Journal
JOURNAL OF BIOTECHNOLOGY
Volume 172, Issue -, Pages 55-58Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.jbiotec.2013.12.003
Keywords
Hydroxypipecolinic acid; Hydroxyproline; Dioxygenase; Hydroxylase; Hydroxylation
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Funding
- Adaptable and Seamless Technology Transfer Program through target-driven RD, JST [A5231157E]
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Microbial hydroxylases were screened for the capacity to effect direct hydroxylation of proline and pipecolinic acid, based on genomic information. Of the eight candidates screened, 2-oxoglutaratedependent hydroxylase from Streptosporangium roseum NBRC 3776T and aspartyl/asparaginyl p-hydroxylase from Catenulispora acidiphila NBRC 102108T showed both proline and pipecolinic acid hydroxylation activities. In the case of L-proline hydroxylation, both enzymes catalyzed the simultaneous formation of cis-3-hydroxy-L-proline and cis-4-hydroxy-L-proline, and cis-4-hydroxy-L-proline was preferentially produced. In the case of L-pipecolinic acid hydroxylation, both enzymes catalyzed the simultaneous formation of cis-3-hydroxy-L-pipecolinic acid and cis-5-hydroxy-L-pipecolinic acid. While the former enzyme preferentially produced cis-3-hydroxy-L-pipecolinic acid, the latter enzyme preferentially produced cis-5-hydroxy-L-pipecolinic acid. (C) 2013 Elsevier B.V. All rights reserved.
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