Open AccessDrosophila Lactate Dehydrogenase. Functional and Evolutionary Aspects
Author(s) -
Karvountzi E.,
Kilias G.,
Alahiotis S. N.
Publication year - 1995
Publication title -
hereditas
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.819
H-Index - 50
eISSN - 1601-5223
pISSN - 0018-0661
DOI - 10.1111/j.1601-5223.1995.00061.x
Subject(s) - biology , lactate dehydrogenase , drosophila (subgenus) , evolutionary biology , l lactate dehydrogenase , genetics , biochemistry , enzyme , gene
The functional characteristics of homogeneously purified LDH were studied in the eight D. melanogaster species subgroup at two different growing temperatures (14°C, 25°C). The V max , k cat , V max /K c NAD . K m LaC and k Cat /K s NAD K m LaC values detected at the permissive growink temperature of 25°C, were found to converge with the consensus phylogeny of these species which consists of two ( melanogaster, yakuba ) complexes. This scheme, also verified by the Micro‐Complement Fixation (MC'F) method in another study in our Laboratory, substantiates the connection between the enzyme function and the phylogeny of these species. We propose that the major variation of the Ldh gene in this subgroup has arisen prior to the first species divergence, the final result of which is the eight sibling species. On the other hand, the variable catalytic differentiation observed at the restrictive temperature of 14°C may enrich the species with hidden adaptive possibilities.