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Characterization of tetrathionate hydrolase from the marine acidophilic sulfur-oxidizing bacterium, Acidithiobacillus thiooxidans strain SH.
- Source :
- Bioscience, Biotechnology & Biochemistry; Jan2018, Vol. 82 Issue 1, p152-160, 9p
- Publication Year :
- 2018
-
Abstract
- Tetrathionate hydrolase (4THase), a key enzyme of the S4-intermediate (S4I) pathway, was partially purified from marine acidophilic bacterium,Acidithiobacillus thiooxidansstrain SH, and the gene encoding this enzyme (SH-tth) was identified. SH-Tth is a homodimer with a molecular mass of 97 ± 3 kDa, and contains a subunit 52 kDa in size. Enzyme activity was stimulated in the presence of 1 M NaCl, and showed the maximum at pH 3.0. Although 4THases fromA. thiooxidansand the closely relatedAcidithiobacillus caldusstrain have been reported to be periplasmic enzymes, SH-Tth seems to be localized on the outer membrane of the cell, and acts as a peripheral protein. Furthermore, both 4THase activity and SH-Tth proteins were detected in sulfur-grown cells of strain SH. These results suggested that SH-Tth is involved in elemental sulfur-oxidation, which is distinct from sulfur-oxidation in other sulfur-oxidizing strains such asA. thiooxidansandA. caldus. SH-Tth from the marine bacterium exhibited halophilic features distinct from those of the limneticAf-Tth. [ABSTRACT FROM PUBLISHER]
- Subjects :
- BACTERIAL enzymes
ACIDITHIOBACILLUS caldus
HYDROLASES
Subjects
Details
- Language :
- English
- ISSN :
- 09168451
- Volume :
- 82
- Issue :
- 1
- Database :
- Supplemental Index
- Journal :
- Bioscience, Biotechnology & Biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 127589174
- Full Text :
- https://doi.org/10.1080/09168451.2017.1415128