THE NUCLEOTIDE AND DEDUCED AMINO-ACID-SEQUENCES OF A CDNA-ENCODING LACTATE-DEHYDROGENASE FROM CAENORHABDITIS-ELEGANS - THE EVOLUTIONARY RELATIONSHIPS OF LACTATE-DEHYDROGENASES FROM MAMMALS, BIRDS, AMPHIBIAN, FISH, NEMATODE, PLANTS, BACTERIA, MYCOPLASMA, AND PLASMODIUM

The nucleotide and deduced amino-acid sequences of a cDNA encoding L-l actate dehydrogenase (LDH) from nematode, Caenorhabditis elegans, were reported. This first invertebrate LDH sequence of 333 amino acids, in cluding the initiation methionine, exhibits 63% identity with that of the most primitive vertebrate lamprey. The evolutionary relationships among 36 LDH isozymes from mammals, birds, amphibian, fish, nematode, plants, bacteria, mycoplasma and plasmodium were analyzed. The inverte brate nematode LDH is evolutionarily positioned between plant LDH and mammalian testicular LDH-C isozymes. The mammalian LDH-C isozyme appea rs to have arisen after the invertebrate LDH, but prior to the diverge nce of vertebrate LDH-A (muscle) and LDH-B (heart) isozymes as describ ed previously. (C) 1994 Academic Press, Inc.