Metal-cation regulation of enzyme dynamics is a key factor influencing the activity of S-adenosyl-l-homocysteine hydrolase from Pseudomonas aeruginosa

Author:

Czyrko Justyna,Sliwiak Joanna,Imiolczyk Barbara,Gdaniec Zofia,Jaskolski Mariusz,Brzezinski KrzysztofORCID

Funder

Narodowe Centrum Nauki (National Science Centre)

Publisher

Springer Science and Business Media LLC

Subject

Multidisciplinary

Reference76 articles.

1. Richards, H. H., Chiang, P. K. & Cantoni, G. L. Adenosylhomocysteine hydrolase. Crystallization of the purified enzyme and its properties. J Biol Chem 253, 4476–4480 (1978).

2. Poulton, J. E. & Butt, V. S. Purification and properties of S-adenosyl-l-methionine: caffeic acid O-methyltransferase from leaves of spinach beet (Beta vulgaris L.). Biochim Biophys Acta 403, 301–314 (1975).

3. Chiang, P. K. & Cantoni, G. L. Perturbation of biochemical transmethylations by 3-deazaadenosine in vivo. Biochem Pharmacol 28, 1897–1902 (1979).

4. Chiang, P. K. Biological effects of inhibitors of S-Adenosylhomocysteine hydrolase. Pharmacol Ther 77, 115–134 (1998).

5. Hershfield, M. S. Apparent suicide inactivation of human lymphoblast S-adenosylhomocysteine hydrolase by 2′-deoxyadenosine and adenine arabinoside. A basis for direct toxic effects of analogs of adenosine. J Biol Chem 254, 22–25 (1979).

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