 |
VOOZH | about |
|
VOOZH | about |
*615499
Table of Contents
Alternative titles; symbols
HGNC Approved Gene Symbol: PDP2
Cytogenetic location: 16q22.1 Genomic coordinates (GRCh38) : 16:66,880,515-66,891,101 (from NCBI)
Pyruvate dehydrogenase phosphatases (EC 3.1.3.43) are mitochondrial serine phosphatases that dephosphorylate and activate the inactive phosphorylated pyruvate dehydrogenase complex. Unlike PDP1, which has both catalytic (PDP1; 605993) and regulatory (PDPR; 617835) subunits, PDP2 consists of only a catalytic subunit (Kato and Kato, 2010).
By sequencing clones obtained from a size-fractionated fetal brain cDNA library, Nagase et al. (2000) cloned PDP2, which they designated KIAA1348. The deduced 545-amino acid protein shares 84% identity with rat Pdp2. RT-PCR ELISA detected PDP2 expression in all adult and fetal tissues and specific adult brain regions examined. Expression was highest in adult ovary and lowest in adult spleen and skeletal muscle.
Huang et al. (1998) found that both recombinant rat Pdp1 and Pdp2 showed high specificity for the pyruvate dehydrogenase complex and little to no activity for the related mitochondrial multienzyme complex, branched-chain alpha-ketoacid dehydrogenase (see 608348). However, the phosphatases showed significantly different kinetics and dependence on cofactors. Pdp2 showed almost 10-fold lower sensitivity to Mg(2+) than Pdp1, and only Pdp1 was regulated by Ca(2+). Pdp2 also showed sensitivity to spermine, which had no effect on Pdp1.
By radiation hybrid analysis, Nagase et al. (2000) mapped the PDP2 gene to chromosome 16. Hartz (2013) mapped the PDP2 gene to chromosome 16q22.1 based on the alignment of the PDP2 sequence (GenBank AB037769) with the genomic sequence (GRCh37).
Hartz, P. A. Personal Communication. Baltimore, Md. 10/25/2013.
Huang, B., Gudi, R., Wu, P., Harris, R. A., Hamilton, J., Popov, K. M. Isoenzymes of pyruvate dehydrogenase phosphatase: DNA-derived amino acid sequences, expression, and regulation. J. Biol. Chem. 273: 17680-17688, 1998. [PubMed: 9651365, related citations] [Full Text]
Kato, J., Kato, M. Crystallization and preliminary crystallographic studies of the catalytic subunits of human pyruvate dehydrogenase phosphatase isoforms 1 and 2. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 66: 342-345, 2010. [PubMed: 20208177, images, related citations] [Full Text]
Nagase, T., Kikuno, R., Ishikawa, K., Hirosawa, M., Ohara, O. Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 7: 65-73, 2000. [PubMed: 10718198, related citations] [Full Text]
Alternative titles; symbols
HGNC Approved Gene Symbol: PDP2
Cytogenetic location: 16q22.1 Genomic coordinates (GRCh38) : 16:66,880,515-66,891,101 (from NCBI)
Pyruvate dehydrogenase phosphatases (EC 3.1.3.43) are mitochondrial serine phosphatases that dephosphorylate and activate the inactive phosphorylated pyruvate dehydrogenase complex. Unlike PDP1, which has both catalytic (PDP1; 605993) and regulatory (PDPR; 617835) subunits, PDP2 consists of only a catalytic subunit (Kato and Kato, 2010).
By sequencing clones obtained from a size-fractionated fetal brain cDNA library, Nagase et al. (2000) cloned PDP2, which they designated KIAA1348. The deduced 545-amino acid protein shares 84% identity with rat Pdp2. RT-PCR ELISA detected PDP2 expression in all adult and fetal tissues and specific adult brain regions examined. Expression was highest in adult ovary and lowest in adult spleen and skeletal muscle.
Huang et al. (1998) found that both recombinant rat Pdp1 and Pdp2 showed high specificity for the pyruvate dehydrogenase complex and little to no activity for the related mitochondrial multienzyme complex, branched-chain alpha-ketoacid dehydrogenase (see 608348). However, the phosphatases showed significantly different kinetics and dependence on cofactors. Pdp2 showed almost 10-fold lower sensitivity to Mg(2+) than Pdp1, and only Pdp1 was regulated by Ca(2+). Pdp2 also showed sensitivity to spermine, which had no effect on Pdp1.
By radiation hybrid analysis, Nagase et al. (2000) mapped the PDP2 gene to chromosome 16. Hartz (2013) mapped the PDP2 gene to chromosome 16q22.1 based on the alignment of the PDP2 sequence (GenBank AB037769) with the genomic sequence (GRCh37).
Hartz, P. A. Personal Communication. Baltimore, Md. 10/25/2013.
Huang, B., Gudi, R., Wu, P., Harris, R. A., Hamilton, J., Popov, K. M. Isoenzymes of pyruvate dehydrogenase phosphatase: DNA-derived amino acid sequences, expression, and regulation. J. Biol. Chem. 273: 17680-17688, 1998. [PubMed: 9651365] [Full Text: https://doi.org/10.1074/jbc.273.28.17680]
Kato, J., Kato, M. Crystallization and preliminary crystallographic studies of the catalytic subunits of human pyruvate dehydrogenase phosphatase isoforms 1 and 2. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 66: 342-345, 2010. [PubMed: 20208177] [Full Text: https://doi.org/10.1107/S1744309110003131]
Nagase, T., Kikuno, R., Ishikawa, K., Hirosawa, M., Ohara, O. Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 7: 65-73, 2000. [PubMed: 10718198] [Full Text: https://doi.org/10.1093/dnares/7.1.65]
Dear OMIM User,
To ensure long-term funding for the OMIM project, we have diversified our revenue stream. We are determined to keep this website freely accessible. Unfortunately, it is not free to produce. Expert curators review the literature and organize it to facilitate your work. Over 90% of the OMIM's operating expenses go to salary support for MD and PhD science writers and biocurators. Please join your colleagues by making a donation now and again in the future. Donations are an important component of our efforts to ensure long-term funding to provide you the information that you need at your fingertips.
Thank you in advance for your generous support,
Ada Hamosh, MD, MPH
Scientific Director, OMIM