PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 8917428-0 1996 Threonine autophosphorylation and nucleotidylation of the hepatic membrane protein PC-1. Threonine 0-9 ectonucleotide pyrophosphatase/phosphodiesterase 1 Homo sapiens 83-87 8917428-2 1996 It has been suggested, however, that PC-1 is not a real protein kinase and that the autophosphorylated enzyme represents a nucleotidylated derivative, which is formed on Thr238 (murine PC-1) as a catalytic intermediate during ATP hydrolysis [Belli, S.I., Mercuri, F.A., Sali, A.& Goding, J.W. Adenosine Triphosphate 226-229 ectonucleotide pyrophosphatase/phosphodiesterase 1 Mus musculus 185-189 8917428-2 1996 It has been suggested, however, that PC-1 is not a real protein kinase and that the autophosphorylated enzyme represents a nucleotidylated derivative, which is formed on Thr238 (murine PC-1) as a catalytic intermediate during ATP hydrolysis [Belli, S.I., Mercuri, F.A., Sali, A.& Goding, J.W. Adenosine Monophosphate 279-282 ectonucleotide pyrophosphatase/phosphodiesterase 1 Mus musculus 185-189 8917428-6 1996 We have investigated the proposed multifunctional role of PC-1 and show here that ATP hydrolysis and autophosphorylation represent two distinct catalytic reactions. Adenosine Triphosphate 82-85 ectonucleotide pyrophosphatase/phosphodiesterase 1 Homo sapiens 58-62 8917428-12 1996 We propose that autophosphorylation of PC-1 on Thr238 at low ATP concentrations serves as an autoregulatory mechanism that makes Thr238 unavailable for participation in the hydrolysis of extracellular nucleotides when they become scarce. Adenosine Triphosphate 61-64 ectonucleotide pyrophosphatase/phosphodiesterase 1 Homo sapiens 39-43