Premium
Pyridine Nucleotide‐Linked Lactate Dehydrogenase of Tetrahymena : Evidence for D‐ and L‐Enzymes in the Mitochondria
Author(s) -
Stearns Frank M.,
Eichel Herbert J.
Publication year - 2021
Publication title -
journal of eukaryotic microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.067
H-Index - 77
eISSN - 1550-7408
pISSN - 1066-5234
DOI - 10.1111/jeu.12851
Subject(s) - nad+ kinase , biochemistry , biology , tetrahymena , mitochondrion , lactate dehydrogenase , enzyme , oxidative phosphorylation , flavoprotein , respiratory chain , dehydrogenase , oxidase test , nadh dehydrogenase , mitochondrial dna , gene
An NAD‐linked lactate dehydrogenase (LDH) in a crude mitochondrial fraction obtained from Tetrahymena homogenates was previously reported by this laboratory. This fraction contains the NADH and succinate oxidase system as well as the mitochondrial cytochromes and carries out oxidative phosphorylation. The preparation catalyzes the oxidation of D‐ and L‐lactate linked only to certain analogs of NAD; it has not been possible to demonstrate NAD‐dependent D‐ or L‐lactate oxidation nor is there any evidence that either of these enzymes is a flavoprotein as indicated by their inability to reduce directly certain artificial electron acceptors. A lactate racemase is not present.