The molecular basis of these adaptations in the pika have occurred because of a series of genetic evolutionary changes, including HIF-1 a (Li et al., 2009; Zhao et al., 2004), hemoglobin (Yang et al., 2007), vascular endothelial growth factor (VEGF) (Li et al., 2013; Zheng et al., 2011) testis-specific lactate dehydrogenase (LDH-C4) (Wang et al., 2013), pyruvate carboxylase (Sun et al., 2013), myoglobin (Qi et al., 2008), cytochromec oxidase (Luo et al., 2008), neuron nitric oxide synthase (nNOS) (Pichon et al., 2009), and leptin (Yang et al., 2006, 2008).
The lactate dehydrogenase (LDH) family enzymes catalyze the inter-conversion of pyruvate to lactate with the concomitant oxidation/reduction of NADH to NAD+ (Everse and Kaplan, 1973).
Furthermore, the [I.sub.50] values for ATP and ADP were approximately 2-fold and 5-fold higher, respectively, for anoxic LDH as compared to the control (Table 2), while somewhat rare, inhibition of lactate dehydrogenase by ATP has been shown before in numerous bacteria , and as seen in this study, it is a very weak inhibitor.
Storey, "Purification and properties of white muscle lactate dehydrogenase from the anoxia-tolerant turtle, the red-eared slider, Trachemys scripta elegans," Enzyme Research, vol.
Lactate dehydrogenase (LDH; EC.22.214.171.124) catalyzes this interconversion with nicotinamide adenine dinucleotide (NAD+) as coenzyme.
DNA methylation and expression of genes coding for lactate dehydrogenase A and C during rodent spermatogenesis.
falciparum lactate dehydrogenase (PfLDH) is essential for the anaerobic lifestyle of Plasmodium and a potential drug target .
Barker et al., "The structure of lactate dehydrogenase from Plasmodium falciparum reveals a new target for anti-malarial design," Nature Structural Biology, vol.
Properties of testicular lactate dehydrogenase isoenzyme.
Lactate dehydrogenase X, malate dehydrogenase and total protein in rat spermatozoa during epididymal transit.
During metabolism, lactate dehydrogenase, a well-characterized enzyme found in many animals, converts a compound called pyruvate into one called lactate.
In the notothenioids, lactate dehydrogenase converts pyruvate at speeds comparable to those in animals with higher body temperatures, even though cold generally slows such reactions.