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Titolo:
Development of the regio- and stereospecific proline hydroxylases and their application
Autore:
Shibasaki, T; Mori, H; Ozaki, A;
Indirizzi:
Kyowa Hakko Kogyo Co Ltd, Tokyo Res Labs, Tokyo 1948533, Japan Kyowa HakkoKogyo Co Ltd Tokyo Japan 1948533 Labs, Tokyo 1948533, Japan
Titolo Testata:
JOURNAL OF SYNTHETIC ORGANIC CHEMISTRY JAPAN
fascicolo: 6, volume: 57, anno: 1999,
pagine: 523 - 531
SICI:
0037-9980(199906)57:6<523:DOTRAS>2.0.ZU;2-C
Fonte:
ISI
Lingua:
JPN
Soggetto:
PERFORMANCE LIQUID-CHROMATOGRAPHY; AMINO-ACIDS; HYDROXYPROLINE; STREPTOMYCES; 4-HYDROXYLASE; 3-HYDROXYLASE; PURIFICATION; ETAMYCIN; ENZYME;
Keywords:
proline 4-hydroxylase; proline 3-hydroxylase; 2-oxoglutarate-dependent dioxygenases; trans-4-hydroxy-L-proline; cis-3-hydroxy-L-proline; biotransformation; enzymatic synthesis; regio- and stereospecific hydroxylation;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Physical, Chemical & Earth Sciences
Citazioni:
26
Recensione:
Indirizzi per estratti:
Indirizzo: Shibasaki, T Kyowa Hakko Kogyo Co Ltd, Tokyo Res Labs, 3-6-6 Asahimachi, Tokyo 1948533,Japan Kyowa Hakko Kogyo Co Ltd 3-6-6 Asahimachi Tokyo Japan 1948533
Citazione:
T. Shibasaki et al., "Development of the regio- and stereospecific proline hydroxylases and their application", J SYN ORG J, 57(6), 1999, pp. 523-531

Abstract

This article describes microbial proline hydroxylases which carry out regio- and stereospecific hydroxylation of free L-proline and their applicationto the enzymatic synthesis of hydroxyprolines and related compounds. Proline 4-hydroxylase activities were detected in 8 actinomycetes strains, and proline 3-hydroxylase activities were detected in 3 actinomycetes and 2 Bacillus strains. Both enzymes were purified and characterized. The enzymes required 2-oxoglutarate and Fe2+ for the reaction. Proline 4-hydroxylase hydroxylated L-proline in a regio- and stereospecific manner at C-4 to form trans -4-hydroxy-L-proline, while 3-hydroxylase hydroxylated C-3 of L-proline to form cis-3-hydroxy-L-proline. Efficient biotransformation systems of L-proline to trans-4-hydroxy-L-proline or cis-3-hydroxy-L-proline were established using recombinant DNA technology. Both of the enzymes hydroxylated L-2-azetidine carboxylate, 3, 4-dehydro-L-proline and L-pipecolate in a regio- and stereospecific manner, however, D-proline, N-substituted L-proline, L-proline eater and peptidyl L-proline do not react as substrates for either 4- or 3-hydroxylases.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 31/03/20 alle ore 19:23:17