## Dedicated to Professor Albert Eschenmoser on the occasion of his 75th birthday The enzymes (carotene dioxygenases, CDOs) that cleave b,b-carotene 1 to provide retinal 2 as a precursor for retinol (vitamin A) are of significance to animal and human nutrition. To date two modes of cleavage of 1
The Substrate Specificity of β, β-Carotene 15,15′-Monooxygenase
✍ Scribed by Gabriele M. Wirtz; Claus Bornemann; Alfred Giger; Robert K. Müller; Heinz Schneider; Götz Schlotterbeck; Gerhard Schiefer; Wolf-Dietrich Woggon
- Publisher
- John Wiley and Sons
- Year
- 2001
- Tongue
- German
- Weight
- 207 KB
- Volume
- 84
- Category
- Article
- ISSN
- 0018-019X
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
## Abstract Of all presently available Baeyer–Villiger monooxygenases, phenylacetone monooxygenase (PAMO) is the only representative for which a structure has been determined. While it is an attractive biocatalyst because of its thermostability, it is only active with a limited number of substrates
due credit for contributions, references are designated by first letters of the above-named authors. At risk of appearing to favour ones' own wares, we humbly refer readers to our cited papers for contextual commentaries.
~-2'-Deoxy-[9,Amino-~~N~]Adenosine has been constructed in 4 steps from commercially available 5-amino-4,6-dichloropyrirnidine and 15NH3. The reactions have been scaled to provide significant quantities of labeled nucleoside.