Unprecedented lysyloxidase activity of Pichia pastoris benzylamine oxidase.

Tur SS; Lerch K

doi:10.1016/0014-5793(88)80228-x

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Journal article

Unprecedented lysyloxidase activity of Pichia pastoris benzylamine oxidase.

Tur SS Biochemisches Institut Universität Zürich, Switzerland.
Lerch K

1988-09-26

Published in:

FEBS letters. - 1988

English 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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