7zd4
Crystal structure of Pseudomonas aeruginosa S-adenosyl-L-homocysteine hydrolase soaked with Cu+ ionsCrystal structure of Pseudomonas aeruginosa S-adenosyl-L-homocysteine hydrolase soaked with Cu+ ions
Structural highlights
FunctionSAHH_PSEAE May play a key role in the regulation of the intracellular concentration of adenosylhomocysteine. Publication Abstract from PubMedWe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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