Structurally Linked Dynamics in Lactate Dehydrogenases of Evolutionarily Distinct Species.

ABSTRACT: We present new findings about how primary and secondary structure affects the role of fast protein motions in the reaction coordinates of enzymatic reactions. Using transition path sampling and committor distribution analysis, we examined the difference in the role of these fast protein motions in the reaction coordinate of lactate dehydrogenases (LDHs) of Apicomplexa organisms Plasmodium falciparum and Cryptosporidium parvum. Having evolved separately from a common malate dehydrogenase ancestor, the two enzymes exhibit several important structural differences, notably a five-amino acid insertion in the active site loop of P. falciparum LDH. We find that these active site differences between the two organisms' LDHs likely cause a decrease in the contribution of the previously determined LD

SUBMITTER: Varga MJ 

PROVIDER: S-EPMC5507060 | biostudies-literature | 2017 May

REPOSITORIES: biostudies-literature