Aromatic amine dehydrogenase
From Proteopedia
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| - | <StructureSection load='2i0s' size=' | + | <StructureSection load='2i0s' size='350' side='right' caption='Structure of aromatic amine dehydrogenase large subunit (cyan and green) and small subunit (magenta and salmon) with cofactor TTQ complex with phenylacetaldehyde (PDB code [[2i0s]]).' scene='59/593968/Cv/1'> |
== Function == | == Function == | ||
| - | '''Aromatic amine dehydrogenase''' (AADH) catalyzes the conversion of primary aromatic amine and acceptor to aldehyde and reduced acceptor. The acceptor co-factor is tryptophan tryptophylquinone (TTQ). | + | '''Aromatic amine dehydrogenase''' (AADH) catalyzes the conversion of primary aromatic amine and acceptor to aldehyde and reduced acceptor. The acceptor co-factor is tryptophan tryptophylquinone (TTQ).<ref>PMID:8188594</ref> |
| - | == | + | == Structural highlights == |
| - | == | + | AADH structure consists of <scene name='59/593968/Cv/2'>2 large</scene> and <scene name='59/593968/Cv/3'>2 small subunits</scene> with the <scene name='59/593968/Cv/5'>co-factor TTQ attached covalently to the small subunit</scene>.<ref>PMID:17475620</ref> |
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==3D structures of aromatic amine dehydrogenase== | ==3D structures of aromatic amine dehydrogenase== | ||
| + | [[Aromatic amine dehydrogenase 3D structures]] | ||
| - | + | </StructureSection> | |
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== References == | == References == | ||
Current revision
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References
- ↑ Govindaraj S, Eisenstein E, Jones LH, Sanders-Loehr J, Chistoserdov AY, Davidson VL, Edwards SL. Aromatic amine dehydrogenase, a second tryptophan tryptophylquinone enzyme. J Bacteriol. 1994 May;176(10):2922-9. PMID:8188594
- ↑ Roujeinikova A, Hothi P, Masgrau L, Sutcliffe MJ, Scrutton NS, Leys D. New insights into the reductive half-reaction mechanism of aromatic amine dehydrogenase revealed by reaction with carbinolamine substrates. J Biol Chem. 2007 Aug 17;282(33):23766-77. Epub 2007 May 1. PMID:17475620 doi:10.1074/jbc.M700677200
