Escherichia coli amine oxidase

C.G. Saysell, W.S. Tambyrajah, J.M. Murray, C.M. Wilmot, S.E.V. Philips, M.J. McPherson, P.F. Knowles, Probing the catalytic mechanism of Escherichia coli amine oxidase using mutational variants and a reversible inhibitor as a substrate analogue, Biochem. J. 365 (2002) 809-816. 

Murray, J. M., Wilmot, C. M., Saysell, C. G., Jaeger, J., Knowles, P. F., Phillips, S. E. V., and McPherson, M. J., 1999, The active site base controls cofactor reactivity in Escherichia coli amine oxidase X-ray crystallographic studies with mutational variants. Biochemistry, 38 8217n8227. 

The deamination of primary amines such as phenylethylamine by Escherichia coli (Cooper et al. 1992) and Klebsiella oxytoca (Flacisalihoglu et al. 1997) is carried out by an oxidase. This contains copper and topaquinone (TPQ), which is produced from tyrosine by dioxygenation. TPQ is reduced to an aminoquinol that in the form of a Cu(l) radical reacts with O2 to form H2O2, Cu(ll), and the imine. The mechanism has been elucidated (Wihnot et al. 1999), and involves formation of a Schiff base followed by hydrolysis in reactions that are formally analogous to those involved in pyridoxal-mediated transamination. 

Cooper RA, PE Knowles, DE Brown, MA McGuirl, DM Dooley (1992) Evidence for copper and 3,4,6-trihy-droxyphenylalanine quinone cofactor as an amine oxidase from Gram-negative Escherichia coli K-12. Biochem J 288 337-340. 

Amine oxidase from Aspergillus niger and monoamine oxidase from Escherichia coli can be used for the oxidative deamination of amines, forming the corre-... 

Yoshida et al. (1997) achieved the production of vanillin by oxidation of vanillylamine using amine oxidase (AO) from Aspergillus niger and monoamine oxidase (MAO) from Escherichia coli. Enzyme kinetic studies have revealed that AO is... 

Moenne-Loccoz, P., Nakamura, N., Steinebach, V., Duine, J. A., Mure, M., Klinman, J. P., and Sanders-Loehr, J., 1995, Characterisation of the TOPA quinone cofactor in amine oxidase from Escherichia coli by resonance Raman spectroscopy, 1995 Biochemistry 34 7020n7026. 

The enantioselective oxidation of amphetamine SS by copper containing amine oxidases from Escherichia coli and Klebsiella oxytoca was reported in 2000 by Had salihoglu et al. [34] Moderate E values of 1S were obtained, opening up the possibility for future applications of amine oxidase catalyzed resolutions of substi tuted amphetamines (Figure 14.2S). 

The crystal structure of amine oxidase from Escherichia coli reveals that the C-terminal domain (440 amino acids) primarily has a /3-sandwich structure. This domain contains the active site with a type 2 copper center, the cofactor, and the dimerization contact site. Furthermore, there are three domains of approximately 100 amino acids length which have an a- and a /3-structure. The second and third of these smaller domains show marked sequence homology and are conserved in the amine oxidases of various organisms. The first of these smaller domains may, however, be lacking in some amine oxidases [28]. The structure of an eukariotic aminoxidase from pea seedling is seen in [121]. 

The crystal structure of CuAO has been solved from Escherichia coli (ECAO), pea seedling (PSAO), Arthrobacter globiformis (AGAO), Hansetmla polymorpha (HPAO), Pichia pastoris (PPLO), " bovine serum amine oxidase (BSAO), ° and human vascular adhesion protein (VAP-1). ... 

In the amine oxidase from Escherichia coli, the topa quinone was confirmed by a detailed analysis of the cofactor dipeptide X-Asp [67] and the resonance Raman spectrometry of the enzyme and its derivatives[68,69]. The primary structure of the enzyme also contains the cofactor consensus sequence [70]. More bacterial genes were shown to encode proteins containing the topa quinone consensus sequence, such as amine oxidase from Klebsiella aerogenes [71], phenethylamine oxidase and histamine oxidase from Arthrobacter globiformis [72,73], and methylamine oxidase from Arthrobacter strain PI [74]. Amino acid sequences around the position of the cofactor for selected amine oxidases from various sources are given in Table 1. 

Fig. (2). Ribbon diagram of the three-dimensional crystal structure of copper amine oxidase from Escherichia coli [28], Similar structures of amine oxidases from pea seedlings [29], Arthrobacter globiformis [30] and Hansenula pclymorpha [31 ] lack the domain D1.

Autocatalytic formation of topa quinone in prokaryotic copper amine oxidases has already been demonstrated several times in vitro. Escherichia coli K-12 produced almost inactive amine oxidase after... 

Recently, Knowles and co-workers using flash-freezing techniques obtained x-ray crystal structures of several species related to the oxidative half reaction of the amine oxidase from Escherichia coli. The structure of the anaerobically P-phenylethylamine-reduced amine oxidase shows that the reduced cofactor TPQ exists in the aminoquinol form possessing a hydrogen bond between the 0-2 of the aminoquinol and axial water that coordinates to the copper ion, while the product phenylacetaldehyde remains bound at the... 

Hacisalihoglu, A., Jongejan, A., Jongejan, J. A., and Durne, J. A., "Enantioselective oxidation of amphetamine by copper-containing quinoprotein amine oxidases from Escherichia coli and Klebsiella oxytoca.". Mol. Catal. B Enzym., 11,81-88 (2000). 

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