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Titolo:
The substrate specificity of beta,beta-carotene 15,15 '-monooxygenase
Autore:
Wirtz, GM; Bornemann, C; Giger, A; Muller, RK; Schneider, H; Schlotterbeck, G; Schiefer, G; Woggon, WD;
Indirizzi:
Univ Basel, Inst Organ Chem, CH-4056 Basel, Switzerland Univ Basel BaselSwitzerland CH-4056 an Chem, CH-4056 Basel, Switzerland F Hoffmann La Roche & Co Ltd, Vitamins & Fine Chem Div, CH-4070 Basel, Switzerland F Hoffmann La Roche & Co Ltd Basel Switzerland CH-4070 asel, Switzerland F Hoffmann La Roche & Co Ltd, Div Pharmaceut, CH-4070 Basel, Switzerland FHoffmann La Roche & Co Ltd Basel Switzerland CH-4070 asel, Switzerland
Titolo Testata:
HELVETICA CHIMICA ACTA
fascicolo: 8, volume: 84, anno: 2001,
pagine: 2301 - 2315
SICI:
0018-019X(2001)84:8<2301:TSSOB1>2.0.ZU;2-N
Fonte:
ISI
Lingua:
ENG
Soggetto:
BETA-CAROTENE; VITAMIN-A; CONVERSION; RETINOIDS; CLEAVAGE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Physical, Chemical & Earth Sciences
Citazioni:
30
Recensione:
Indirizzi per estratti:
Indirizzo: Woggon, WD Univ Basel, Inst Organ Chem, St Johanns Ring 19, CH-4056 Basel,Switzerland Univ Basel St Johanns Ring 19 Basel Switzerland CH-4056 erland
Citazione:
G.M. Wirtz et al., "The substrate specificity of beta,beta-carotene 15,15 '-monooxygenase", HELV CHIM A, 84(8), 2001, pp. 2301-2315

Abstract

The synthesis of several substrate analogues of the enzyme beta,beta -carotene 15,15'-monooxygenase is reported. The substrate specificity of enriched enzyme fractions isolated from chicken intestinal mucosa was investigated. Regarding substrate binding/cleavage, these experiments demonstrate that i) any deviation from the 'rod-like' beta,beta -carotene structure is not tolerated, ii) one 'natural', unsubstituted beta -ionone ring is required, iii) the position and presence of the Me groups attached to the polyene chain is significant. These results suggest a hydrophobic barrel-like substratebinding site in which the protein's amino acid residues through interaction with the Me groups, direct the central C=C bond in binding distance to the active site's metal-oxo center, supporting the unique regiospecificity ofcleavage to retinal (provitamin A).

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/04/20 alle ore 20:52:42