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EC Number Subunits Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.379? x * 38000, recombinant His-tagged enzyme, SDS-PAGE 763170
Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.379dimer 2 * 38000, SDS-PAGE -, 730341
Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.379homodimer D-ManDH2 constitutively forms a dimeric structure. Each of the two subunits binds the NADH and AOA molecules between the N-terminal (residues 1-176) and C-terminal (residues 180-311). The intersubunit contact is formed between the two C-terminal domains of the dimer on the opposite side of NADH and AOA, and exhibits no significant structural change among the three D-ManDH2 structures. The N-terminal domain exhibits a shear motion along the C-terminal domain between the binary and ternary complex structures, following the domain closure through the hinge motion between the apo and binary complex structures. Residue Asn105 forms hydrogen bonds with both the nicotinamide-ribose of NADH and the carbonyl oxygen of AOA in the ternary complex structure, suggesting that this residue promotes the shear motion of the N-terminal domain 762694
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