Cloning of an isozyme of proline 3-hydroxylase and its purification from recombinant Escherichia coli |
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| Authors: | Takeshi Shibasaki Hideo Mori Akio Ozaki |
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| Affiliation: | (1) Tokyo Research Laboratories, Kyowa Hakko Kogyo Co., Ltd., 3-6-6 Asahimachi, Machida, Tokyo, 194-8533, Japan;(2) Development Department, Bio-chemicals Company, Kyowa Hakko Kogyo Co., Ltd, 6-1, Ohtemachi, 1-Chome, Chiyoda-ku, Tokyo, 100-8185, Japan;(3) Present address: Technical Research Laboratories, Kyowa Hakko Kogyo Co., Ltd., 1-1 Kyowamachi, Hofu, Yamaguchi, 747-8522, Japan |
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| Abstract: | An isozyme gene of proline 3-hydroxylase was cloned from Streptomyces sp. strain TH1 (Mori H, Shibasaki T, Yano K, Ozaki A, J. Bacteriol. 1997, 179: 5677–5683). The isozyme gene (870 bp) encodes a protein of molecular weight of 33,573. Both 3-hydroxylase genes are identical at 76.2% in amino acid sequence. His-motifs conserved in 2-oxoglutarate-dependent dioxygenases are conserved in both genes. Although characteristics of both recombinant 3-hydroxylases are similar, specific activities to l-proline and proline analogs are different. |
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| Keywords: | hydroxyproline 2-oxoglutarate-dependent dioxygenase substrate specificity |
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