Structures of the carbinolamine and schiff-base intermediates in the reductive half-reaction of aromatic amine dehydrogenase (AADH) with p-methoxyphenylethylamine
2hkr is a 4 chain structure with sequence from Alcaligenes faecalis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
AAUB_ALCFA Oxidizes primary aromatic amines and, more slowly, some long-chain aliphatic amines, but not methylamine or ethylamine. Uses azurin as an electron acceptor to transfer electrons from the reduced tryptophylquinone cofactor.[1][2][3][4]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
↑Chistoserdov AY. Cloning, sequencing and mutagenesis of the genes for aromatic amine dehydrogenase from Alcaligenes faecalis and evolution of amine dehydrogenases. Microbiology. 2001 Aug;147(Pt 8):2195-202. PMID:11495996
↑Hothi P, Khadra KA, Combe JP, Leys D, Scrutton NS. Tryptophan tryptophylquinone cofactor biogenesis in the aromatic amine dehydrogenase of Alcaligenes faecalis. Cofactor assembly and catalytic properties of recombinant enzyme expressed in Paracoccus denitrificans. FEBS J. 2005 Nov;272(22):5894-909. PMID:16279953 doi:https://dx.doi.org/EJB4990
↑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
↑Masgrau L, Roujeinikova A, Johannissen LO, Hothi P, Basran J, Ranaghan KE, Mulholland AJ, Sutcliffe MJ, Scrutton NS, Leys D. Atomic description of an enzyme reaction dominated by proton tunneling. Science. 2006 Apr 14;312(5771):237-41. PMID:16614214 doi:312/5771/237