Structural changes and interactions involved in the Ca(super.2+)-triggered stabilization of the cell-bound cell envelope proteinase in Lactococcus lactis subsp. cremoris SK11

Article Abstract:

Structural changes and interactions that are part of the Ca(super.2+)-triggered stabilization of the cell envelope proteinase (CEP) that is cell-bound in the cheese starter Lactococcus lactis subsp. cremoris SK11 are discussed. It appears that in the Ca-free CEP the absence of local calcium-mediated backbone rigidity and neutralization of negative electrostatic potentials in the weak Ca-binding sites increase the relative effectiveness of electrostatic repulsion forces on the protein enough to cause the instability that is seen. The lack of significant hydrophobic stabilization also has a role. The proteinase is the only extracellular cell surface proteinase of the organism and is required for normal growth in milk.

Netherlands

---

Purification and characterization of cystathionine beta-lyase from Lactococcus lactis subsp. cremoris B78 and its possible role in flavor development in cheese

Article Abstract:

An enzyme isolated from Lactococcus lactis subspecies cremoris B78 resembles Cystathionine beta-lyase and breaks down sulfur-containing amino acids. This enzyme is probably involved in inducing flavor in cheese. The enzyme of 130 to 165 kilo dalton comprises four identical subunits. It catalyzes alpha,gamma-elimination reactions producing methanethiol from methionine which gives origin to the flavor compounds in cheese.

Bacteria, Microbial enzymes, Amino acid metabolism

---

Mitochondrial function in cell wall blycoprotein synthesis in Saccharomyces cerevisiae NCYC 625 (wild type) and (rho(super.0)) mutants

Article Abstract:

Mitochondrial function in cell wall glycoprotein synthesis in Saccharomyces cerevisiae NCYC 625 (wild type) and (rho(super.0)) mutants has been studied. Phosphopeptidomannans (PPMs) were studied. The aerobic wild-type cultures were very flocculent. All others were weaky flocculent. Ligands implicated in flocculation of mutants or antimycin-treated cells were not aggregated as much by concanavalin A as those of the wild type. Alterations of PPM structures may be responsible for reduced flocculation of cells grown in certain conditions.

United States, France, Hungary, Statistical Data Included, Usage, Microbiology, Lectins, Mitochondria, Saccharomyces, Cellular control mechanisms, Cell regulation, Cellular recognition, Lectin structure-activity relationships

Similar abstracts:

• Abstracts: Cloning and sequence analysis of putative histidine protein kinases isolated from Lactococcus lactis MG1363. Six putative two-component regulatory systems isolated from Lactococcus lactis subsp. cremoris MG1363
• Abstracts: Affinity purification and characterization of a fibrinogen-binding protein complex which protects mice against lethal challenge with streptococcus equi subsp. equi
• Abstracts: Structure and mechanism of yeast RNA triphosphatase: an essential component of the mRNA capping apparatus. Structural organization of the RNA polymerase-promoter open complex
• Abstracts: Lateral signaling mediated by axon contact and calcium entry regulates asymmetric odorant receptor expression in C. elegans
• Abstracts: Weakening effect of cell pearmeabilizers on gram-negative bacteria causing biodeterioration. Lactic acid permeabilizes gram-negative bacteria by disrupting the outer membrane

This website is not affiliated with document authors or copyright owners. This page is provided for informational purposes only. Unintentional errors are possible.