Takeuchi T et al. (2011) Biol Pharm Bull "-galactosidases from jack bean and Streptococcus have different cleaving abilities towards fucose-containing sugars."

Kasai K, Natsuka S, Takeuchi T, Arata Y, Sugiura K, Nishiyama K, Takahashi H, Natsugari H

[Biol Pharm Bull, 2011]

We examined the sugar-cleaving abilities of -galactosidases from jack bean and Streptococcus towards sugars containing fucose residues, and found that jack bean -galactosidase has an ability to cleave the 1-3 linkage between galactose (Gal) and fucose (Fuc) residues, but not 1-4 linkage. On the other hand, streptococcal -galactosidase was found to cleave the linkage in both Gal1-4Fuc and Gal1-3Fuc disaccharide units. Such a difference in sugar-cleaving abilities between these 2 -galactosidases will be useful for structural analysis of glycans, especially those from species belonging to Protostomia, such as Caenorhabditis elegans.

Wexler M et al. (2000) J Biol Chem "TatD is a cytoplasmic protein with DNase activity. No requirement for TatD family proteins in sec-independent protein export."

Stanley NR, Robinson C, Jack RL, Wexler M, Sargent F, Palmer T, Bogsch EG, Berks BC

[J Biol Chem, 2000]

The Escherichia coli Tat system mediates Sec-independent export of protein precursors bearing twin arginine signal peptides. Genes known to be involved in this process include tatA, tatB, and tatC that form an operon with a fourth gene, tatD. The tatD gene product has two homologues in E. coli coded by the unlinked ycfH and yjjV genes. An E. coli strain with in-frame chromosomal deletions in all three of tatD, ycfH, and yjjV exhibits no significant defect in the cellular location of five cofactor-containing enzymes that are synthesized with twin arginine signal peptides. Neither these mutations nor overproduction of the TatD protein cause any discernible effect on the export kinetics of an additional E. coli Tat pathway substrate. It is concluded that proteins of the TatD family have no obligate involvement in protein export by the Tat system. TatD is shown to be a cytoplasmic protein. TatD binds to immobilized Ni(2+) or Zn(2+) affinity columns and exhibits magnesium-dependent DNase activity. Features of the tatA operon that may control TatD expression are discussed.

Dosoky NS et al. (2016) Medicines (Basel) "Composition and Biological Activities of Murraya paniculata (L.) Jack Essential Oil from Nepal."

Satyal P, Setzer WN, Gautam TP, Dosoky NS

[Medicines (Basel), 2016]

Murraya paniculata (L.) Jack, a small tropical evergreen shrub growing in Nepal, has numerous uses in traditional medicine for treatment of abdominal pain, diarrhea, stomach ache, headache, edema, thrombosis, and blood stasis. The present study investigated the chemical composition and bioactivities of the leaf essential oil from M. paniculata from Nepal. The essential oil from leaves was obtained by hydrodistillation and a detailed chemical analysis was conducted by gas chromatography-mass spectrometry (GC-MS). The essential oil was screened for antimicrobial activity using the microbroth dilution test, for nematicidal activity against Caenorhabditis elegans, and for lethality against brine shrimp (Artemia salina). A total of 76 volatile components were identified from the essential oil. The major components were methyl palmitate (11.1%), isospathulenol (9.4%), (E,E)-geranyl linalool (5.3%), benzyl benzoate (4.2%), selin-6-en-4-ol (4.0%), -caryophyllene (4.0%), germacrene B (3.6%), germacrene D (3.4%), and -elemene (3.2%). The essential oil showed no antibacterial activity, marginal antifungal activity against Aspergillus niger (MIC = 313 g/mL), a moderate activity against A. salina (LC50 = 41 g/mL), and a good nematicidal activity against C. elegans (LC50 = 37 g/mL).