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- W2010132684 abstract "Methylamine dehydrogenase (MADH) possesses an alpha(2)beta(2) subunit structure with each smaller beta subunit possessing a tryptophan tryptophylquinone (TTQ) prosthetic group. Phe(55) of the alpha subunit is located where the substrate channel from the enzyme surface opens into the active site. Site-directed mutagenesis studies have revealed several roles for this residue in catalysis and electron transfer (ET) by MADH. Site-directed mutagenesis of either alpha Phe(55) or beta Ile(107) (a residue in the beta subunit which interacts with alpha Phe(55)) converts MADH into enzymes with specificities for long-chain amines, amylamine or propylamine. Mutation of alpha Phe(55) also affects monovalent cation binding to the active site. alpha F55A MADH exhibits an increased K(d) for cation-dependent spectral changes and a decreased K(d) for cation-dependent stimulation of the rate of gated ET from N-quinol MADH to amicyanin. These results demonstrate that alpha Phe(55) is able to directly participate in a wide range of biochemical processes not typically observed for a phenylalanine residue." @default.
- W2010132684 created "2016-06-24" @default.
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- W2010132684 date "2003-04-01" @default.
- W2010132684 modified "2023-09-23" @default.
- W2010132684 title "Probing mechanisms of catalysis and electron transfer by methylamine dehydrogenase by site-directed mutagenesis of αPhe55" @default.
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- W2010132684 doi "https://doi.org/10.1016/s1570-9639(03)00056-6" @default.
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