Cited 32 time in
Multifunctional enzymes in archaea: promiscuity and moonlight
| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Jia, Baolei | - |
| dc.contributor.author | Cheong, Gang-Won | - |
| dc.contributor.author | Zhang, Shihong | - |
| dc.date.accessioned | 2022-12-27T00:36:37Z | - |
| dc.date.available | 2022-12-27T00:36:37Z | - |
| dc.date.issued | 2013-03 | - |
| dc.identifier.issn | 1431-0651 | - |
| dc.identifier.issn | 1433-4909 | - |
| dc.identifier.uri | https://scholarworks.gnu.ac.kr/handle/sw.gnu/20788 | - |
| dc.description.abstract | Enzymes from many archaea colonizing extreme environments are of great interest because of their potential for various biotechnological processes and scientific value of evolution. Many enzymes from archaea have been reported to catalyze promiscuous reactions or moonlight in different functions. Here, we summarize known archaeal enzymes of both groups that include different kinds of proteins. Knowledge of their biochemical properties and three-dimensional structures has proved invaluable in understanding mechanism, application, and evolutionary implications of this manifestation. In addition, the review also summarizes the methods to unravel the extra function which almost was discovered serendipitously. The study of these amazing enzymes will provide clues to optimize protein engineering applications and how enzymes might have evolved on Earth. | - |
| dc.format.extent | 11 | - |
| dc.language | 영어 | - |
| dc.language.iso | ENG | - |
| dc.publisher | SPRINGER JAPAN KK | - |
| dc.title | Multifunctional enzymes in archaea: promiscuity and moonlight | - |
| dc.type | Article | - |
| dc.publisher.location | 일본 | - |
| dc.identifier.doi | 10.1007/s00792-012-0509-1 | - |
| dc.identifier.scopusid | 2-s2.0-84874560411 | - |
| dc.identifier.wosid | 000315574600001 | - |
| dc.identifier.bibliographicCitation | EXTREMOPHILES, v.17, no.2, pp 193 - 203 | - |
| dc.citation.title | EXTREMOPHILES | - |
| dc.citation.volume | 17 | - |
| dc.citation.number | 2 | - |
| dc.citation.startPage | 193 | - |
| dc.citation.endPage | 203 | - |
| dc.type.docType | Review | - |
| dc.description.isOpenAccess | N | - |
| dc.description.journalRegisteredClass | sci | - |
| dc.description.journalRegisteredClass | scie | - |
| dc.description.journalRegisteredClass | scopus | - |
| dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
| dc.relation.journalResearchArea | Microbiology | - |
| dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
| dc.relation.journalWebOfScienceCategory | Microbiology | - |
| dc.subject.keywordPlus | ENTNER-DOUDOROFF PATHWAY | - |
| dc.subject.keywordPlus | INTRINSICALLY UNSTRUCTURED PROTEINS | - |
| dc.subject.keywordPlus | AUTOCRINE MOTILITY FACTOR | - |
| dc.subject.keywordPlus | APOPTOSIS-INDUCING FACTOR | - |
| dc.subject.keywordPlus | SULFOLOBUS-SOLFATARICUS | - |
| dc.subject.keywordPlus | PHOSPHOGLUCOSE ISOMERASE | - |
| dc.subject.keywordPlus | CRYSTAL-STRUCTURE | - |
| dc.subject.keywordPlus | PYROCOCCUS-FURIOSUS | - |
| dc.subject.keywordPlus | NADH OXIDASE | - |
| dc.subject.keywordPlus | FRUCTOSE-1,6-BISPHOSPHATE ALDOLASE/PHOSPHATASE | - |
| dc.subject.keywordAuthor | Archaea | - |
| dc.subject.keywordAuthor | Promiscuity | - |
| dc.subject.keywordAuthor | Moonlight | - |
| dc.subject.keywordAuthor | Application | - |
| dc.subject.keywordAuthor | Evolution | - |
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