7zd4
From Proteopedia
(Difference between revisions)
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== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/SAHH_PSEAE SAHH_PSEAE] May play a key role in the regulation of the intracellular concentration of adenosylhomocysteine. | [https://www.uniprot.org/uniprot/SAHH_PSEAE SAHH_PSEAE] May play a key role in the regulation of the intracellular concentration of adenosylhomocysteine. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | We report biochemical and structural studies on inhibiting bacterial S-adenosyl-L-homocysteine hydrolase by transition metal cations. Our results revealed diverse molecular mechanisms of enzyme inactivation. Depending on the cation, the mechanism is based on arresting the enzyme in its closed, inactive conformation, disulfide bond formation within the active site or oxidation of the intermediate form of a cofactor. | ||
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| + | A closer look at molecular mechanisms underlying inhibition of S-adenosyl-L-homocysteine hydrolase by transition metal cations.,Gawel M, Malecki PH, Sliwiak J, Stepniewska M, Imiolczyk B, Czyrko-Horczak J, Jakubczyk D, Marczak L, Plonska-Brzezinska ME, Brzezinski K Chem Commun (Camb). 2024 Oct 8;60(81):11504-11507. doi: 10.1039/d4cc03143a. PMID:39230573<ref>PMID:39230573</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7zd4" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Crystal structure of Pseudomonas aeruginosa S-adenosyl-L-homocysteine hydrolase soaked with Cu+ ions
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