Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: EC:2.7.11.2 (
PDK1
)
2,238
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Succinyl-CoA synthetase and the alpha-subunit of pyruvate dehydrogenase are phosphorylated after incubation of mitochondria from brain, heart, and liver with [gamma-32P]ATP. Dichloroacetate, a known specific inhibitor for
pyruvate dehydrogenase kinase
, inhibits not only the phosphate incorporation into the alpha-subunit of pyruvate dehydrogenase but also the autophosphorylation of
succinyl-CoA synthetase
. AMP also inhibits the phosphorylation of both proteins. Phosphorylation of the alpha-subunit of pyruvate dehydrogenase in liver mitochondria is significantly lower than in mitochondria from other tissues.
...
PMID:The effect of dichloroacetate on the phosphorylation of mitochondria proteins. 683 84
Serine and threonine kinase
STK1
and STK2 play an important regulatory role in the process of pollen development in maize. Six homologous sequences which were similar with
STK1
and STK2 having more than 80 % similarity were found at NCBI, and they all belong to
STK
gene family. Phylogenetic analysis showed that
STK
family in maize might belong to RLK family. In
STK
family, gene duplication event was occurred during evolutionary process, and experienced purifying selection after gene duplication and the time of gene duplication was about 12 million years ago. The domains of
STK
family belongs to single transmembrane protein, which have intracellular conserved kinase catalytic domain and extracellular receptor domain on N-terminal. The evolution of intracellular selection was faster than extracellular selection, and positive selection or weak purifying selection play an important role. Analyzing its unique Usp domain we found that it was located between sensor domain at N-terminal and catalytic domain at C-terminal, which belongs to hydrophobic protein with several phosphorylation sites, acting on serine and threonine protein phosphorylation. The kinship of Usp domain in
STK
family was close to 35-like protein containing U-box domain, predicting that they might belong to the same family with a similar structure and function, so that we can predict the function of Usp domain in
STK
family.
...
PMID:Phylogenetic analysis of STK gene family and Usp domain in maize. 2532 19