Journal
JOURNAL OF INORGANIC BIOCHEMISTRY
Volume 105, Issue 10, Pages 1259-1272Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.jinorgbio.2011.06.006
Keywords
Vicinal Oxygen Chelate; Isomerase; Epimerase; Dioxygenase; Metal; VOC
Funding
- National Science Foundation [MCB0843619]
- UWM Research Growth Initiative
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The vicinal oxygen chelate family of enzymes catalyzes a highly diverse set of chemistries that derives from one common mechanistic trait: bidentate coordination to a divalent metal center by a substrate or intermediate or transition state through vicinal oxygen atoms. The array of reactions catalyzed by this family is mediated structurally by a common fold and protein-chelating residues that secure and localize a metal ion. The common fold has topological symmetry being comprised of two beta alpha beta beta beta units that form an incompletely closed barrel of beta-sheet about the metal ion. Interestingly, despite the diversity of the reactions catalyzed and the large number of metals observed to bind and promote the chemistry, this semi-symmetrical open barrel extends metal liganding side chains inward from a highly positionally conserved constellation of amino acid residues within the structure. Moreover, the core barrel fold arises from an array of possible intra/inter domain and subunit arrangements of the individual beta alpha beta beta beta units that are universally observed to stack side-by-side contacting along the first beta-strand of each. While there are examples of enzymes that use this fold and do not bind a metal ion, this review is concerned with summarizing the key structural and mechanistic correlations that can be made for the metal-dependent vicinal oxygen chelate enzyme family members. (C) 2011 Elsevier Inc. All rights reserved.
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