Determination of the dissociation constants of pea diamine oxidase

Pec, P.; Haviger, A.; Frebort, I.

Determination of the dissociation constants of pea diamine oxidase

1992

Pec, P. | Haviger, A. | Frebort, I.

The activity of diamine oxidase [EC 1.4.3.6], (DAO) isolated from pea cotyledons was measured in Britton-Robinson buffers at pH range 5.0 - 9.6 by spectrophotometric method with E-1,4-diamino-2-butene as substrate. The enzyme has the highest activity at pH = 7.7 and in pH > 8.0 it is irreversible denaturated with time. The dissociation constants of the enzyme and enzyme-substrate complex were calculated by Dixon's method from plots of log Vmax, log K(M) and log Vmax/K(M) against pH. The pK(E)A = 6.5 suggests that histidine is in active site of DAO.

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AGROVOC Keywords

binding sites binding sites catalase chemistry enzyme activity enzymology fabaceae histidine histidine kinetics liver metabolism ph pisum sativum plants

Bibliographic information

Published in

Biochemistry international

Volume 26 Issue 1 Pagination 87 - 96 ISSN 0158-5231

Other Subjects

Hydrogen-ion concentration; Medicinal; Amine oxidase (copper-containing); Primary-amine oxidase; Substrates; Amine oxidase (copper-containing)

Language

English

Note

2019-12-05

Type

Journal Article; Text

In AGRIS since: 2024-02-27

Format: MODS

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Determination of the dissociation constants of pea diamine oxidase

1992

AGROVOC Keywords

Bibliographic information