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CreatorTitleDescriptionSubjectDate
1 Blumenthal, Donald K.Characterization of the calmodulin-binding and catalytic domains in skeletal muscle myosin light chain kinase.Limited proteolysis has been utilized to study the structural organization of rabbit skeletal muscle myosin light chain kinase. The enzyme (Mr approximately 89,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis) consists of an amino-terminal, protease-susceptible region of unidentified...Enzymology; Skeletal Muscle; Proteolysis, Peptide Fragments1995-09-15
2 Blumenthal, Donald K.Characterization of the phosphotyrosyl protein phosphatase activity of calmodulin-dependent protein phosphatase.Calmodulin-dependent protein phosphatase from bovine brain and heart was assayed for phosphotyrosine and phosphoserine phosphatase activity using several substrates: 1) smooth muscle myosin light chain (LC20) phosphorylated on tyrosine or serine residues, 2) angiotensin I phosphorylated on tyrosine,...Metabolism; Phosphatase Activity1986-07-25
3 Blumenthal, Donald K.Characterization of the regulatory domain of the gamma-subunit of phosphorylase kinase. The two noncontiguous calmodulin-binding subdomains are also autoinhibitory.Phosphorylase kinase is a multimeric protein kinase (alpha 4 beta 4 gamma 4 delta 4) whose enzymatic activity is conferred by its gamma-subunit. A library of 18 overlapping synthetic peptides spanning residues 277-386 of the gamma-subunit has been prepared to use in identifying important regulatory ...Metabolism; Phosphorylase Kinase1995-09-22
4 Blumenthal, Donald K.; Trewhella, JillConformationally dynamic C helix of the RIalpha subunit of protein kinase A mediates isoform-specific domain reorganization upon C subunit binding.Different isoforms of the full-length protein kinase A (PKA) regulatory subunit homodimer (R2) and the catalytic (C) subunit-bound holoenzyme (R2C2) have very different global structures despite similar molecular weights and domain organization within their primary sequences. To date, it has been th...Protein Isoforms; Global Structures; cAMP2005-10-21
5 Blumenthal, Donald K.Dephosphorylation of cAMP-dependent protein kinase regulatory subunit (type II) by calmodulin-dependent protein phosphatase. Determinants of substrate specificity.Calmodulin-dependent protein phosphatase purified from bovine cardiac muscle catalyzed the rapid dephosphorylation of Ser-95 of bovine cardiac cAMP-dependent protein kinase regulatory subunit (RII). The kinetic constants determined for the reaction (Km = 20 microM; Vmax = 2 mumol min-1 mg-1) are com...Metabolism; High Pressure Liquid; Enzymology1985-06-25
6 Blumenthal, Donald K.Effects of deletions in the central helix of calmodulin on enzyme activation and peptide binding.Using site-directed mutagenesis we have expressed in Escherichia coli three engineered calmodulins (CaM) containing deletions in the solvent-exposed region of the central helix. These are CaM delta 84, Glu-84 removed; CaM delta 83-84, Glu-83 and Glu-84 removed; and CaM delta 81-84, Ser-81 through Gl...Drug Effects; Genetics; Metabolism1989-05-15
7 Hendee, Shonn P.; Faour, Fouad A.; Christensen, Douglas A.; Patrick, Baharah; Durney, Carl H.; Blumenthal, Donald K.Effects of weak extremely low frequency magnetic fields on calcium/calmodulin interactions.Mechanisms by which weak electromagnetic fields may affect biological systems are of current interest because of their potential health effects. Lednev has proposed an ion parametric resonance hypothesis (Lednev, 1991, Bioelectromagnetics, 12:71-75), which predicts that when the ac, frequency of a c...Electromagnetic Fields; Calcium-binding Proteins; Lednev's Theory1996-06
8 Blumenthal, Donald K.Gamma-subunit of skeletal muscle phosphorylase kinase contains two noncontiguous domains that act in concert to bind calmodulin.Phosphorylase kinase is a Ca2+-regulated, multisubunit enzyme that contains calmodulin as an integral subunit (termed the delta-subunit). Ca2+-dependent activity of the enzyme is thought to be regulated by direct interaction of the delta-subunit with the catalytic subunit (the gamma-subunit) in the ...Pharmacology; Metabolism; Enzymology1989-10-15
9 Blumenthal, Donald K.Identification of the calmodulin-binding domain of skeletal muscle myosin lightIn 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 inhibit...Peptides; Enzymes; Protein sequence1985-05
10 Blumenthal, Donald K.Identification of the substrate and pseudosubstrate binding sites of phosphorylase kinase gamma-subunit.Using site-directed mutagenesis, we proposed that an autoinhibitory domain(s) is located at the C-terminal region (301-386) of the phosphorylase kinase gamma-subunit (Huang, C.-Y.F., Yuan C.-J., Livanova, N.B., and Graves, D.J. (1993) Mol. Cell. Biochem. 127/128, 7-18). Removal of the putative inhib...Mutagenesis; Autoinhibitory Domain; Peptides1995-03-31
11 Blumenthal, Donald K.Phosphorylation of cardiac troponin by guanosine 3':5'-monophosphate-dependent protein kinase.Homogeneous cGMP-dependent protein kinase catalyzes the rapid incorporation of phosphate, specifically into the inhibitory subunit of purified cardiac troponin with a maximal incorporation of 1 mol of phosphate/mol of troponin. When troponin was incubated in the presence of both cGMP- and cAMP-depen...Protein Kinases1978-01-25
12 Baehr, Wolfgang; Prestwich, Glenn D.Photoreceptor cGMP phosphodiesterase delta subunit (PDEdelta) functions as a prenyl-binding proteinBovine PDEdelta was originally copurified with rod cGMP phosphodiesterase (PDE) and shown to interact with prenylated, carboxymethylated C-terminal Cys residues. Other studies showed that PDEdelta can interact with several small GTPases including Rab13, Ras, Rap, and Rho6, all of which are prenylate...Fluorescence Resonance Energy Transfer; GTP Phosphohydrolases; Immunohistochemistry2004
13 Poulter, Charles DalePrenyltransferase. Kinetic studies of the 1'-4 coupling reaction with avian liver enzyme.Prenyltransferase catalyzes the sequential, irreversible 1'-4 condensation of isopentenyl-PP with dimethylallyl-PP and geranyl-PP to yield farnesyl-PP. A kinetic study shows substrate inhibition by isopentenyl-PP at concentrations above 0.7 microM when the concentration of geranyl-PP is 1.0 microM o...Birds; Kinetics; Structure-Activity Relationship; Substrate Specificity1979-10-10
14 Blumenthal, Donald K.Rabbit skeletal muscle myosin light chain kinase. The calmodulin binding domain as a potential active site-directed inhibitory domain.A synthetic peptide modeled after the calmodulin (CaM)-binding domain of rabbit skeletal muscle myosin light chain kinase, Lys-Arg-Arg-Trp-Lys5-Lys-Asn-Phe-Ile-Ala10-Val-Ser-Ala-Ala-+ ++Asn15-Arg-Phe-Glycyl amide (M5), inhibited the CaM-independent chymotryptic fragment of the enzyme, C35 (Edelman, ...Synthetic Peptide1987-09-05
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