Kinetics and specificity of guinea pig liver aldehyde oxidase and bovine milk xanthine oxidase towards substituted benzaldehydes

• Autorzy: Panoutsopoulos G. I. , Beedham C.
• Języki publikacji: EN

Abstrakty

EN

Molybdenum-containing enzymes, aldehyde oxidase and xanthine oxidase, are im­portant in the oxidation of N-heterocyclic xenobiotics. However, the role of these en­zymes in the oxidation of drug-derived aldehydes has not been established. The present investigation describes the interaction of eleven structurally related benzaldehydes with guinea pig liver aldehyde oxidase and bovine milk xanthine oxidase, since they have similar substrate specificity to human molybdenum hydroxylases. The compounds under test included mono-hydroxy and mono-methoxy benzaldehydes as well as 3,4-dihydroxy-, 3-hydroxy-4-methoxy-, 4-hydroxy-3-metho- xy-, and 3,4-dimethoxy-benzaldehydes. In addition, various amines and catechols were tested with the molybdenum hydroxylases as inhibitors of benzaldehyde oxida­tion. The kinetic constants have shown that hydroxy-, and methoxy-benzaldehydes are excellent substrates for aldehyde oxidase (Km values 5*10 M to 1^10 M) with lower affinities for xanthine oxidase (Km values around 10- M). Therefore, alde­hyde oxidase activity may be a significant factor in the oxidation of the aromatic alde­hydes generated from amines and alkyl benzenes during drug metabolism. Com­pounds with a 3-methoxy group showed relatively high Vmax values with aldehyde oxidase, whereas the presence of a 3-hydroxy group resulted in minimal Vmax values or no reaction. In addition, amines acted as weak inhibitors, whereas catechols had a more pronounced inhibitory effect on the aldehyde oxidase activity. It is therefore possible that aldehyde oxidase may be critical in the oxidation of the analogous phenylacetaldehydes derived from dopamine and noradrenaline.

Słowa kluczowe

EN

aldehyde oxidase; xanthine oxidase; specificity; protocatechuic aldehyde; dopamine; benzaldehyde; guinea pig; bovine milk; kinetics; liver; isovanillin

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2004
• Tom: 51
• Numer: 3
• Opis fizyczny: p.649-663,fig.,ref.

Twórcy

autor

Panoutsopoulos G. I.

• University of Bradford, Bradford, U.K.

autor

Beedham C.

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