Crystal structures of the elusive Rhizobium etli l-asparaginase reveal a peculiar active site
L-asparaginases catalyse the hydrolysis of L-asparagine to L-aspartic acid and ammonia. Here, the authors present high resolution crystal structures of Rhizobium etli L-asparaginase that contains a Zn2+ binding site without a catalytic role and discuss the catalytic mechanism of the enzyme.
| Main Authors: | , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2021-11-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-021-27105-x |
| _version_ | 1818824849614700544 |
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| author | Joanna I. Loch Barbara Imiolczyk Joanna Sliwiak Anna Wantuch Magdalena Bejger Miroslaw Gilski Mariusz Jaskolski |
| author_facet | Joanna I. Loch Barbara Imiolczyk Joanna Sliwiak Anna Wantuch Magdalena Bejger Miroslaw Gilski Mariusz Jaskolski |
| author_sort | Joanna I. Loch |
| collection | DOAJ |
| description | L-asparaginases catalyse the hydrolysis of L-asparagine to L-aspartic acid and ammonia. Here, the authors present high resolution crystal structures of Rhizobium etli L-asparaginase that contains a Zn2+ binding site without a catalytic role and discuss the catalytic mechanism of the enzyme. |
| first_indexed | 2024-12-19T00:02:25Z |
| format | Article |
| id | doaj.art-c9f06facb4a14c2fae5b9053da75c6f1 |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-12-19T00:02:25Z |
| publishDate | 2021-11-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-c9f06facb4a14c2fae5b9053da75c6f12022-12-21T20:46:24ZengNature PortfolioNature Communications2041-17232021-11-0112111110.1038/s41467-021-27105-xCrystal structures of the elusive Rhizobium etli l-asparaginase reveal a peculiar active siteJoanna I. Loch0Barbara Imiolczyk1Joanna Sliwiak2Anna Wantuch3Magdalena Bejger4Miroslaw Gilski5Mariusz Jaskolski6Department of Crystal Chemistry and Crystal Physics, Faculty of Chemistry, Jagiellonian UniversityInstitute of Bioorganic Chemistry, Polish Academy of SciencesInstitute of Bioorganic Chemistry, Polish Academy of SciencesDepartment of Crystal Chemistry and Crystal Physics, Faculty of Chemistry, Jagiellonian UniversityInstitute of Bioorganic Chemistry, Polish Academy of SciencesInstitute of Bioorganic Chemistry, Polish Academy of SciencesInstitute of Bioorganic Chemistry, Polish Academy of SciencesL-asparaginases catalyse the hydrolysis of L-asparagine to L-aspartic acid and ammonia. Here, the authors present high resolution crystal structures of Rhizobium etli L-asparaginase that contains a Zn2+ binding site without a catalytic role and discuss the catalytic mechanism of the enzyme.https://doi.org/10.1038/s41467-021-27105-x |
| spellingShingle | Joanna I. Loch Barbara Imiolczyk Joanna Sliwiak Anna Wantuch Magdalena Bejger Miroslaw Gilski Mariusz Jaskolski Crystal structures of the elusive Rhizobium etli l-asparaginase reveal a peculiar active site Nature Communications |
| title | Crystal structures of the elusive Rhizobium etli l-asparaginase reveal a peculiar active site |
| title_full | Crystal structures of the elusive Rhizobium etli l-asparaginase reveal a peculiar active site |
| title_fullStr | Crystal structures of the elusive Rhizobium etli l-asparaginase reveal a peculiar active site |
| title_full_unstemmed | Crystal structures of the elusive Rhizobium etli l-asparaginase reveal a peculiar active site |
| title_short | Crystal structures of the elusive Rhizobium etli l-asparaginase reveal a peculiar active site |
| title_sort | crystal structures of the elusive rhizobium etli l asparaginase reveal a peculiar active site |
| url | https://doi.org/10.1038/s41467-021-27105-x |
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