Article Abstract:
Whole cells of Streptomyces sp. strain TH1 and Bacillus sp. strains TH2 and TH3 from soils exhibit proline 3-hydroxylase activities that hydroxylate L-proline to cis-3-hydroxy-L-proline. S. canus ATCC 12647, producing the 3-hydroxyproline-containing peptide antibiotic telomycin, also shows proline 3-hydroxylase activity. The hydroxylation of proline is regio- and stereospecific at position 3 of L-proline as no other hydroxylation product is formed. The 3-hydroxylases probably belong to dioxygenases related to 2-oxoglutarate, as hydroxylation requires glutarate and ferrous ion.
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Article Abstract:
Research was conducted to examine the high-level formation of lipase from Pseudomonas cepacia ATCC 21088 in Escherichia coli with pCYTEXP1 under the control of the strong promoter, lambda-P(sub RL). No overexpression of the modified lipase chaperone was observed in E. coli. Truncation of the gene resulted to overexpression of the chaperone in E. coli. Results indicate that a simple rapid refolding procedure could yield a highly active Pseudomonas lipase expressed in E. coli.
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Article Abstract:
A study was conducted to analyze strains of Streptomyces for their ability to regio- and stereoselectively hydroxylate beta and/or alpha-ionone to 3-hydroxy derivatives. Results indicated that the strains supported little conversion to 4-hydroxy and no conversion to 3-hydroxy products. Findings also showed that the enzymatic hydroxylation of alpha-ionone by the strains of Streptomyces supported high regio- and stereoselectivity.
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