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

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Query: EC:2.7.11.1 (protein kinase)
81,284 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A functional vascular smooth-muscle actin from bovine aorta was purified to homogeneity by an original method and was able to polymerize. Aortic actin is composed of two major isoforms and at least two minor ones. This actin was not phosphorylated by either cyclic AMP-dependent protein kinase or C kinase. The physical properties of aortic actin were found to be very similar to those of skeletal-muscle actin, except for amino acid composition (three tryptophan residues instead of four). The aortic actin and skeletal-muscle actin differ in the extent of activation of the Mg-dependent ATPase of skeletal-muscle myosin.
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PMID:Preparation and characterization of bovine aortic actin. 316 Mar 41

cdc2+ and CDC28 play central roles in the cell division cycles of the widely divergent yeasts Schizosaccharomyces pombe and Saccharomyces cerevisiae, respectively. The genes encode protein kinases that show 62% protein sequence identity and are capable of cross-complementation. Monoclonal antibodies were raised against p34cdc2, and a subset recognize p36cdc28. The cross-reacting antibodies detected a 34 kd homolog of the p34cdc2/p36CDC28, protein in HeLa cells. Human p34 was also recognized by an affinity-purified polyclonal anti-p34cdc2 serum. Peptide mapping of p34cdc2, p36CDC28, and human p34 revealed complete conservation of four tryptophan residues in the three proteins. p34 thus appears to be closely related to the two yeast proteins. In addition, a p34 immune complex showed protein kinase activity in vitro, and HeLa cell p34 interacts with p13, the human homolog of the suc1+ gene product of S. pombe.
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PMID:Identification of p34 and p13, human homologs of the cell cycle regulators of fission yeast encoded by cdc2+ and suc1+. 329 53

The complete amino acid sequence of bovine brain DARPP-32, a dopamine- and cyclic AMP-regulated neuronal phosphoprotein, which is a potent and specific inhibitor of the catalytic subunit of protein phosphatase-1, has been determined. The S-14C-carboxymethylated protein was subjected to enzymatic cleavage by endoproteinase Lys-C, endoproteinase Arg-C, trypsin, chymotrypsin, and Staphylococcus aureus V8 protease, and to chemical cleavage by cyanogen bromide. The overlapping sets of peptides were purified by high performance liquid chromatography and subjected to amino acid sequencing by automated Edman degradation to deduce the complete sequence. The protein consists of a single NH2-terminal blocked polypeptide chain of 202 residues, with a calculated molecular mass of 22,591 daltons, excluding the unidentified NH2-terminal blocking group. This molecular mass is significantly lower than earlier estimates based on sodium dodecyl sulfate-polyacrylamide gel electrophoresis or hydrodynamic measurements. The threonine residue that is phosphorylated by cyclic AMP-dependent protein kinase (Hemmings, H. C., Jr., Williams, K. R., Konigsberg, W. H., and Greengard, P. (1984) J. Biol. Chem. 259, 14486-14490), and that must be phosphorylated for the expression of inhibitory activity, is located at position 34. The molecule contains only 1 cysteine residue and 1 tryptophan residue, at positions 72 and 161, respectively. DARPP-32 is very hydrophilic, and contains a stretch of 16 consecutive acidic residues from position 119 to 134. The predicted secondary structure suggests the presence of 47% alpha-helix, 7% beta-sheet, and 46% random coil, with 11 beta-turns. Comparison of the complete amino acid sequence of bovine DARPP-32 with that of rabbit skeletal muscle protein phosphatase inhibitor-1 revealed a significant amount of sequence identity in the NH2-terminal regions of these two proteins. The active region of inhibitor-1 has been localized to an NH2-terminal fragment (Aitken, A., and Cohen, P. (1982) FEBS Lett. 147, 54-58), the part of the molecule that is most similar to DARPP-32. These data suggest that these two protein phosphatase inhibitors may share a common structural basis for their inhibitory activity and may be related by a common ancestral gene.
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PMID:DARPP-32, a dopamine- and cyclic AMP-regulated neuronal phosphoprotein. Primary structure and homology with protein phosphatase inhibitor-1. 351 Oct 54

In the course of determining the primary structure of rabbit skeletal muscle myosin light chain kinase (MLCK; ATP:protein phosphotransferase, EC 2.7.1.37) a peptide fragment was obtained that appears to represent the calmodulin-binding domain of this enzyme. Low concentrations of the peptide inhibited calmodulin activation of MLCK (Ki congruent to 1 nM). The peptide was not associated with a catalytically active, calmodulin-independent form of MLCK that was obtained by limited proteolysis. The peptide is 27 residues in length and represents the carboxyl terminus of MLCK. The sequence of the peptide shows no significant homology with any known protein sequence. The peptide contains one tryptophanyl residue and a high percentage of basic and hydrophobic residues, but no acidic or prolyl residues. Much of the sequence has a high probability of forming alpha helix. A chemically synthesized peptide has been prepared to study the interactions of the peptide and calmodulin in more detail. The intrinsic tryptophan fluorescence of the synthetic peptide shows a significant enhancement (approximately equal to 45%) in the presence of Ca2+ and calmodulin; fluorescence enhancement is maximal at a peptide:calmodulin stoichiometry of 1:1. Calmodulin-Sepharose affinity chromatography in the presence of 2 M urea indicates that the interaction of peptide and calmodulin is Ca2+-dependent. The results of these studies indicate that the catalytic and calmodulin-binding domains of MLCK represent distinct and separable regions of the protein. In addition, the results provide a basis for future studies of the molecular and evolutionary details of calmodulin-dependent enzyme regulation.
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PMID:Identification of the calmodulin-binding domain of skeletal muscle myosin light chain kinase. 385 14

