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provides coniferyl ferulate(CAS#:2651-15-2) MSDS, density, melting point, boiling point, structure, formula, molecular weight etc. Articles of coniferyl ferulate are included as well.>> amp version: coniferyl ferulate
Pyridoxal-5′-phosphate or PLP, the active form of vitamin B6, is a highly versatile cofactor that participates in a large number of mechanistically diverse enzymatic reactions in basic metabolism. PLP-dependent enzymes account for ∼1.5% of most prokaryotic genomes and are estimated to be involved in ∼4% of all catalytic reactions, making this an important class of enzymes. Here, we structurally and functionally characterize three novel PLP-dependent enzymes from bacteria in the human microbiome: two are from Eubacterium rectale, a dominant, nonpathogenic, fecal, Gram-positive bacteria, and the third is from Porphyromonas gingivalis, which plays a major role in human periodontal disease. All adopt the Type I PLP-dependent enzyme fold and structure-guided biochemical analysis enabled functional assignments as tryptophan, aromatic, and probable phosphoserine aminotransferases.
human microbiome, PLP-dependent enzymes, crystal structure, biochemical characterization, structural genomics, Protein Structure Initiative
Molecular characterization of novel pyridoxal-5′-phosphate-dependent enzymes from the human microbiome
Nicholas M Fleischman,1 Debanu Das,2,3 Abhinav Kumar,2,3 Qingping Xu,2,3 Hsiu-Ju Chiu,2,3 Lukasz Jaroszewski,2,4,5 Mark W Knuth,2,6 Heath E Klock,2,6 Mitchell D Miller,2,3 Marc-Andre Elsliger,2,7 Adam Godzik,2,4,5 Scott A Lesley,2,6,7 Ashley M Deacon,2,3 Ian A Wilson,2,7,* and Michael D Toney1
The reovirus cell attachment protein, sigma1, is a trimer with a ‘lollipop’ structure. Recent findings indicate that the N-terminal fibrous tail and the C-terminal globular head each possess a distinct trimerization domain. The region responsible for N-terminal trimerization (formation of a triple alpha-helical coiled-coil) is located at the N-terminal one-third of sigma1. In this study, we investigated the temporality and ATP requirement of this trimerization event in the context of sigma1 biogenesis. In vitro co-synthesis of the full-length (FL) and a C-terminally truncated (d44) sigma1 protein revealed a preference for homotrimer over heterotrimer formation, suggesting that assembly at the N-terminus occurs co-translationally. This was corroborated by the observation that polysome-associated sigma1 chains were trimeric as well as monomeric. Truncated proteins (d234 and d294) with C-terminal deletions exceeding half the length of sigma1 were found to trimerize post-translationally. This trimerization did not require ATP since it proceeded normally in the presence of apyrase. In contrast, formation of stable FL sigma1 trimers was inhibited by apyrase treatment. Collectively, our data suggest that assembly of nascent sigma1 chains at the N-terminus is intrinsically ATP independent, and occurs co-translationally when the ribosomes have traversed past the midpoint of the mRNA.
Co-translational trimerization of the reovirus cell attachment protein.
R Gilmore, M C Coffey, G Leone, K McLure, and P W Lee
1996 Jun 3;
β-Adrenergic receptors (β-ARs) enhance cardiac contractility by increasing cAMP levels and activating PKA. PKA increases Ca2+-induced Ca2+ release via phosphorylation of L-type Ca2+ channels (LTCCs) and ryanodine receptor 2. Multiple cyclic nucleotide phosphodiesterases (PDEs) regulate local cAMP concentration in cardiomyocytes, with PDE4 being predominant for the control of β-AR-dependent cAMP signals. Three genes encoding PDE4 are expressed in mouse heart: Pde4a, Pde4b, and Pde4d. Here we show that both PDE4B and PDE4D are tethered to the LTCC in the mouse heart but that β-AR stimulation of the L-type Ca2+ current (ICa,L) is increased only in Pde4b-/- mice. A fraction of PDE4B colocalized with the LTCC along T-tubules in the mouse heart. Under β-AR stimulation, Ca2+ transients, cell contraction, and spontaneous Ca2+ release events were increased in Pde4b-/- and Pde4d-/- myocytes compared with those in WT myocytes. In vivo, after intraperitoneal injection of isoprenaline, catheter-mediated burst pacing triggered ventricular tachycardia in Pde4b-/- mice but not in WT mice. These results identify PDE4B in the CaV1.2 complex as a critical regulator of ICa,L during β-AR stimulation and suggest that distinct PDE4 subtypes are important for normal regulation of Ca2+-induced Ca2+ release in cardiomyocytes.
Phosphodiesterase 4B in the cardiac L-type Ca2+ channel complex regulates Ca2+ current and protects against ventricular arrhythmias in mice
Jerôme Leroy,1,2 Wito Richter,3 Delphine Mika,1,2 Liliana R.V. Castro,1,2 Aniella Abi-Gerges,1,2 Moses Xie,3 Colleen Scheitrum,3 Florence Lefebvre,1,2 Julia Schittl,1,2 Philippe Mateo,1,2 Ruth Westenbroek,4 William A. Catterall,4 Flavien Charpentier,5,6 Marco Conti,3 Rodolphe Fischmeister,1,2 and Gregoire Vandecasteele1,2
2011 Jul 1;