| characterization of poly-gamma-glutamate hydrolase encoded by a bacteriophage genome: possible role in phage infection of bacillus subtilis encapsulated with poly-gamma-glutamate. | some bacillus subtilis strains, including natto (fermented soybeans) starter strains, produce a capsular polypeptide of glutamate with a gamma-linkage, called poly-gamma-glutamate (gamma-pga). we identified and purified a monomeric 25-kda degradation enzyme for gamma-pga (designated gamma-pga hydrolase, pghp) from bacteriophage phinit1 in b. subtilis host cells. the monomeric pghp internally hydrolyzed gamma-pga to oligopeptides, which were then specifically converted to tri-, tetra-, and penta- ... | 2003 | 12732513 |
| poly-gamma-glutamate capsule-degrading enzyme treatment enhances phagocytosis and killing of encapsulated bacillus anthracis. | the poly-gamma-d-glutamic acid capsule confers antiphagocytic properties on bacillus anthracis and is essential for virulence. in this study, we showed that capd, a gamma-polyglutamic acid depolymerase encoded on the b. anthracis capsule plasmid, degraded purified capsule and removed the capsule from the surface of anthrax bacilli. treatment with capd induced macrophage phagocytosis of encapsulated b. anthracis and enabled human neutrophils to kill encapsulated organisms. a second glutamylase, p ... | 2007 | 17074794 |
| crystallization and preliminary crystallographic analysis of poly-gamma-glutamate hydrolase from bacteriophage phinit1. | particular bacillus subtilis strains produce a capsular polypeptide poly-gamma-glutamate (gamma-pga) that functions as a physical barrier against bacteriophage infection. bacteriophage phinit1 can infect b. subtilis and produces a novel gamma-pga hydrolase pghp. pghp was overexpressed, purified and crystallized by the sitting-drop vapour-diffusion method. the crystals diffracted to a resolution of 2.4 a using a synchrotron x-ray source and were found to belong to space group p3(1)21 or p3(2)21. | 2009 | 19724131 |
| crystal structure of bacteriophage ϕnit1 zinc peptidase pghp that hydrolyzes γ-glutamyl linkage of bacterial poly-γ-glutamate. | poly-γ-glutamate hydrolase p (pghp) of bacillus subtilis bacteriophage φnit1 hydrolyzes the γ-glutamyl peptide linkage of extracellular poly-γ-glutamate produced by bacilli, which facilitates infection and propagation of phage progenies. crystal structure of pghp was determined at a resolution of 1.9 å. structure of pghp was elucidated as a globular protein with an open α/β mixed core structure and a seven-stranded parallel/anti-parallel β-sheet. the β-sheet contained a core four-stranded parall ... | 2011 | 22105902 |