An unusual fructose 1,6-bisphosphate-activated lactate dehydrogenase from the ascidian Pyura stolonifera

@inproceedings{Brennan1995AnUF,
  title={An unusual fructose 1,6-bisphosphate-activated lactate dehydrogenase from the ascidian Pyura stolonifera},
  author={Sue Brennan and Jean S. Holder and John Baldwin},
  year={1995}
}
Abstract Lactate dehydrogenase (LDH) was purified from the siphon muscle of the intertidal ascidian Pyura stolonifera . The enzyme is unique among chordate LDHs but resembles some bacterial and platyhelminth LDHs in being activated by fructose 1,6-bisphosphate (FBP). Concentrations of FBP in the range 5μM to 0.5 mM increase V max of the pyruvate reductase reaction by 130% to 210%, and decrease K m pyruvate 5 to 11 fold and K m NADH 2.5 to 5 fold. The enzyme is also activated by inorganic… CONTINUE READING

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