Journal Article

PUBDB-2023-00367

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Structure‐Based Demystification of Radical Catalysis by a Coenzyme B$_{12}$ Dependent Enzyme—Crystallographic Study of Glutamate Mutase with Cofactor Homologues

Gruber, K. (Corresponding author)Extern* ; Csitkovits, V. ; Łyskowski, A. ; Kratky, C. ; Kräutler, B. (Corresponding author)

2022
Wiley-VCH Weinheim

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Please use a persistent id in citations: doi:10.1002/ange.202208295  doi:10.3204/PUBDB-2023-00367

Abstract: 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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Contributing Institute(s):

1. DOOR-User (DOOR ; HAS-User)

Research Program(s):

1. 899 - ohne Topic (POF4-899) (POF4-899)

Experiment(s):

1. DORIS Beamline BW7 (DORIS III)

Appears in the scientific report 2022

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Database coverage:
; ; ; DEAL Wiley ; Ebsco Academic Search ; Nationallizenz ; SCOPUS

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