Results 1 to 10 of about 32,792 (197)

Dimer-monomer transition defines a hyper-thermostable peptidoglycan hydrolase mined from bacterial proteome by lysin-derived antimicrobial peptide-primed screening [PDF]

open access: greeneLife
Phage-derived peptidoglycan hydrolases (i.e. lysins) are considered promising alternatives to conventional antibiotics due to their direct peptidoglycan degradation activity and low risk of resistance development.
Li Zhang   +11 more
doaj   +6 more sources

INHIBITION AND ACTIVATION OF BARLEY PEPTIDE HYDROLASES I. PEPTIDE HYDROLASE A [PDF]

open access: bronzeJournal of the Institute of Brewing, 1971
Barley peptide hydrolase A acting on N-benzoyl-dl-arginine-p-nitroanilide as substrate is inhibited by the sulphydryl reagents N-ethyl maleimide and p-chloro-mercuriphenyl sulphonate. Oxidized glutathione, however, is non-inhibitory and several sulphydryl compounds are not stimulatory.
W. C. Burger   +2 more
openalex   +3 more sources

The Peptide Hydrolase System of the Leuconostoc

open access: bronzeJournal of Food Protection, 1990
The intracellular peptide hydrolase activities of Leuconostoc species were determined using various aminopeptidase, dipeptidase, carboxypeptidase substrates, and casein. The activities were separated by disc gel electrophoresis. All strains had aminopeptidase activity as determined with amino acid ß-napthylamides and dipeptidase.
H. El‐Shafei, M. El‐Soda, N. Ezzat
openalex   +4 more sources

Histidine-Triad Hydrolases Provide Resistance to Peptide-Nucleotide Antibiotics [PDF]

open access: yesmBio, 2020
The Escherichia coli microcin C (McC) and related compounds are potent Trojan horse peptide-nucleotide antibiotics. The peptide part facilitates transport into sensitive cells.
Eldar Yagmurov   +7 more
doaj   +5 more sources

Reassessing the substrate specificities of the major Staphylococcus aureus peptidoglycan hydrolases lysostaphin and LytM [PDF]

open access: yeseLife
Orchestrated action of peptidoglycan (PG) synthetases and hydrolases is vital for bacterial growth and viability. Although the function of several PG synthetases and hydrolases is well understood, the function, regulation, and mechanism of action of PG ...
Lina Antenucci   +6 more
doaj   +2 more sources

Specificity determinants of acylaminoacyl‐peptide hydrolase [PDF]

open access: greenProtein Science, 1992
AbstractIn an attempt to explore how specific features of the substrate's primary structure may affect the activity of rabbit muscle acylaminoacyl‐peptide hydrolase (EC 3.4.19.1), a number of acetylated peptides containing specific amino acid replacements in specific positions were prepared and compared as substrates for the hydrolase.
Radha Krishna, Finn Wold
openalex   +5 more sources

Peptide hydrolase activities of the mucosa of human small intestine [PDF]

open access: bronzeJournal of Clinical Investigation, 1969
Few studies have been published on peptide hydrolase activities of human small intestine mucosa. We developed methods to screen tissue extracts for such enzymes and to quantitate hydrolase activities for dipeptides containing the aromatic amino acid L-phenylalanine.
William D. Heizer, Leonard Laster
openalex   +4 more sources

Acyl peptide hydrolase degrades monomeric and oligomeric amyloid-beta peptide [PDF]

open access: goldMolecular Neurodegeneration, 2009
Abstract Background The abnormal accumulation of amyloid-beta peptide is believed to cause malfunctioning of neurons in the Alzheimer's disease brain. Amyloid-beta exists in different assembly forms in the aging mammalian brain including monomers, oligomers, and aggregates, and in senile plaques, fibrils.
Rina Yamin   +4 more
openalex   +7 more sources

Peptide hydrolases ofBrevibacterium linens [PDF]

open access: bronzeFEMS Microbiology Letters, 1978
Helge Torgersen, Terje SÃ ̧rhaug
  +5 more sources

Aspartic Peptide Hydrolases in Salmonella enterica Serovar Typhimurium [PDF]

open access: bronzeJournal of Bacteriology, 2001
ABSTRACT Two well-characterized enzymes in Salmonella enterica serovar Typhimurium and Escherichia coli are able to hydrolyze N-terminal aspartyl (Asp) dipeptides: peptidase B, a broad-specificity aminopeptidase, and peptidase E, an Asp-specific dipeptidase.
Rachel A. Larsen   +2 more
openalex   +4 more sources

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