Difference between revisions of "Part:BBa K3416005"
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| + | =Introduction= | ||
| + | ==Biology== | ||
| + | ===Description of the Pfs=== | ||
| + | 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase (EC 3.2.2.9) (MTAN) catalyzes the irreversible cleavage of the glycosidic bond in 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH) and plays a key role in four metabolic processes: biological methylation, polyamine biosynthesis, methionine recycling and bacterial quorum sensing. | ||
| + | |||
| + | H<sub>2</sub>O + S-adenosyl-L-homocysteine → adenine + S-(5-deoxy-D-ribose-5-yl)-L-homocysteine | ||
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| + | 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase (EC 3.2.2.9) cleaves the glycosidic bond of 5’-methylthioadenosine (MTA) and S-adenosylhomocysteine (AdoHcy) to adenine and its corresponding thiol ribose. This hydrolysis reaction is irreversible, with Km=0.43μM and 4.3μM for MTA and AdoHcy, respectively<sup>2</sup>. MTA and AdoHcy are catabolized differently in mammals and microbes<sup>1</sup>. | ||
| + | |||
| + | The MTA/AdoHcy nucleosidase active has three separate regions, the purine, ribose, and 5'-alkylthio binding subsites. The three region active site was determined by the presence of adenine and the inhibitors: 5'-methylthio tubercidin (MTT), formycin A (FMA), 5'-methylthio-immucillin A (MT-ImmA), and 5'-methylthio-4'- deoxy-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin A (MTDADMe-ImmA). The structure of MTA/AdoHcy nucleosidase suggests that enzyme is functional as a dimer, with each monomer consisting of a nine-stranded mixed β sheet flanked by six α helices and a small 310 helix. The nucleosidase has no similarity to any known protein<sup>2</sup>. | ||
Revision as of 12:13, 11 October 2020
Introduction
Biology
Description of the Pfs
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase (EC 3.2.2.9) (MTAN) catalyzes the irreversible cleavage of the glycosidic bond in 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH) and plays a key role in four metabolic processes: biological methylation, polyamine biosynthesis, methionine recycling and bacterial quorum sensing.
H2O + S-adenosyl-L-homocysteine → adenine + S-(5-deoxy-D-ribose-5-yl)-L-homocysteine
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase (EC 3.2.2.9) cleaves the glycosidic bond of 5’-methylthioadenosine (MTA) and S-adenosylhomocysteine (AdoHcy) to adenine and its corresponding thiol ribose. This hydrolysis reaction is irreversible, with Km=0.43μM and 4.3μM for MTA and AdoHcy, respectively2. MTA and AdoHcy are catabolized differently in mammals and microbes1.
The MTA/AdoHcy nucleosidase active has three separate regions, the purine, ribose, and 5'-alkylthio binding subsites. The three region active site was determined by the presence of adenine and the inhibitors: 5'-methylthio tubercidin (MTT), formycin A (FMA), 5'-methylthio-immucillin A (MT-ImmA), and 5'-methylthio-4'- deoxy-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin A (MTDADMe-ImmA). The structure of MTA/AdoHcy nucleosidase suggests that enzyme is functional as a dimer, with each monomer consisting of a nine-stranded mixed β sheet flanked by six α helices and a small 310 helix. The nucleosidase has no similarity to any known protein2.