Article: Crystal structure of L-arabinose 1-dehydrogenase as a short-chain reductase/dehydrogenase protein
Biochemical and biophysical research communications. 2022 May 14, v. 604
2022
Abstract: l-Arabinose 1-dehydrogenase (AraDH) catalyzes the NAD(P)⁺-dependent oxidation of l-arabinose to L-arabinono-1,4-lactone in the non-phosphorylative l-arabinose pathway, and is classified into glucose-fructose oxidoreductase and short-chain dehydrogenase/ ... ...
Abstract | l-Arabinose 1-dehydrogenase (AraDH) catalyzes the NAD(P)⁺-dependent oxidation of l-arabinose to L-arabinono-1,4-lactone in the non-phosphorylative l-arabinose pathway, and is classified into glucose-fructose oxidoreductase and short-chain dehydrogenase/reductase (SDR). We herein report the crystal structure of a SDR-type AraDH (from Herbaspirillum huttiense) for the first time. The interactions between Asp49 and the 2′- and 3′-hydroxyl groups of NAD⁺ were consistent with strict specificity for NAD⁺. In a binding model for the substrate, Ser155 and Tyr168, highly conserved in the SDR superfamily, interacted with the C1 and/or C2 hydroxyl(s) of l-arabinose, whereas interactions between Asp107, Arg109, and Gln206 and the C2 and/or C3 hydroxyl(s) were unique to AraDH. Trp200 significantly contributed to the selectivities of the C4 hydroxyl and C6 methyl of substrates. |
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Keywords | Herbaspirillum ; arabinose ; crystal structure ; models ; oxidation ; oxidoreductases ; research |
Language | English |
Dates of publication | 2022-0514 |
Size | p. 14-21. |
Publishing place | Elsevier Inc. |
Document type | Article |
ZDB-ID | 205723-2 |
ISSN | 0006-291X ; 0006-291X |
ISSN (online) | 0006-291X |
ISSN | 0006-291X |
DOI | 10.1016/j.bbrc.2022.03.028 |
Database | NAL-Catalogue (AGRICOLA) |
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