Crystal Structure of Glycerol Dehydrogenase from Klebsiella pneumoniae

被引:0
作者
Ko, Gyeong Soo [2 ]
Nguyen, Thang Quyet [2 ]
Koh, Seri [1 ,2 ,3 ]
Kang, Wonchull [1 ,2 ,3 ]
机构
[1] Soongsil Univ, Coll Nat Sci, Dept Chem, Seoul 06978, South Korea
[2] Soongsil Univ, Integrat Inst Basic Sci, Coll Nat Sci, Seoul 06978, South Korea
[3] Soongsil Univ, Dept Green Chem & Mat Engn, Seoul 06978, South Korea
来源
JOURNAL OF THE KOREAN CHEMICAL SOCIETY-DAEHAN HWAHAK HOE JEE | 2024年 / 68卷 / 01期
关键词
Glycerol dehydrogenase; GldA; Glycerol; Ethylene glycol; Biofuel; ESCHERICHIA-COLI; MOLECULAR CHARACTERIZATION; PURIFICATION; 1,3-PROPANEDIOL; REGENERATION;
D O I
10.5012/jkcs.2024.68.1.32
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
. Glycerol dehydrogenase (GlyDH) plays a crucial role in the glycerol metabolism pathway by catalyzing the oxidation of glycerol to dihydroxyacetone (DHA). Previous studies of GlyDH have predominantly focused on unraveling the structural features of the active site and its binding interactions with ligand. However, the structural details of GlyDH in complex with both NAD+ and the substrate bound have remained elusive. In this study, we present the crystal structures of Klebsiella pneumoniae GlyDH (KpGlyDH) in the absence and presence of NAD+ at a resolution of 2.1 angstrom. Notably, both structures reveal the binding of the substrate, ethylene glycol, to the zinc ion. Interestingly, a significant change in the coordination number of the zinc ion is observed, with three in the absence of NAD+ and four in its presence. These findings shed light on the structural aspects of GlyDH and its interactions with NAD+ and the substrate.
引用
收藏
页码:32 / 39
页数:8
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