Your browser doesn't support javascript.
loading
Unprecedented lysyloxidase activity of Pichia pastoris benzylamine oxidase.
Tur, S S; Lerch, K.
Afiliação
  • Tur SS; Biochemisches Institut Universität Zürich, Switzerland.
FEBS Lett ; 238(1): 74-6, 1988 Sep 26.
Article em En | MEDLINE | ID: mdl-2901988
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.
Assuntos
Buscar no Google
Base de dados: MEDLINE Assunto principal: Pichia / Benzilamina Oxidase / Saccharomycetales / Aminoácido Oxirredutases / Proteína-Lisina 6-Oxidase / Monoaminoxidase Idioma: En Ano de publicação: 1988 Tipo de documento: Article
Buscar no Google
Base de dados: MEDLINE Assunto principal: Pichia / Benzilamina Oxidase / Saccharomycetales / Aminoácido Oxirredutases / Proteína-Lisina 6-Oxidase / Monoaminoxidase Idioma: En Ano de publicação: 1988 Tipo de documento: Article