Lactate dehydrogenase-B cDNA from the teleost Fundulus heteroclitus: evolutionary implications.
A cDNA that encodes the heart-type lactate dehydrogenase (LDH-B) from the teleost fish Fundulus heteroclitus was cloned and sequenced. The protein encoded by the cDNA was analyzed in relation to 13 LDH proteins from a variety of taxa. One of the deductions from this analysis is that LDH-B proteins have residues in the active site that are unique and that may be important in determining the biochemistry of the heart-type isozyme. Phylogenetic analysis of the LDH sequences indicates that the branch lengths are greater in lower vertebrates, suggesting that the amino acid replacement rates vary depending on the evolutionary constraints within each taxon. Furthermore, the analysis suggests that LDH-C arose prior to the divergence of the LDH-A and LDH-B isozymes and thus that it is probably ancestral to these isozymes.
Crawford
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DL
Department of Biology, Johns Hopkins University.
Constantino
H R
HR
Powers
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DA
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D005075:Biological Evolution; D003532:Cyprinodontiformes / Q000235:genetics*; D004247:DNA / Q000235:genetics; D007527:Isoenzymes; D007695:Killifishes / Q000235:genetics*; D007770:L-Lactate Dehydrogenase / Q000235:genetics*; D008969:Molecular Sequence Data; D009206:Myocardium / Q000201:enzymology; D010802:Phylogeny; D012689:Sequence Homology, Nucleic Acid
D007527:Isoenzymes; D004247:DNA; D007770:L-Lactate Dehydrogenase