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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
MeSH Review

Catalytic Domain

 
 
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Disease relevance of Catalytic Domain

 

Psychiatry related information on Catalytic Domain

 

High impact information on Catalytic Domain

  • IKK contains two catalytic subunits, IKKalpha and IKKbeta, both of which are able to correctly phosphorylate IkappaB [7].
  • Although lacking catalytic domains, all the receptors couple ligand binding to the rapid induction of protein tyrosine phosphorylation [8].
  • Structure-function analysis of CD45 and other PTPs has identified structural features of PTP catalytic domains required for enzymatic activity [9].
  • Circularly permuted polypeptide chains are being used to study the folding and assembly pathways, and the recently determined crystal structure of the active nonallosteric catalytic subunit has led to new questions regarding the activated form of ATCase [10].
  • Other structural and mutational probes of the F1 and F0 portions of the ATP synthase are reviewed, together with kinetic and other evaluations of catalytic site occupancy and behavior during hydrolysis or synthesis of ATP [11].
 

Chemical compound and disease context of Catalytic Domain

 

Biological context of Catalytic Domain

 

Anatomical context of Catalytic Domain

 

Associations of Catalytic Domain with chemical compounds

  • Four major serine/threonine-specific protein phosphatase catalytic subunits are present in the cytoplasm of animal cells [22].
  • Protein kinase casein kinase II (Ck2) is a cyclic-AMP and calcium-independent serine-threonine kinase that is composed of two catalytic subunits (alpha and alpha') and two regulatory beta-subunits [27].
  • The posttranslational conversion of cysteine to C(alpha)-formylglycine in the catalytic site of mammalian sulfatases is deficient in the rare but devastating disorder multiple sulfatase deficiency (MSD) [28].
  • A gene (pkn1) thus cloned contains an ORF of 693 amino acid residues whose amino-terminal domain shows significant sequence similarity with the catalytic domain of eukaryotic protein serine/threonine kinases [29].
  • In liver and muscle, loss of the major regulatory isoform caused a great decrease in expression and activity of class IA Pi3k catalytic subunits; nevertheless, homozygous mice still displayed hypoglycaemia, lower insulin levels and increased glucose tolerance [30].
 

Gene context of Catalytic Domain

 

Analytical, diagnostic and therapeutic context of Catalytic Domain

References

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  30. Hypoglycaemia, liver necrosis and perinatal death in mice lacking all isoforms of phosphoinositide 3-kinase p85 alpha. Fruman, D.A., Mauvais-Jarvis, F., Pollard, D.A., Yballe, C.M., Brazil, D., Bronson, R.T., Kahn, C.R., Cantley, L.C. Nat. Genet. (2000) [Pubmed]
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