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| Home > Publications database > Structure‐Based Demystification of Radical Catalysis by a Coenzyme B$_{12}$ Dependent Enzyme—Crystallographic Study of Glutamate Mutase with Cofactor Homologues > print |
| 001 | 491728 | ||
| 005 | 20250724152219.0 | ||
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| 082 | _ | _ | |a 660 |
| 100 | 1 | _ | |a Gruber, Karl |0 P:(DE-H253)PIP1083241 |b 0 |e Corresponding author |
| 245 | _ | _ | |a Structure‐Based Demystification of Radical Catalysis by a Coenzyme B$_{12}$ Dependent Enzyme—Crystallographic Study of Glutamate Mutase with Cofactor Homologues |
| 260 | _ | _ | |a Weinheim |c 2022 |b Wiley-VCH |
| 336 | 7 | _ | |a article |2 DRIVER |
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| 520 | _ | _ | |a Catalysis by radical enzymes dependent on coenzyme B$_{12}$ (AdoCbl) relies on the reactive primary 5′-deoxy-5′adenosyl radical, which originates from reversible Co−C bond homolysis of AdoCbl. This bond homolysis is accelerated roughly 10$^{12}$-fold upon binding the enzyme substrate. The structural basis for this activation is still strikingly enigmatic. As revealed here, a displaced firm adenosine binding cavity in substrate-loaded glutamate mutase (GM) causes a structural misfit for intact AdoCbl that is relieved by the homolytic Co−C bond cleavage. Strategically interacting adjacent adenosine- and substrate-binding protein cavities provide a tight caged radical reaction space, controlling the entire radical path. The GM active site is perfectly structured for promoting radical catalysis, including “negative catalysis”, a paradigm for AdoCbl-dependent mutases. |
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| 700 | 1 | _ | |a Csitkovits, Vanessa |b 1 |
| 700 | 1 | _ | |a Łyskowski, Andrzej |0 0000-0001-8625-4164 |b 2 |
| 700 | 1 | _ | |a Kratky, Christoph |b 3 |
| 700 | 1 | _ | |a Kräutler, Bernhard |0 0000-0002-2222-0587 |b 4 |e Corresponding author |
| 773 | _ | _ | |a 10.1002/ange.202208295 |g Vol. 134, no. 35 |0 PERI:(DE-600)1479266-7 |n 35 |p e202208295 |t Angewandte Chemie |v 134 |y 2022 |x 0932-2132 |
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