Aromatic amine dehydrogenase

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).^[1]

Structural highlights

AADH structure consists of and with the .^[2]

3D structures of aromatic amine dehydrogenase

Aromatic amine dehydrogenase 3D structures

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).

Drag the structure with the mouse to rotate

ReferencesReferences

↑ 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

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

[1] 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

[2] 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

[1]

[2]