- 1) Remuzon, P., trans-4-Hydroxy-L-proline, a useful and versatile chiral starting block. Tetrahedron, 52, 13803-13835 (1996).
- 2) Seki, M. and Matsumoto, K., A convenient synthesis of (2S, 4S)-4-hydroxyproline. Biosci. Biotechnol. Biochem., 59, 1161-1162 (1995).
- 3) Baker, G. L., Fritschel, S. J., Stille, J. R., and Stille, J. K., Transition-metal-catalyzed asymmetric organic synthesis via polymer-attached optically active phosphine ligands. 5.1 Preparation of amino acids in high optically yield via catalytic hydrogenation. J. Org. Chem., 46, 2954-2960 (1981).
- 4) Katsumata, R. and Yokoi, H., Japan Kokai Tokkyo Koho, H03-266995 (Nov. 27, 1991).
- 5) Katsumata, R., Hashimoto, S., Ikeda, M., Kawanishi, M., and Sakado, K., Japan Kokai Tokkyo Koho, H06-062880 (Mar. 8, 1994).
- 6) Serizawa, N., Matsuoka, T., Hosoya, T., and Furuya, K., Fermentative production of trans-4-hydroxy-L-proline by Clonostachys cylindrospora. Biosci. Biotechnol. Biochem., 59, 555-557 (1995).
- 7) Matsuoka, T., Serizawa, N., Hosoya, T., and Furuya, K., Japan Kokai Tokkyo Koho, H05-236980 (Sep. 18, 1993).
- 8) Maruhashi, K., Japan Kokai Tokkyo Koho, H09-173093 (Jul. 8, 1997).
- 9) Iizuka, S., Matsuura, Y., Nemoto, A., Ishihara, M., Takase, I., and Miyashiro, S., Japan Kokai Tokkyo Koho, H06-245782 (Sep. 6, 1994).
- 10) Cardinale, G. J. and Udenfriend, S., Prolyl hydroxylase. Adv. Enzymol., 41, 245-300 (1974).
- 11) Katz, E., Kamal, F., and Mason, K., Biosynthesis of trans-4-hydroxy-L-proline by Streptomyces griseoviridus. J. Biol. Chem., 254, 6684-6690 (1979).
- 12) Onishi, M., Okumura, Y., Okamoto, R., and Ishikura, T., Proline hydroxylation by cell free extract of a streptomycete. Biochem. Biophys. Res. Commun., 120, 45-51 (1984).
- 13) Lawrence, C. C., Sobey, W. J., Field, R. A., Baldwin, J. E., and Schofield, C. J., Purification and initial characterization of proline 4-hydroxylase from Streptomyces griseoviridus P8648: a 2-oxoacid, ferrous-dependent dioxygenase involved in etamycin biosynthesis. Biochem. J., 313, 185-191 (1996).
- 14) Shibasaki, T., Mori, H., Chiba S., and Ozaki A., Microbial proline 4-hydroxylase screening and gene cloning. Appl. Environ. Microbiol., 65, 4028-4031 (1999).
- 15) Ozaki, A., Shibasaki, T., and Mori, H., Specific proline and hydroxyproline detection method by post-column derivatization for high-performance liquid chromatography. Biosci. Biotechnol. Biochem., 59, 1764-1765 (1995).
- 16) Nishi, T., Saito, A., Oka, T., Itoh, S., Takaoka, C., and Taniguchi, T., Construction of plasmid expression vectors carrying the Escherichia coli tryptophan promoter. Agric. Biol. Chem., 48, 669-675 (1984).
- 17) Caro, L. and Berg, C. M., P1 transduction. Methods Enzymol., 21, 444-458 (1971).
- 18) Dassa, E. and Boquet, P. L., Identification of the gene appA for the acid phosphatase (pH optimum 2.5) of Escherichia coli. Mol. Gen. Genet., 200, 68-73 (1985).
- 19) Bochner, B. R. and Savageau, M. A., Generalized indicator plate for genetic, metabolic, and taxonomic studies with microorganisms. Applied. Environ. Microbiol., 33, 434-444 (1977).
- 20) de Boer, H. A., Comstock, L. J., and Vasser, M., The tac promoter: A functional hybrid derived from the trp and lac promoters. Proc. Natl. Acad. Sci. USA, 80, 21-25 (1983).
- 21) Andersson, S. G. E. and Kurland, C. G., Codon preferences in free-living microorganisms. Microbiol. Rev., 54, 198-210 (1990).
- 22) Wada, K., Wada, Y., Ishibashi, F., Gojobori, T., and Ikemura, T., Codon usage tabulated from GenBank genetic sequence data. Nucleic Acids Res., 20, 2111-2118 (1992).
- 23) Goldman, E., Rosenburg, A. H., Zubay, G., and Studier, F. W., Consecutive low-usage leucine codons block translation only when near the 5′ end of a message in Escherichia coli. J. Mol. Biol., 245, 467-473 (1995).
- 24) Yokota, A., Shimizu, H., Terasawa, Y., Takaoka, N., and Tomita, F., Pyruvic acid production by a lipoic acid auxotroph of Escherichia coli W1485. Appl. Microbiol. Biotechnol., 41, 638-643 (1994).
- . 1996. p. 358- 379.
- 26) Mori, H., Shibasaki, T., Yano, K., and Ozaki, A., Purification and cloning of a proline 3-hydroxylase, a novel enzyme which hydroxylates free L-proline to cis-3-hydroxy-L-proline. J. Bacteriol., 179, 5677-5683 (1997).
- 27) Shibasaki, T., Sakurai, W., Hasegawa, A., Uosaki, Y., Mori, H., Yoshida, M., and Ozaki, A., Substrate selectivities of proline hydroxylases. Tetrahedron Lett., 40, 5227-5230 (1999).
Full access
Enzymatic Production of trans-4-Hydroxy-L-proline by Regio- and Stereospecific Hydroxylation of L-Proline
Reprints and Corporate Permissions
Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?
To request a reprint or corporate permissions for this article, please click on the relevant link below:
Academic Permissions
Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?
Obtain permissions instantly via Rightslink by clicking on the button below:
If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.
Related research
People also read lists articles that other readers of this article have read.
Recommended articles lists articles that we recommend and is powered by our AI driven recommendation engine.
Cited by lists all citing articles based on Crossref citations.
Articles with the Crossref icon will open in a new tab.