Amine oxidase, Arthrobacter globiformi

In contrast to the substantial work with MAO, relatively little research has been reported on the mechanism of inhibition of copper-containing amine oxidases and SSAO by cyclopropylamines. Bovine plasma amine oxidase, equine plasma amine oxidase, Escherichia coii amine oxidase, and Arthrobacter globiformis amine oxidase were inhibited by frans-2-phenylcyclopropylamine (8a) and the mode of inhibition was shown by spectral and crystal structure analyses to be competitive and reversible [36,37,129],... 

Shepard E. M. Dooley D. M. Intramolecular electron transfer rate between active-site copper and TPQ in Arthrobacter globiformis amine oxidase. J. Biol. Inorg. Chem. 2006, 11, 1039-1048. 

Wilce, M. C. J-, Dooley, D. M., Freeman, H. C., Guss, J. M., Matsunami, H., Mclntire, W. S., Ruggiero, C. E., Tanizawa, K., and Yamaguchi, H., 1997, Crystal shnctiwes of die copper-containing amine oxidase from Arthrobacter globiformis in the holo and apo forms. Biochemistry, 36 16116fil6133. 

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.

Hess CR, Juda GA, Dooley DM, Amii RN, Hill MG, Winkler JR, Gray HB (2003) Gold electrodes wired for coupling with the deeply buried active site of Arthrobacter globiformis amine oxidase. J Am ChemSoc 125 7156-7157... 

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