Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.jsb.2013.03.001
Title: Structural basis for cofactor and substrate selection by cyanobacterium succinic semialdehyde dehydrogenase
Authors: Yuan, Z.
Yin, B.
Wei, D.
Yuan, Y.R.A. 
Keywords: Cofactor preference
Crystal structures
G. oxydans ALDH Gox0499
Substrate selection
Synechococcus SSADH (Sp2771)
Issue Date: May-2013
Citation: Yuan, Z., Yin, B., Wei, D., Yuan, Y.R.A. (2013-05). Structural basis for cofactor and substrate selection by cyanobacterium succinic semialdehyde dehydrogenase. Journal of Structural Biology 182 (2) : 125-135. ScholarBank@NUS Repository. https://doi.org/10.1016/j.jsb.2013.03.001
Abstract: Aldehyde dehydrogenase (ALDH) catalyzes the oxidation of aldehydes to carboxylic acids. Cyanobacterium Synechococcus contains one ALDH enzyme (Sp2771), together with a novel 2-oxoglutarate decarboxylase, to complete a non-canonical tricarboxylic acid cycle. However, the molecular mechanisms for substrate selection and cofactor preference by Sp2771 are largely unknown. Here, we report crystal structures of wild type Sp2771, Sp2771 S419A mutant and ternary structure of Sp2771 C262A mutant in complex with NADP+ and SSA, as well as binary structure of Gluconobacter oxydans aldehyde dehydrogenase (Gox0499) in complex with PEG. Structural comparison of Sp2771 with Gox0499, coupled with mutational analysis, demonstrates that Ser157 residue in Sp2771 and corresponding Pro159 residue in Gox0499 play critical structural roles in determining NADP+ and NAD+ preference for Sp2771 and Gox0499, respectively, whereas size and distribution of hydrophobic residues along the substrate binding funnel determine substrate selection. Hence, our work has provided insightful structural information into cofactor and substrate selection by ALDH. © 2013 Elsevier Inc.
Source Title: Journal of Structural Biology
URI: http://scholarbank.nus.edu.sg/handle/10635/101742
ISSN: 10478477
DOI: 10.1016/j.jsb.2013.03.001
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