Stereochemistry of phytoene

Khatoon, Naeema; Loeber, D. E.; Toube, T. P.; Weedon, B. C. L.

doi:10.1039/c39720000996

Cited by 13 publications

(2 citation statements)

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“…From the reaction between cysteine and a,b-unsaturated aldehydes, however, the formation of complex mixtures consisting of mono-and bis-adducts and thiazolidines has been reported [24]. Therefore, the cysteine conjugate 11 of the most abundant sulfanylalkanol 6 was synthesized from 3-methylhex-2-enal (13) [25] via 1,4-addition of (S)-N-Boc-cysteine, followed by in situ reduction with NaBH 4 and subsequent acid hydrolysis according to Daniels and Richert [26] (Scheme 2). The cysteine conjugate 12 already mentioned in [24] was prepared from 8 as described for 11, and fully characterized for the first time.…”

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Identification of Odoriferous Sulfanylalkanols in Human Axilla Secretions and Their Formation through Cleavage of Cysteine Precursors by a CS Lyase Isolated from Axilla bacteria

Natsch

Schmid²,

Flachsmann³

2004

Chemistry & Biodiversity

107

127

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Human axillary odor is known to be formed upon the action of Corynebacteria sp. on per se odorless axilla secretions. Besides the known odoriferous acids, we report the occurrence in human axilla secretions of four odoriferous sulfanylalkanols, namely 3-sulfanylhexan-1-ol (3), 2-methyl-3-sulfanylbutan-1-ol (4), 3-sulfanylpentan-1-ol (5), and 3-methyl-3-sulfanylhexan-1-ol (6). These compounds have a pungent sweat/kitchen odor, also reminiscent of onions with some fruity connotations, and perception thresholds in the pg/l range. It was postulated that the odorless precursors for these compounds are cysteine conjugates. Bacterial isolates obtained from the human axilla and belonging to the Corynebacteria were, indeed, found to have the enzymatic capacity to release various thiols from cysteine conjugates. The metC gene, which is known to code for a cystathione-beta-lyase, was cloned from the axilla isolate Corynebacterium striatum Ax20 and heterologously expressed in E. coli. The pure recombinant enzyme cleaves various cysteine conjugates and has a similar substrate specificity as the cell homogenates of the wild-type. The recombinant enzyme was finally incubated with odorless axilla secretions and shown to release odoriferous thiols.

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