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Article title matches
- Category:Tryptophan tryptophylquinone (59 bytes)
1: List of pages with the keyword Tryptophan tryptophylquinone - Category:Trytpophan tryptophylquinone (59 bytes)
1: List of pages with the keyword Trytpophan tryptophylquinone - Category:Cystein tryptophylquinone (56 bytes)
1: List of pages with the keyword Cystein tryptophylquinone - Category:Tryptophylquinone (48 bytes)
1: List of pages with the keyword Tryptophylquinone
Page text matches
- 2iuq (5,270 bytes)
11: ...n acceptor to transfer electrons from the reduced tryptophylquinone cofactor.<ref>PMID:11495996</ref> <ref>PMID:16279...
24: ...ogenase (AADH) uses a covalently bound tryptophan tryptophylquinone (TTQ) cofactor to oxidatively deaminate primary a... - 2iup (5,248 bytes)
11: ...n acceptor to transfer electrons from the reduced tryptophylquinone cofactor.<ref>PMID:11495996</ref> <ref>PMID:16279...
24: ...ogenase (AADH) uses a covalently bound tryptophan tryptophylquinone (TTQ) cofactor to oxidatively deaminate primary a... - 2iur (5,197 bytes)
11: ...n acceptor to transfer electrons from the reduced tryptophylquinone cofactor.<ref>PMID:11495996</ref> <ref>PMID:16279...
24: ...ogenase (AADH) uses a covalently bound tryptophan tryptophylquinone (TTQ) cofactor to oxidatively deaminate primary a... - 2iuv (5,188 bytes)
11: ...n acceptor to transfer electrons from the reduced tryptophylquinone cofactor.<ref>PMID:11495996</ref> <ref>PMID:16279...
24: ...ogenase (AADH) uses a covalently bound tryptophan tryptophylquinone (TTQ) cofactor to oxidatively deaminate primary a... - 1jju (4,418 bytes)
24: ... is contained an unusual redox cofactor, cysteine tryptophylquinone (CTQ), consisting of an orthoquinone-modified try... - 1jmx (4,331 bytes)
24: ...nal chemical cross-links that encage the cysteine tryptophylquinone cofactor, involving a cysteine side chain bridged... - 1jmz (4,327 bytes)
24: ...nal chemical cross-links that encage the cysteine tryptophylquinone cofactor, involving a cysteine side chain bridged... - 1pby (4,473 bytes)
24: ...ificans contains a novel redox cofactor, cysteine tryptophylquinone (CTQ). This cofactor is derived from a pair of ge... - 2agl (3,264 bytes)
11: ...n acceptor to transfer electrons from the reduced tryptophylquinone cofactor.<ref>PMID:11495996</ref> <ref>PMID:16279... - 2agw (4,565 bytes)
11: ...n acceptor to transfer electrons from the reduced tryptophylquinone cofactor.<ref>PMID:11495996</ref> <ref>PMID:16279... - 2agx (4,578 bytes)
11: ...n acceptor to transfer electrons from the reduced tryptophylquinone cofactor.<ref>PMID:11495996</ref> <ref>PMID:16279... - 2agy (4,581 bytes)
11: ...n acceptor to transfer electrons from the reduced tryptophylquinone cofactor.<ref>PMID:11495996</ref> <ref>PMID:16279... - 2agz (4,635 bytes)
11: ...n acceptor to transfer electrons from the reduced tryptophylquinone cofactor.<ref>PMID:11495996</ref> <ref>PMID:16279... - 2ah1 (4,442 bytes)
11: ...n acceptor to transfer electrons from the reduced tryptophylquinone cofactor.<ref>PMID:11495996</ref> <ref>PMID:16279... - 2bbk (4,854 bytes)
24: ...ins that form the unique redox center, tryptophan tryptophylquinone (TTQ). The active site contains the O-6 carbonyl ... - 2h3x (5,262 bytes)
11: ...n acceptor to transfer electrons from the reduced tryptophylquinone cofactor.<ref>PMID:11495996</ref> <ref>PMID:16279...
24: ...ed. Electrons are transferred from the tryptophan tryptophylquinone (TTQ) cofactor of AADH to the type I copper of th... - 2h47 (5,337 bytes)
11: ...n acceptor to transfer electrons from the reduced tryptophylquinone cofactor.<ref>PMID:11495996</ref> <ref>PMID:16279...
24: ...ed. Electrons are transferred from the tryptophan tryptophylquinone (TTQ) cofactor of AADH to the type I copper of th... - 2hxc (5,242 bytes)
11: ...n acceptor to transfer electrons from the reduced tryptophylquinone cofactor.<ref>PMID:11495996</ref> <ref>PMID:16279...
24: ...ogenase (AADH) uses a covalently bound tryptophan tryptophylquinone (TTQ) cofactor to oxidatively deaminate primary a... - 2i0r (5,195 bytes)
11: ...n acceptor to transfer electrons from the reduced tryptophylquinone cofactor.<ref>PMID:11495996</ref> <ref>PMID:16279...
24: Aromatic amine dehydrogenase uses a tryptophan tryptophylquinone (TTQ) cofactor to oxidatively deaminate primary a... - 2i0s (5,319 bytes)
11: ...n acceptor to transfer electrons from the reduced tryptophylquinone cofactor.<ref>PMID:11495996</ref> <ref>PMID:16279...
24: Aromatic amine dehydrogenase uses a tryptophan tryptophylquinone (TTQ) cofactor to oxidatively deaminate primary a...
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