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000618915 1001_ $$aGawel, Magdalena$$b0
000618915 245__ $$aA closer look at molecular mechanisms underlying inhibition of S -adenosyl- l -homocysteine hydrolase by transition metal cations
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000618915 520__ $$aWe 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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000618915 7001_ $$aMalecki, Piotr H.$$b1
000618915 7001_ $$aSliwiak, Joanna$$b2
000618915 7001_ $$aStepniewska, Marlena$$b3
000618915 7001_ $$aImiolczyk, Barbara$$b4
000618915 7001_ $$aCzyrko-Horczak, Justyna$$b5
000618915 7001_ $$aJakubczyk, Dorota$$b6
000618915 7001_ $$aMarczak, Łukasz$$b7
000618915 7001_ $$00000-0002-0538-6059$$aPlonska-Brzezinska, Marta Eliza$$b8$$eCorresponding author
000618915 7001_ $$0P:(DE-H253)PIP1090221$$aBrzezinski, Krzysztof$$b9$$eCorresponding author
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000618915 773__ $$0PERI:(DE-600)1472881-3$$a10.1039/D4CC03143A$$gVol. 60, no. 81, p. 11504 - 11507$$n81$$p11504-11507$$tChemical communications$$v60$$x1359-7345$$y2024
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