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A model for the solution structure of human Fe(II)-bound acireductone dioxygenase and interactions with the regulatory domain of matrix metalloproteinase I (MMP-1)
The metalloenzyme acireductone dioxygenase (ARD) shows metal-dependent physical and enzymatic activities depending upon the metal bound in the active site. The Fe(II)-bound enzyme catalyzes the penultimate step of the methionine salvage pathway (MSP), converting 1,2-dihydroxy-5-(methylthio)pent-1-en...
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| Vydáno v: | Biochemistry |
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| Hlavní autoři: | , , , , , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
2020
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC7768908/ https://ncbi.nlm.nih.gov/pubmed/33135413 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/acs.biochem.0c00724 |
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