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. 1988 Sep 26;238(1):74-6.
doi: 10.1016/0014-5793(88)80228-x.

Unprecedented lysyloxidase activity of Pichia pastoris benzylamine oxidase

S S Tur  1 , K Lerch
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Free article

Unprecedented lysyloxidase activity of Pichia pastoris benzylamine oxidase

S S Tur et al. FEBS Lett. .
Free article

Abstract

Benzylamine oxidase (EC 1.4.3.6) from the yeast Pichia pastoris is a 106 kDa quinoprotein containing one copper atom per molecule. It has a broad substrate specificity ranging from butylamine to peptidyl lysine in collagen and elastin. The kinetic data obtained using lysine-containing model peptides as substrates indicate an astonishing similarity to mammalian lysyloxidase. This similarity is further supported by the inhibition of both enzymes with beta-aminopropionitrile.

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