Cupriavidus necator was engineered aiming to synthesize poly[(R)-3-hydroxybutyrate-co-3-hydroxypropionate] copolyester, P(3HB-co-3HP), from structurally unrelated carbon sources without addition of any precursor compounds. We modified a metabolic pathway in C. necator for generation of 3-hydroxypropionyl-CoA (3HP-CoA) by introducing malonyl-CoA reductase and the 3HP-CoA synthetase domain of trifunctional propionyl-CoA synthase; both members of the 3-hydroxypropionate cycle, a novel CO(2)-fixation pathway in the green nonsulfur bacterium Chloroflexus aurantiacus .
View Article and Find Full Text PDFActa Crystallogr D Biol Crystallogr
November 2004
Chitosanase from Bacillus sp. strain K17 (ChoK) belongs to glycoside hydrolase family 8 and exhibits subclass II specificity. The purified protein is structurally stable over a wide pH range (3-10), but is active in a much narrower pH range (4.
View Article and Find Full Text PDFCrystal structures of chitosanase from Bacillus sp. K17 (ChoK) have been determined at 1.5 A resolution in the active form and at 2.
View Article and Find Full Text PDFNucleic Acids Res Suppl
September 2003
The gene encoding a novel chitosanase from Bacillus sp. strain K17 was cloned and sequenced. The nucleotide sequence of the gene contained an open reading frame corresponded to a protein of 453 amino acids.
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