/ . Biochem., 81, 1911-1916 (1977)
Enzymatic Oxidation of Isethionate to Sulfoacetaldehyde in Bacterial Extract1 Hiroyuki KONDO, Hisashi NIKI,1 Setsuro TAKAHASHI,1 and Makoto ISHIMOTO Department of Chemical Microbiology, Faculty of Pharmaceutical Sciences, Hokkaido University, Kita-ku, Sapporo, Hokkaido 060 Received for publication, October 29, 1976
Isethionate degradation in a bacterial extract was shown by the isolation of enzymes and by identification of an intermediate to take place in two steps; dehydrogenation to sulfoacetaldehyde and desulfonation leading to the formation of sulfite and acetate. The enzyme responsible for isethionate oxidation in the presence of FAD was particulate in nature and a solubilized preparation obtained by extraction with buffer of low ionic strength had oxidizing activities against only isethionate and n-butanol among compounds tested. The enzyme was inhibited by thiol and carbonyl reagents.
Isethionate, 2-hydroxyethane sulfonate HOCH,CH,SOj", is a normal component of animal tissues. It was found to be formed from taurine in rat brain homogenate (/), dog tissue slices (2, 3), and culture of Aspergillus niger (4), but the enzymatic mechanism of its formation has not been -O3SCH,CH,NH3+ -O.SCHjCHO+H.O
O, —--> -OjSCH.CHO+NH/ ---• CH S COO-+SO, 2 -+2H +
As this bacterium grows on isethionate as well as on taurine, breakdown of isethionate was studied in a cell-free extract of the bacterium. Intermediary formation of sulfoacetaldehyde was in1 This study was supported in part by a Scientific Research Grant from the Ministry of Education, Science and Culture of Japan. 1 Present address: Iwanai Health Center, Iwanai-cho, Iwanai-gun, Hokkaido 045. 1 Present address: Tsukui Senior High School, Tsukuicho, Tsukui-gun, Kanagawa 220-02. Abbreviation: PMS, phenazine methosulfate.
Vol. 81, No. 6, 1977
elucidated. Its catabolic pathway is not yet known. Taurine was shown to be degraded in a bacterium via sulfoacetaldehyde (5) by taurine dehydrogenase (6~), and sulfoacetaldehyde sulfo-lyase (7-9) successively, as follows, (1) (2)
dicated. Dehydrogenation of isethionate was performed by the particulate fraction. Several enzymatic properties were investigated, and the results are presented in the present communication. EXPERIMENTAL PROCEDURES Materials—Sulfoacetaldhyde was synthesized as reported previously (
Enzymatic Oxidation of Isethionate to Sulfoacetaldehyde in Bacterial Extract1 Hiroyuki KONDO, Hisashi NIKI,1 Setsuro TAKAHASHI,1 and Makoto ISHIMOTO Department of Chemical Microbiology, Faculty of Pharmaceutical Sciences, Hokkaido University, Kita-ku, Sapporo, Hokkaido 060 Received for publication, October 29, 1976
Isethionate degradation in a bacterial extract was shown by the isolation of enzymes and by identification of an intermediate to take place in two steps; dehydrogenation to sulfoacetaldehyde and desulfonation leading to the formation of sulfite and acetate. The enzyme responsible for isethionate oxidation in the presence of FAD was particulate in nature and a solubilized preparation obtained by extraction with buffer of low ionic strength had oxidizing activities against only isethionate and n-butanol among compounds tested. The enzyme was inhibited by thiol and carbonyl reagents.
Isethionate, 2-hydroxyethane sulfonate HOCH,CH,SOj", is a normal component of animal tissues. It was found to be formed from taurine in rat brain homogenate (/), dog tissue slices (2, 3), and culture of Aspergillus niger (4), but the enzymatic mechanism of its formation has not been -O3SCH,CH,NH3+ -O.SCHjCHO+H.O
O, —--> -OjSCH.CHO+NH/ ---• CH S COO-+SO, 2 -+2H +
As this bacterium grows on isethionate as well as on taurine, breakdown of isethionate was studied in a cell-free extract of the bacterium. Intermediary formation of sulfoacetaldehyde was in1 This study was supported in part by a Scientific Research Grant from the Ministry of Education, Science and Culture of Japan. 1 Present address: Iwanai Health Center, Iwanai-cho, Iwanai-gun, Hokkaido 045. 1 Present address: Tsukui Senior High School, Tsukuicho, Tsukui-gun, Kanagawa 220-02. Abbreviation: PMS, phenazine methosulfate.
Vol. 81, No. 6, 1977
elucidated. Its catabolic pathway is not yet known. Taurine was shown to be degraded in a bacterium via sulfoacetaldehyde (5) by taurine dehydrogenase (6~), and sulfoacetaldehyde sulfo-lyase (7-9) successively, as follows, (1) (2)
dicated. Dehydrogenation of isethionate was performed by the particulate fraction. Several enzymatic properties were investigated, and the results are presented in the present communication. EXPERIMENTAL PROCEDURES Materials—Sulfoacetaldhyde was synthesized as reported previously (
