-[2-[2-amino-3-(2-carboxyethyl)-6,7-dioxo-1H-indol-4-yl]-1H-indol-3-yl]propanoic acid
| OtherNames=
|Section1={{Chembox Identifiers
| CASNo_Ref = {{cascite|correct|??}}
| CASNo=134645-25-3
| PubChem=5486829
| SMILES = C1=CC=C2C(=C1)C(=C(N2)C3=CC(=O)C(=O)C4=C3C(=C(N4)N)CCC(=O)O)CC(C(=O)O)N
| MeSHName=Tryptophan+tryptophylquinone
}}
|Section2={{Chembox Properties
| C=22| H=20 | N=4 | O=6
| Appearance=
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|Section3={{Chembox Hazards
| MainHazards=
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Tryptophan tryptophylquinone (TTQ){{cite journal|title= 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|year= 2012|pmc= 3432176|last1= Davidson|first1= V. L.|last2= Liu|first2= A.|journal= Biochimica et Biophysica Acta|volume= 1824|issue= 11|pages= 1299–1305|doi= 10.1016/j.bbapap.2012.01.008|pmid= 22314272}} 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.{{cite journal | author = Davidson VL, Liu A | title = Uncovering novel biochemistry in the mechanism of tryptophan tryptophylquinone cofactor biosynthesis | journal = Curr. Opin. Chem. Biol. | date = 2009 | volume = 13 | issue = 4 | pages = 469–474 | doi = 10.1016/j.cbpa.2009.06.026 | pmid = 19648051 | pmc = 2749888 }}