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A plant‐derived  Enterococcus mundtii  15‐1A, that has been previously isolated from  Brassica rapa  L. subsp.  nipposinica  (L.H. Bailey) Hanelt var.  linearifolia  by our group, possesses two kinds of  l ‐lactate dehydrogenase ( l ‐LDH): LDH‐1 and LDH‐2. LDH‐1 was activated under low concentration of fluctose‐1,6‐bisphosphate (FBP) at both pH 5.5 and 7.5. Although LDH‐2 was also activated under the low concentration of FBP at pH 5.5, a high concentration of FBP is necessary to activate it at pH 7.5. The present study shows the crystal structures of the acidophilic LDH‐2 in a complex with and without FBP and NADH. Although the tertiary structure of the ligands‐bound LDH‐2 is similar to that of the active form of other bacterial  l ‐LDHs, the structure without the ligands is different from that of any other previously determined  l ‐LDHs. Major structural alterations between the two structures of LDH‐2 were observed at two regions in one subunit. At the  N ‐terminal parts of the two regions, the ligands‐bound form takes an α‐helical structure, while the form without ligands displays more disordered and extended structures. A vacuum‐ultraviolet circular dichroism analysis showed that the α‐helix content of LDH‐2 in solution is approximately 30% at pH 7.5, which is close to that in the crystal structure of the form without ligands. A D241N mutant of LDH‐2, which was created by us to easily form an α‐helix at one of the two parts, exhibited catalytic activity even in the absence of FBP at both pH 5.5 and 7.5.

An alternative allosteric regulation mechanism of an acidophilic l ‐lactate dehydrogenase from Enterococcus mundtii 15‐1A