Pyruvate dehydrogenase phosphatase regulatory subunit is a
protein that in humans is encoded by the PDPR
gene.[5]
Structure
The complete
cDNA of PDPR, which contains 2885
base pairs, has an
open reading frame of 2634
nucleotides encoding a putative presequence of 31
amino acid residues and a mature protein of 847. Characteristics of native PDPR include ability to decrease the sensitivity of the catalytic subunit to
Mg2+, and reversal of this inhibitory effect by the polyamine
spermine. A
BLAST search of protein databases revealed that PDPr is distantly related to the mitochondrial flavoprotein
dimethylglycine dehydrogenase, which functions in
choline degradation.[6]
As PDPR is involved in the regulation of the central
metabolic pathway, its participation in disease
pathophysiology is likely, but there has been no published research on this thus far.[5]
^Sugden MC, Holness MJ (May 2003). "Recent advances in mechanisms regulating glucose oxidation at the level of the pyruvate dehydrogenase complex by PDKs". American Journal of Physiology. Endocrinology and Metabolism. 284 (5): E855-62.
doi:
10.1152/ajpendo.00526.2002.
PMID12676647.
Further reading
Sugden MC, Holness MJ (May 2003). "Recent advances in mechanisms regulating glucose oxidation at the level of the pyruvate dehydrogenase complex by PDKs". American Journal of Physiology. Endocrinology and Metabolism. 284 (5): E855-62.
doi:
10.1152/ajpendo.00526.2002.
PMID12676647.
Pyruvate dehydrogenase phosphatase regulatory subunit is a
protein that in humans is encoded by the PDPR
gene.[5]
Structure
The complete
cDNA of PDPR, which contains 2885
base pairs, has an
open reading frame of 2634
nucleotides encoding a putative presequence of 31
amino acid residues and a mature protein of 847. Characteristics of native PDPR include ability to decrease the sensitivity of the catalytic subunit to
Mg2+, and reversal of this inhibitory effect by the polyamine
spermine. A
BLAST search of protein databases revealed that PDPr is distantly related to the mitochondrial flavoprotein
dimethylglycine dehydrogenase, which functions in
choline degradation.[6]
As PDPR is involved in the regulation of the central
metabolic pathway, its participation in disease
pathophysiology is likely, but there has been no published research on this thus far.[5]
^Sugden MC, Holness MJ (May 2003). "Recent advances in mechanisms regulating glucose oxidation at the level of the pyruvate dehydrogenase complex by PDKs". American Journal of Physiology. Endocrinology and Metabolism. 284 (5): E855-62.
doi:
10.1152/ajpendo.00526.2002.
PMID12676647.
Further reading
Sugden MC, Holness MJ (May 2003). "Recent advances in mechanisms regulating glucose oxidation at the level of the pyruvate dehydrogenase complex by PDKs". American Journal of Physiology. Endocrinology and Metabolism. 284 (5): E855-62.
doi:
10.1152/ajpendo.00526.2002.
PMID12676647.