Hansenula polymorpha amine oxidase

Welford R. W. D. Lam A. Mirica L. M. Klinman J. P. Partial conversion of Hansenula polymorpha amine oxidase into a plant amine oxidase implications for copper chemistry and mechanism. Biochemistry 2007, 46, 10817-10827. 

Mills S. A. Goto Y. SuQ. Plastino J. Klinman J. P. Mechanistic comparison of the cobalt-substituted and wild-type copper amine oxidase from Hansenula polymorpha. Biochemistry 2002, 41, 10577-10584. 

Takahashi K. Klinman J. P. Relationship of stopped flow to steady state parameters in the dimeric copper amine oxidase from Hansenula polymorpha and the role of zinc in inhibiting activity at alternate copper-containing subunits. Biochemistry 2006, 45, 4683 1694. 

Bruinenberg, P. G., Evers, M., Waterham, H. R., Kuipers, J., and Amberg, A. C., 1989, Cloning and sequencing of the peroxisomal amine oxidase gene from Hansenula polymorpha, Biochem. Biophys. Acta, 1008 157iil67. 

Plastino, J., Green, E. L., Sanders-Loehr, J., and Klinman, J. P., 1999, An unexpected role for the active site base in cofactor orientation and flexibility in the copper amine oxidase from Hansenula polymorpha. Biochemistry, 820488216D. 

Diamine oxidase occurs, like amine oxidase, in bacteria, animals, and plants [133]. The comparison of amino acid sequences of the amiloride-binding protein from human kidney, rat colon, diamine oxidase from human placenta, pig kidney, and amine oxidase from Hansenula polymorpha and lentil seeds has shown that the amiloride-binding protein and diamine oxidase are identical proteins[29]. The amiloride-binding protein was previously postulated to function as an epithelial sodium-transporter. While its physiological function is still... 

Table 1. Alignment of amino acid sequences of several copper amine oxidase around the position of topa quinone. The sequences were obtained by translation the corresponding cDNAs except for the enzymes from porcine kidney and porcine serum and the benzylamine oxidase from Hansenula polymorpha where they were determined by automated Edman degradation of peptides. Homologous consensus sequence around the cofactor is underlined, the tyrosyl precursor of topa quinone is shown as y.

The most recent crystallographic study discloses the structure of the methylamine oxidase from the yeast Hansenula polymorpha [31], which shows an integrated network of water molecules providing electron transfer from topa quinone to copper and other important features such as the channel for oxygen entry and hydrogen peroxide release. The role of the active site aspartate base (Asp319) in the aminotransferase mechanism of the copper amine oxidase from H. polymorpha has been probed by site-directed mutagenesis [141]. It has been demonstrated by several... 

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