83178-70-5Relevant academic research and scientific papers
Gene cloning and characterization of thiourocanate hydratase from Burkholderia sp. HME13
Hayashi, Motoko,Kashiwagi, Takehiro,Kato, Shin-Ichiro,Kim, Chul-Sa,Kurita, Syuya,Matsuo, Hidenori,Miyaoku, Haruna,Muramatsu, Hisashi,Nagata, Shinji,Yamamoto, Hiroaki
, p. 333 - 341 (2020)
A novel enzyme, thiourocanate hydratase, which catalyses the conversion of thiourocanic acid to 3-(5-oxo-2-thioxoimidazolidin-4-yl) propionic acid, was isolated from the ergothioneine-utilizing strain, Burkholderia sp. HME13. When the HME13 cells were cultured in medium containing ergothioneine as the sole nitrogen source, thiourocanate-metabolizing activity was detected in the crude extract from the cells. However, activity was not detected in the crude extract from HME13 cells that were cultured in Luria-Bertani medium. The gene encoding thiourocanate hydratase was cloned and expressed in Escherichia coli, and the recombinant enzyme was purified to homogeneity. The enzyme showed maximum activity at pH 7.5 and 55°C and was stable between pH 5.0 and 10.5, and at temperatures up to 45°C. The Km and Vmax values of thiourocanate hydratase towards thiourocanic acid were 30 μM and 7.1 μmol/min/mg, respectively. The enzyme was strongly inhibited by CuCl2 and HgCl2. The amino acid sequence of the enzyme showed 46% identity to urocanase from Pseudomonas putida, but thiourocanate hydratase had no urocanase activity.
Studies in thiohydantoin chemistry. II: C-terminal sequencing of peptides
Casagranda, Franca,Duggan, Brendan M.,Kirkpatrick, Alan,Laslett, Robert L.,Wilshire, John F.K.
, p. 551 - 560 (2007/10/03)
An investigation has been carried out into the thiocyanate degradation (AcOH/Ac2O/HSCN) procedure as it relates to the C-terminal sequencing of peptides, particular emphasis being placed on the sequencing of amino acid residues containing sensi
