Pea (Pisum sativum) diamine oxidase contains pyrroloquinoline quinone as a cofactor

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Pea (Pisum sativum) diamine oxidase contains pyrroloquinoline quinone as a cofactor.

Diamine oxidase was prepared from pea (Pisum sativum) seedlings by a new purification procedure involving two h.p.l.c. steps. We studied the optical and electrochemical properties of the homogeneous enzyme and also analysed the hydrolysed protein by several methods. The data presented here suggest that the carbonyl cofactor of diamine oxidase is firmly bound pyrroloquinoline quinone.

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Galactose oxidase from Dactylium dendroides was shown to contain one molecule of covalently bound pyrroloquinoline quinone (PQQ)/enzyme molecule. From the spectroscopic characteristics reported for the enzyme forms, a mechanistic role for PQQ could be deduced. In analogy with other quinoproteins, the initial formation of a PQQ-substrate adduct is proposed. Following internal hydrogen transfer, ...

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Pea, Pisum sativum, and Its Anticancer Activity

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ژورنال

عنوان ژورنال: Biochemical Journal

سال: 1987

ISSN: 0264-6021,1470-8728

DOI: 10.1042/bj2420603