The Scientific Panel on Food Additives, Flavourings, Processing Aids and Materials in Contact with Food (the Panel) is asked to advise the Commission on the implications for human health of chemically defined flavouring substances used in or on foodstuffs in the Member States. In particular, the Scientific Panel is asked to evaluate the 47 flavouring substances in this Flavouring Group Evaluation 6, Revision 1 (FGE.06Rev1), using the procedure as referred to in the Commission Regulation EC No 1565/2000. These 47 flavouring substances belong to chemical groups 1 and 4 of Annex I of the Commission Regulation (EC) No 1565/2000.

Opinion of the Scientific Panel on Food Additives, Flavourings, Processing Aids and Materials in contact with Food (AFC) on a request from the Commission, Flavouring Group Evaluation 22: Ring-substituted phenolic substances from chemical groups 21 and 25: Question No EFSA-Q-2003-165

The FEMA GRAS assessment of benzyl derivatives used as flavor ingredients.

(1985). Molybdenum Hydroxylases as Drug-Metabolizing Enzymes. Drug Metabolism Reviews: Vol. 16, No. 1-2, pp. 119-156.

Molybdenum Hydroxylases as Drug-Metabolizing Enzymes

The enzyme “aldehyde oxidase” is an iminium oxidase. Reaction with nicotine Δ1′(5′) iminium ion

Mammalian aldehyde oxidases (AOXs; EC1.2.3.1) are a group of conserved proteins belonging to the family of molybdo-flavoenzymes along with the structurally related xanthine dehydrogenase enzyme. AOXs are characterized by broad substrate specificity, oxidizing not only aromatic and aliphatic aldehydes into the corresponding carboxylic acids, but also hydroxylating a series of heteroaromatic rings. The number of AOX isoenzymes expressed in different vertebrate species is variable. The two extremes are represented by humans, which express a single enzyme (AOX1) in many organs and mice or rats which are characterized by tissue-specific expression of four isoforms (AOX1, AOX2, AOX3, and AOX4). In vertebrates each AOX isoenzyme is the product of a distinct gene consisting of 35 highly conserved exons. The extant species-specific complement of AOX isoenzymes is the result of a complex evolutionary process consisting of a first phase characterized by a series of asynchronous gene duplications and a second phase where the pseudogenization and gene deletion events prevail. In the last few years remarkable advances in the elucidation of the structural characteristics and the catalytic mechanisms of mammalian AOXs have been made thanks to the successful crystallization of human AOX1 and mouse AOX3. Much less is known about the physiological function and physiological substrates of human AOX1 and other mammalian AOX isoenzymes, although the importance of these proteins in xenobiotic metabolism is fairly well established and their relevance in drug development is increasing. This review article provides an overview and a discussion of the current knowledge on mammalian AOX.

Structure and function of mammalian aldehyde oxidases

1. Isoquinoline, cinnoline, quinoxaline, quinazoline and phthalazine were incubated with preparations of rabbit liver aldehyde oxidase. 2. The oxidation products, 1-hydroxyisoquinoline, 4-hydroxycinnoline, 2-hydroxy- and 2,3-dihydroxy-quinoxaline, 4-hydroxy- and 2,4-dihydroxy-quinazoline, and 1-hydroxyphthalazine were identified by comparison of their spectral and chromatographic characteristics with those of authentic compounds. 3. Michaelis-Menten constants are reported for the action of the parent heterocycles with aldehyde oxidase. The compounds reported in this study are among the most efficient substrates yet described for rabbit liver aldehyde oxidase. 4. The compounds in 1 above were incubated with bovine milk xanthine oxidase: only quinazoline and phthalazine yielded significant amounts of metabolites. Km values were calculated for these compounds. 5. Incubation of the heterocycles with rat liver preparations gave qualitatively the same results as those obtained using rabbit liver, but smaller amounts of the oxidation products were detected from rat liver incubations.

The oxidation of azaheterocycles with mammalian liver aldehyde oxidase.

Most r e p o r t s on t h e o x i d a t i v e metabol ism of d rugs are c o n f i n e d t o t h e membranebound microsomal cytochrome P-450 system. However, a n o t h e r enzyme, a ldehyde o x i d a s e , p r e s e n t i n t h e c y t o s o l of l i v e r c e l l s , is c a p a b l e of c a t a l y s i n g t h e hydroxy la t io t of c e r t a i n aromatic N-he te rocyc le s . Although it i s p r e s e n t i nman ( S t a n l o v i c & Chaykin, 1971) , t h e l e v e l of t h i s enzyme is s p e c i e s dependen t , and is most abundant i n r a b b i t l i v e r , which was used i n t h e p r e s e n t s t u d y . Th i s p a p e r r e p o r t s t h e r e s u l t s of i n v i t r o s t u d i e s o f t h e metabol ism o f some mono and d i a z a h e t e r o c y c l e s by t h e above enzymes. Compounds were i n c u b a t e d w i t h t h e a ldehyde o x i d a s e c o n t a i n i n g 100 000 g s u p e r n a t a n t f r a c t i o n and t h e p r o d u c t s were i d e n t i f i e d by comparison o f t h e i r ch romatograph ic and s p e c t r o s c o p i c p r o p e r t i e s w i t h t h o s e o f a u t h e n t i c compounds. v e r s i o n was obse rved i n most cases. Km v a l u e s were de t e rmined d i r e c t l y or by t h e method of K r e n i t s k y & o t h e r s (1372) u s i n g p a r t i a l l y p u r i f i e d enzyme. O x i d a t i o n by t h e cytochrome P-450 sys t em was i n v e s t i g a t e d u s i n g e i t h e r t h e 10,000 g s u p e r n a t a n t f r a c t i o n or t h e 100 000 g microsomal p e l l e t .

The metabolism of N-heterocycles [proceedings].

F r e s h l y prepared s l i c e s of r a b b i t l i v e r , which i s a p a r t i c u l a r l y r i c h source of aldehyde oxidase, xere incubated with phtha laz ine i n the presence of hydralazine. The oxida t ion of ph tha laz ine was monitore4 b y HgLC over a n i n e t y minute per iod and was found t o b e cons iderably reduced conpared t o c o n t r o l incubat ions cont a i n i n g no drug.

The inhibition of rabbit liver aldehyde oxidase by hydralazine

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The oxidation of azaheterocycles with mammalian liver aldehyde oxidase.

The metabolism of N-heterocycles [proceedings].

The inhibition of rabbit liver aldehyde oxidase by hydralazine