The amino acid sequence of rabbit skeletal muscle heat-stable inhibitor of the cAMP-dependent protein kinase has been determined by microsequencing techniques. Proof of the structure involved a series of nonoverlapping tryptic fragments for primary identification of 86% of the amino acids. Complementary fragments generated by cleavage with chymotrypsin, Staphylococcus aureus V8 proteinase, and mast cell proteinase II contributed to proof of the structure. The inhibitor is a single polypeptide chain of 75 residues and has a molecular weight of 7829. It lacks tryptophan, proline, and sulfur-containing amino acids. The amino terminus of the inhibitor is blocked by an unidentified group. The amino-terminal region of the molecule contains the kinase inhibitory domain, and synthetic peptides based on the sequence of residues 11-30 are potent competitive inhibitors of the cAMP-dependent protein kinase [Scott, J. D., Fischer, E. H., Demaille, J. G. & Krebs, E. G. (1985) Proc. Natl. Acad. Sci. USA 82, 4379-4383]. Residues 14-22 show considerable homology to the "hinge-regions" of the regulatory subunits of the cAMP-dependent protein kinase. The remainder of the molecule shows no similarity to the known amino acid sequence of any protein.
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PMID:Amino acid sequence of the heat-stable inhibitor of the cAMP-dependent protein kinase from rabbit skeletal muscle. 389 70

Tryptophan has been demonstrated earlier to induce in the livers of rats and mice a rapid stimulation of polyribosomal aggregation and protein synthesis which has been attributed in part to stimulation of translocation of nuclear mRNA into the cytoplasm. This study was concerned with how tryptophan acts to affect the nuclei, particularly the nuclear membranes, in enhancing the nucleocytoplasmic translocation of mRNA of liver cells of rats fasted overnight. The results reveal that tryptophan rapidly becomes incorporated into proteins and also binds to proteins of hepatic cells, particularly proteins of the nuclear envelopes. In vitro binding of 3H-tryptophan to proteins (trichloroacetic-acid-precipitable) of nuclei and cytosols (when incubated together or separately) of livers of tryptophan-treated (10 minutes) rats is increased in comparison with binding to components of control rats. These findings correlate with the enhanced in vitro release of nuclear RNA and the increased activities of nuclear NTPase and protein phosphokinase of the livers of the experimental rats. Preincubation of hepatic nuclei with concanavalin A prevented the increases in in vitro binding of 3H-tryptophan to nuclear proteins, in prelabeled nuclear RNA release, and in nuclear NTPase activity of livers of the tryptophan-treated rats. The results suggest that tryptophan rapidly binds with hepatic proteins (possibly glycoproteins) associated with the nuclear membrane, leading to an increase in the activities of enzymes involved in phosphorylation and dephosphorylation and in release of nuclear mRNA into the cytoplasm.
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PMID:Nutritional control of protein synthesis. Studies relating to tryptophan-induced stimulation of nucleocytoplasmic translocation of mRNA in rat liver. 609 45

Type I cyclic AMP (cAMP)-dependent protein kinase is composed of a dimeric regulatory subunit (R(2)) and two catalytic subunits (C subunits). The R(2) dimer binds four cAMP molecules to release the two C subunits. To characterize the cAMP binding sites and elucidate their role in the release of the C subunits, the R(2) dimer has been studied by equilibrium methods. The cAMP titration of R(2) was monitored by endogenous tryptophan fluorescence, and the results suggest one class of binding sites. The titration plot is monotonic for saturation of four sites per R(2). A similar titration monitored by near-UV circular dichroic changes exhibited profound changes in the region of the (1)L(b) tyrosine and (1)L(a) and (1)L(b) tryptophan transitions; a plot of these data also showed a linear monotonic response. Thus, the fluorescence and circular dichroic changes show that cAMP binding to R(2) induces a conformational or structural change. The one apparent class of binding sites implies that all binding sites are characterized by similar K(d) values or by K(d) values much less than the receptor concentration. The reactivity of the cysteine sulfhydryl groups with 5,5'-dithiobis(2-nitrobenzoic acid) showed that saturation with cAMP indirectly protects one sulfhydryl group per R monomer. Analysis of cAMP activation of the holoenzyme, detected by phosphotransferase assays, showed that saturation of both cAMP binding sites per R monomer is necessary to effect the release of the C subunit. By using a fluorescent analog of cAMP, 1,N(6)-etheno-cyclic AMP (epsilon cAMP), the (epsilon cAMP)(4).R(2) complex was titrated with C subunit, causing the release of epsilon cAMP. The titration showed that the release of epsilon cAMP was a positive cooperative process; its Hill plot had a slope of 2.6 and the K(a1) and K(an) values obtained by extrapolation were 2.1 x 10(7) M(-1) and 5.0 x 10(8) M(-1), respectively. The calculated DeltaDeltaG for first and last site coupling was 1.9 kcal/mol (1 cal = 4.18 J) of holoenzyme.
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PMID:Cyclic AMP-dependent protein kinase I: cyclic nucleotide binding, structural changes, and release of the catalytic subunits. 626 17

