In the title compound, C(19)H(17)N(2)O(2)P, the six-membered 1,3,2-oxaza-phosphinine ring adopts a boat conformation with the phosphoryl O atom in an equatorial position. The dihedral angle between the 6-methyl-2-pyridyl and phenyl groups is 75.5 (1)°. These substituents are trans to each other, and are oriented at angles of 57.2 (1) and 74.8 (1)°, respectively, to the benzene ring. The crystal...

In the mol-ecular structure of the title compound, [CaNa(C10H20Cl3N3O2P)3(H2O)], the Ca2+ ion has a slightly distorted octa-hedral coordination environment defined by six O atoms which belong to the carbonyl and phosphoryl groups of the three coordinating ligands. Two Cl atoms of CCl3 groups and four O atoms form the coordination environment of the Na+ ion: three from the carbonyl groups of lig...

Glycogen phosphorylase has been isolated from rabbit muscle in two different molecular forms, phosphorylase a, a tetramer with a molecular weight of 495,000 (2-4), and phosphorylase b, a dimer with a molecular weight of 242,000 (3-5). The dimerization of the protein that occurs in the conversion of phosphorylase 6 to a with phosphorylase kinase, Mg++, and ATP has been found to result from the i...

We have probed the electrostatic environment of the active site of the Tetrahymena group I ribozyme (E) using protonated 2'-aminoguanosine (), in which the 2'-OH of the guanosine nucleophile (G) is replaced by an group. At low concentrations of divalent metal ion (2 mM Mg(2+)), binds at least 200-fold stronger than G or G(NH)()2, with a dissociation constant of </=1 microM from the ribozyme. ol...

The active site of the cAMP-dependent protein kinase catalytic subunit harbors a cluster of acidic residues-Asp 127, Glu 170, Glu 203, Glu 230, and Asp 241-that are not conserved throughout the protein kinase family. Based on crystal structures of the catalytic subunit, these amino acids are removed from the site of phosphoryl transfer and are implicated in substrate recognition. Glu 230, the m...

Activated Lactococcus lactis beta-phosphoglucomutase (betaPGM) catalyzes the conversion of beta-d-glucose 1-phosphate (betaG1P) derived from maltose to beta-d-glucose 6-phosphate (G6P). Activation requires Mg(2+) binding and phosphorylation of the active site residue Asp8. Initial velocity techniques were used to define the steady-state kinetic constants k(cat) = 177 +/- 9 s(-)(1), K(m) = 49 +/...

We have previously shown that the lipooligosaccharide (LOS) from Neisseria meningitidis and N. gonorrhoeae engages the TLR4-MD-2 complex. In this study, we report that LOS from different meningococcal and gonococcal strains have different potencies to activate NF-κB through TLR4-MD-2 and that the relative activation can be correlated with ion abundances in MALDI-TOF mass spectrometry that are i...