Soybean lipoxygenase: Substrate structure and product selectivity

Scheller, G.; Jäger, E.; Hoffmann, Bastian; Schmitt, Melanie; Schreier, Peter

doi:10.1021/jf00055a005

Cited by 16 publications

(9 citation statements)

References 8 publications

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“…Conjugated hydroperoxydienes 1b-5b were obtained by enzymatic oxidation of the corresponding 3′(Z),6′(Z)-dienes 1a-5a with soybean LOX-1 (Scheme 1) (20). Steric analysis of the hydroperoxy products (see Ref.…”

Section: Resultsmentioning

confidence: 99%

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Catalytic properties of allene oxide synthase from flaxseed (Linum usitatissimum L.)

Schneider

Schreier

1998

Lipids

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We investigated the catalytic and kinetic properties of allene oxide synthase (AOS; E.C. 4.2.1.92) from flaxseed (Linum usitatissimum L.). Both Michaelis constant and maximal initial velocity for the conversion of 9(S)- and 13(S)-hydroperoxides of linoleic and linolenic acid were determined by a photometric assay. 13(S)-Hydroperoxy-9(Z), 11(E)-octadecadienoic acid [13(S)-HPOD] as the most effective substrate was converted at 116.9 +/- 5.8 nkat/mg protein by the flax enzyme extract. The enzyme was also incubated with a series of variable conjugated hydroperoxy dienyladipates. Substrates with a shape similar to the natural hydroperoxides showed the best reactivity. Monoenoic substrates as oleic acid hydroperoxides were not converted by the enzyme. In contrast, 12-hydroperoxy-9(Z), 13(E)-octadecadienoic acid was a strong competitive inhibitor for AOS catalyzed degradation of 13(S)-HPOD. The inhibitor constant was determined to be 0.09 microM. Based on these results, we concluded that allene oxide synthase requires conjugated diene hydroperoxides for successful catalysis. Studying the enantiomeric preference of the enzyme, we found that AOS was also able to metabolize (R)-configurated fatty acid hydroperoxides. Conversion of these substrates into labile allene oxides was confirmed by steric analysis of the stable alpha-ketol hydrolysis products.

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Section: Resultsmentioning

confidence: 99%

“…The variable conjugated 3′(Z),5′(E)-7′-hydroperoxides 1b-5b were obtained by soybean LOX-1 oxygenation of the corresponding 3′(Z),6′(Z)-pentadienes 1a-5a (20). Work-up procedure of the products was performed as described above.…”

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confidence: 99%

Catalytic properties of allene oxide synthase from flaxseed (Linum usitatissimum L.)

Schneider

Schreier

1998

Lipids

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“…oleamide has been shown to induce sleep, probably because it has a ‘horse shoe’ conformation [21]. N ‐linoleoyl amide with two cis double bonds may adopt an even more pronounced ‘horse shoe’ conformation [20], and induce sleep as well. The oxygenated lipoxygenase product N ‐linoleoyl amide does not have the ‘horse shoe’ conformation, due to the presence of the cis – trans ‐conjugated diene, and therefore may not induce sleep.…”

Section: Discussionmentioning

confidence: 99%

Dioxygenation of N‐linoleoyl amides by soybean lipoxygenase‐1

Stelt¹,

Nieuwenhuizen²,

Veldink³

et al. 1997

FEBS Letters

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Anandamide, a novel neurotransmitter, has been reported to be dioxygenated by brain lipoxygenase [1, 11]. Anandamides constitute a new class of neuroregulatory fatty acid amides. However, little is known about the enzymatic dioxygenation of these lipids. Therefore, we have tested several members of the neuroactive fatty acid amide class containing a 1Z,4Z‐pentadiene system whether they could be dioxygenated by soybean lipoxygenase‐1, which is a model enzyme for mammalian lipoxygenases. In this study it was found that lipoxygenase‐1 converts N‐linoleoylethanolamide (ODNHEtOH), N‐linoleoylamide (ODNH2), N‐linoleoylmethylamide (ODNHMe) and N,N‐linoleoyldimethylamide (ODN(Me)2 into 13‐(S)‐hydroperoxy‐9Z,11E‐octadeca‐9,11‐dienoyl amides derivatives. The apparent K m values for ODNHEtOH (23.6±3.7 μM), ODNH2 (8.60±0.65 μM) and linoleic acid (OD: 8.85±0.74 μM) are not significantly different. The k cat for ODNH2 (32.4±1.2 s−1) is twice as small as compared to the turnover numbers of the other substrates, viz. ODNHEtOH (61.6±5.0 s−1) and OD (54.4±2.0 s−1). The results suggest that N‐linoleoyl ethanolamide and N‐linoleoyl amide can be readily converted by lipoxygenases in vivo.

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“…34 ( DATCHEVA et al, 1991). This concept has been extensively used by SCHELLER et al (1995) in a systematic investigation of the substrate selectivity of soybean lipoxygenase with respect to the alkyl substituent R of Fig. 34.…”

Section: Lipoxygenasesmentioning

confidence: 99%

Hydroxylation and Dihydroxylation

Holland¹

2001

Biotechnology Set

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Soybean lipoxygenase: Substrate structure and product selectivity

Cited by 16 publications

References 8 publications

Catalytic properties of allene oxide synthase from flaxseed (Linum usitatissimum L.)

Catalytic properties of allene oxide synthase from flaxseed (Linum usitatissimum L.)

Dioxygenation of N‐linoleoyl amides by soybean lipoxygenase‐1

Hydroxylation and Dihydroxylation

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