It has been demonstrated earlier that the administration of tryptophan to fasted animals increased the levels of mRNA in the cytoplasm of the liver by stimulating the translocation of nuclear poly(A)-mRNA into the cytoplasm. Also, tryptophan increased the activity of hepatic nuclear envelope (NE) nucleoside triphosphatase, an enzyme considered to be involved in nucleocytoplasmic translocation of mRNA. In this study, the activities of two other NE-associated enzymes, protein phosphokinase and phosphoprotein phosphohydrolase, also implicated in nuclear RNA transport, were investigated in the livers of rats that received a single tube feeding of tryptophan. The administration of tryptophan to fasted rats 10 minutes before killing increased the hepatic NE activities of both enzymes, protein phosphokinase and phosphoprotein phosphohydrolase. Furthermore, tryptophan administration increased the in vivo incorporation of 3H-leucine into NE proteins (+83%) and into other subcellular fractions (+34 to +43%) of the liver compared with that into corresponding fractions of the control rats. Rats that received 3H-leucine to prelabel hepatic proteins and then were treated with puromycin to inhibit further protein synthesis followed by tube feeding of tryptophan revealed greater radioactivity associated with NE proteins than that in controls. These findings suggest that tryptophan may act to stimulate the transport or availability of proteins to the vicinity of the NE, possibly specific regulatory proteins, such as nucleoside triphosphatase, protein phosphokinase and phosphoprotein phosphohydrolase, which show an increase in activity and may then be responsible for the increase in the rate of nucleocytoplasmic translocation of mRNA.
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PMID:Effect of tryptophan on enzymes and proteins of hepatic nuclear envelopes of rats. 682 5

The brain tryptophan hydroxylase is known to be activated by magnesium adenosine triphosphate (MgATP). This activation has been suspected to be a case of enzyme phosphorylation, although convincing evidence is still lacking. In supernatants (100,000 g) from adult mouse midbrains, the addition of 1 mM ATP and 10 mM MgCl2 could increase the tryptophan activity by 70-90%, when the enzyme activity was determined at a subsaturating concentration of 6-MPH4 (0.2 mM). The present study has revealed that the enzyme activation by MgATP could only be achieved from mice after 12 days of postnatal age. No activation was found in midbrain preparations from younger animals, although a substantial level of tryptophan hydroxylase activity was already present. The possibility that some required component(s) for the enzyme activation may be lacking during early development was tested by mixing a dialyzed adult preparation with the neonatal midbrain supernatant. Under these conditions, the tryptophan hydroxylase in the neonatal supernatant was activated by MgATP. Furthermore, the addition of a crude protein kinase fraction from adult midbrain cytosol was also capable of restoring the enzyme activatability in the neonatal preparation. It appears that the lack of activatability by MgATP alone during early development was due to absence of one or more biochemical factors required for the activation.
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PMID:Activation of midbrain tryptophan hydroxylase by MgATP. Absence during early postnatal development. 698 83

Developmental increase of tryptophan oxygenase (L-tryptophan: oxygen 2, 3-oxidoreductase (decyclizing), EC 1.13.11.11) was studied using hepatocytes of neonatal rats in primary culture. Hepatocytes from rats of 2-30-days-old were isolated and cultured for 2 days. In cultured hepatocytes of 2-day-old rats, tryptophan (2.5 mM), dexamethasone (1 x 10(-5) M) and glucagon (1 x 10(-7) M) did not cause the appearance of tryptophan oxygenase. But the enzyme activity became detectable, when hepatocytes from 5-day-old rats were incubated with tryptophan, the oxygenase could be induced precociously by dexamethasone, but by glucagon. The effect of glucagon was first seen 2 weeks after birth. However, in hepatocytes of 9-day-old rats glucagon stimulated formation of cyclic AMP and protein kinase activity (EC 2.7.1.37) and also induced tyrosine aminotransferase (EC 2.6.1.5). When hepatocytes of 9-day-old rats were cultured for 4 days, their tryptophan oxygenase became inducible by glucagon. Insulin almost completely inhibited precocious appearance of the enzyme activity evoked by tryptophan plus dexamethasone in hepatocytes of 9-day-old rats. These studies suggest that the appearance of tryptophan oxygenase in rat liver during development is due to first the onset of gene coding for tryptophan oxygenase and then stimulation by the sequential actions of glucocorticoid and glucagon.
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PMID:Hormonal control of the development of tryptophan oxygenase in primary cultures of young rat hepatocytes. 730 79


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