Identification of substrate-binding and selectivity-related residues of maltooligosyltrehalose synthase from the thermophilic archaeon Sulfolobus solfataricus ATCC 35092.
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| Title: | Identification of substrate-binding and selectivity-related residues of maltooligosyltrehalose synthase from the thermophilic archaeon Sulfolobus solfataricus ATCC 35092. |
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| Authors: | Tseng, Wen-Chi1 tsengwc@mail.ntust.edu.tw, Lin, Chia-Ray2, Hung, Xing-Guang2, Wei, Tsen-Yun2, Chen, Yu-Chun2, Fang, Tsuei-Yun2 tyfang@mail.ntou.edu.tw |
| Source: | Enzyme & Microbial Technology. Mar2014, Vol. 56, p53-59. 7p. |
| Subjects: | Biochemical substrates, Trehalose, Sulfolobus solfataricus, Thermophilic microorganisms, Simulation methods & models, Mutagenesis |
| Abstract: | Highlights: [•] Simulations and mutagenesis were used to assess the important residues of MTSase. [•] Residues D411, D610 and R614 are substrate-binding residues. [•] Residues P402 and A406 are selectivity-related residues. [ABSTRACT FROM AUTHOR] |
| Copyright of Enzyme & Microbial Technology is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.) | |
| Database: | Engineering Source |
| FullText | Text: Availability: 0 |
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| Header | DbId: egs DbLabel: Engineering Source An: 94695383 AccessLevel: 6 PubType: Academic Journal PubTypeId: academicJournal PreciseRelevancyScore: 0 |
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| Items | – Name: Title Label: Title Group: Ti Data: Identification of substrate-binding and selectivity-related residues of maltooligosyltrehalose synthase from the thermophilic archaeon Sulfolobus solfataricus ATCC 35092. – Name: Author Label: Authors Group: Au Data: <searchLink fieldCode="AR" term="%22Tseng%2C+Wen-Chi%22">Tseng, Wen-Chi</searchLink><relatesTo>1</relatesTo><i> tsengwc@mail.ntust.edu.tw</i><br /><searchLink fieldCode="AR" term="%22Lin%2C+Chia-Ray%22">Lin, Chia-Ray</searchLink><relatesTo>2</relatesTo><br /><searchLink fieldCode="AR" term="%22Hung%2C+Xing-Guang%22">Hung, Xing-Guang</searchLink><relatesTo>2</relatesTo><br /><searchLink fieldCode="AR" term="%22Wei%2C+Tsen-Yun%22">Wei, Tsen-Yun</searchLink><relatesTo>2</relatesTo><br /><searchLink fieldCode="AR" term="%22Chen%2C+Yu-Chun%22">Chen, Yu-Chun</searchLink><relatesTo>2</relatesTo><br /><searchLink fieldCode="AR" term="%22Fang%2C+Tsuei-Yun%22">Fang, Tsuei-Yun</searchLink><relatesTo>2</relatesTo><i> tyfang@mail.ntou.edu.tw</i> – Name: TitleSource Label: Source Group: Src Data: <searchLink fieldCode="JN" term="%22Enzyme+%26+Microbial+Technology%22">Enzyme & Microbial Technology</searchLink>. Mar2014, Vol. 56, p53-59. 7p. – Name: Subject Label: Subjects Group: Su Data: <searchLink fieldCode="DE" term="%22Biochemical+substrates%22">Biochemical substrates</searchLink><br /><searchLink fieldCode="DE" term="%22Trehalose%22">Trehalose</searchLink><br /><searchLink fieldCode="DE" term="%22Sulfolobus+solfataricus%22">Sulfolobus solfataricus</searchLink><br /><searchLink fieldCode="DE" term="%22Thermophilic+microorganisms%22">Thermophilic microorganisms</searchLink><br /><searchLink fieldCode="DE" term="%22Simulation+methods+%26+models%22">Simulation methods & models</searchLink><br /><searchLink fieldCode="DE" term="%22Mutagenesis%22">Mutagenesis</searchLink> – Name: Abstract Label: Abstract Group: Ab Data: Highlights: [•] Simulations and mutagenesis were used to assess the important residues of MTSase. [•] Residues D411, D610 and R614 are substrate-binding residues. [•] Residues P402 and A406 are selectivity-related residues. [ABSTRACT FROM AUTHOR] – Name: AbstractSuppliedCopyright Label: Group: Ab Data: <i>Copyright of Enzyme & Microbial Technology is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.) |
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| RecordInfo | BibRecord: BibEntity: Identifiers: – Type: doi Value: 10.1016/j.enzmictec.2014.01.003 Languages: – Code: eng Text: English PhysicalDescription: Pagination: PageCount: 7 StartPage: 53 Subjects: – SubjectFull: Biochemical substrates Type: general – SubjectFull: Trehalose Type: general – SubjectFull: Sulfolobus solfataricus Type: general – SubjectFull: Thermophilic microorganisms Type: general – SubjectFull: Simulation methods & models Type: general – SubjectFull: Mutagenesis Type: general Titles: – TitleFull: Identification of substrate-binding and selectivity-related residues of maltooligosyltrehalose synthase from the thermophilic archaeon Sulfolobus solfataricus ATCC 35092. Type: main BibRelationships: HasContributorRelationships: – PersonEntity: Name: NameFull: Tseng, Wen-Chi – PersonEntity: Name: NameFull: Lin, Chia-Ray – PersonEntity: Name: NameFull: Hung, Xing-Guang – PersonEntity: Name: NameFull: Wei, Tsen-Yun – PersonEntity: Name: NameFull: Chen, Yu-Chun – PersonEntity: Name: NameFull: Fang, Tsuei-Yun IsPartOfRelationships: – BibEntity: Dates: – D: 05 M: 03 Text: Mar2014 Type: published Y: 2014 Identifiers: – Type: issn-print Value: 01410229 Numbering: – Type: volume Value: 56 Titles: – TitleFull: Enzyme & Microbial Technology Type: main |
| ResultId | 1 |
