Aromatic amine dehydrogenase

Tryptophan tryptophanylquinone (TTQ). This recently discovered quinone cofactor is similar to the lysyl tyrosylquinone but is formed from two trypto-phanyl side chains.466 It has been found in methyl-amine dehydrogenase from methylotrophic gramnegative bacteria467-469 and also in a bacterial aromatic amine dehydrogenase.470... 

Govindaraj, S., Eisenstein, E., Jones, L. H., Sanders-Loehr, J., Chistoserdov, A. Y., Davidson, V. L., and Edwards, S. L. 1994, Aromatic amine dehydrogenase, a second tryptophan tryptophylquinone enzyme. J. Bacterial. 176 292292929. 

Hyun, Y-L., and Davidson V. L., 1995, Electron transfer reactions between aromatic amine dehydrogenase and azurin. Biochemistry 34 12249912254. 

Iwaki, M., Yagi, T., Horiike, K., Saeki, Y., Ushijima, T., and Nozaki, M. (1983) Crystallization and properties of aromatic amine dehydrogenase from Pseudomonas sp. Arch. Biochem. Biophys., 220,... 

FIGURE 57-3. Dopamine metabolism in presynaptic dopamine neuron (see text for full details). 30MD, 3-O-methyldopa AC, adenylate cyclase AD, aldehyde dehydrogenase COMT, catechol-O-methyl transferase D1-D3, dopamine receptors DA, dopamine DAT, dopamine transporter DOPAC, 3,4-dihydroxyphenylacetic acid HVA, homovanillic acid r-AAD, r-aromatic amine decarboxylase MAO-B, monoamine oxidase B TH, tyrosine hydroxylase. 

Major oxidations are aromatic, aliphatic, alicyclic, heterocyclic, N-oxidation, S-oxidation, dealkylation. Other enzymes also catalyze phase 1 reactions microsomal flavin monooxygenases, amine oxidases, peroxidases, and alcohol dehydrogenase. 

Other thermophilic enzymes from archaea may be used for analytical and preparative purposes. For instance, the glucose dehydrogenase from S. solfataricus [70] may serve as a suitable tool for glucose determination, whereas the relatively broad substrate spectrum of the esterase from S. acidocaldarius (catalyzes the acyl transfer to various alcohols and amines [71]) or of the alcohol dehydrogenase from S. solfataricus (oxidizes various aliphatic and aromatic alcohols [72]) makes these enzymes rather attractive for... 

The biosynthesis of other volatile phenyl-propanoid-related compoimds such as phenyla-cetaldehyde and 2-phenylethanol, does not occur via trans-cinnamic acid and competes with PAL for Phe utilization [90, 96, 97]. Phenylacetaldehyde biosynthesis from Phe requires the removal of both the carboxyl and amino groups. A classical sequential two-step removal is believed to occur in tomato where Phe was shown to be first converted to phe-nylethylamine by aromatic amino acid decarboxylase (AADC) and further required the action of a hypothesized amine oxidase, dehydrogenase, or transaminase for phenylacetaldehyde formation [97]. On the other hand, in petunia, one bifunctional enzyme, phenylacetaldehyde synthase (PAAS) catalyzes the unprecedented efficient coupling of Phe decarboxylation to oxidation resulting in... 

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