BioDesign 2022; 10(4): 57-63
Published online December 30, 2022
© Korean Society for Structural Biology
Jie Zhang1,2,†, Tingting Bu1,2,†, Yuanyuan Chen1,2, Xue Bai1,2, Shanru He1,2 and Yongbin Xu1,2,*
1Department of Bioengineering, College of Life Science, Dalian Minzu University, Dalian 116600, Liaoning, China
2Key Laboratory of Biotechnology and Bioresources Utilization of Ministry of Education, College of Life Science, Dalian Minzu University, Dalian 116600, China
Correspondence to: *email@example.com
†These authors contributed equally to this work.
Clostridium beijerinckii is a promising industrial microorganism for its ability to produce butanol, acetone, and isopropanol using a wide range of substrates, including pentoses, hexoses, and starch, via fermentation. The ubiquitous and highly abundant glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is essential for most organisms’ energy and carbon metabolism, which plays a critical role in some industrial bacteria. It catalyzes the simultaneous oxidation and phosphorylation of D-glyceraldehyde-3-phosphate into 1,3-bisphosphoglycerate in the presence of inorganic phosphate and nicotinamide adenine dinucleotide (NAD+). We determined the crystal structure of the GAPDH from C. beijerinckii (C. beijerinckii GAPDH). C. beijerinckii GAPDH consists of an α-β-α domain which shares an evolutionarily conserved fold consisting of two juxtaposed domains, an N-terminal NAD+-binding domain (NBD) and a C-terminal catalytic domain (CD). These findings provide insight into the molecular mechanism of action and cofactor-binding of this important industrial bacterial enzyme.