High impact information on LDHA

• Nucleotide and deduced amino acid sequences of chicken lactate dehydrogenase-A [1].
• Evolution of lactate dehydrogenase-A homologs of barracuda fishes (genus Sphyraena) from different thermal environments: differences in kinetic properties and thermal stability are due to amino acid substitutions outside the active site [2].
• We used a full-length cDNA clone of LDH-A of S. lucasana to test, by site-directed mutagenesis, the importance of these sequence changes in establishing the observed differences in kinetics and thermal stability [2].
• Orthologous homologs of lactate dehydrogenase-A (LDH-A) (EC 1.1.1.27; NAD+:lactate oxidoreductase) of six barracuda species (genus Sphyraena) display differences in Michaelis-Menten constants (apparent Km) for substrate (pyruvate) and cofactor (NADH) that reflect evolution at different habitat temperatures [2].
• Lactate dehydrogenase (LDH) isoenzymes, LDH-A and LDH-B, are expressed in premeiotic, meiotic cells, and early spermatids, both in avian and mammalian spermatogenesis [3].

Anatomical context of LDHA

• In the GB the subtype of LDH mRNA was LDM-B only, and in the cerebral cortex and spinal cord, the subtype of LDH mRNA was predominantly LDH-B, and a small amount of LDH-A was found in the chicken and embryo [4].
• Highly polyadenylated forms, particularly of LDH-A, were detected in chicken testis [3].

References