Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.21.4 (trypsin)
 42,187 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A protein in the cell wall of Fusobacterium nucleatum Fev1 remained associated with the peptidoglycan during extraction with various detergents and organic solvents. On digestion of this peptidoglycan-protein complex (PPC) with murein hydrolases, sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) showed polypeptide bands with apparent molecular weights (MWs) in the range of 3000 to 40,000. After reaction with maleic anhydride the electrophoretic mobilities of these polypeptide bands increased to those of MWs 3000 to 12,000. The PPC protein showed a limited susceptibility toward trypsin, giving polypeptides that migrated in SDS-PAGE as a diffuse band with MW in the range of 3000 to 6000. The amino acid composition of all polypeptide bands eluted from SDS-PAGE was very similar, whichever enzyme was used for the solubilization of the PPC, and was nearly identical to that found for the protein moiety of the PPC. On the basis of a MW of 3000 for a protein unit, about one molecule of protein was found per five peptidoglycan subunits. Lanthionine was not found associated with released polypeptide, and muramic acid and glucosamine were either absent or present in amounts less than one molecule per protein unit. The PPC was immunogenic in rabbits, and purified anti-PPC IgG reacted with murein hydrolase-released protein separated on SDS-PAGE but preferentially with bands of MWs greater than 18,000.
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PMID:Partial characterization of a peptidoglycan-protein complex from Fusobacterium nucleatum Fev1. 288 84

When colonizing the digestive tract of mono-associated rats, Ruminococcus gnavus E1 - a bacterium isolated from human faeces - produced a trypsin-dependent anti-Clostridium perfringens substance collectively named Ruminococcin C (RumC). RumC was isolated from the caecal contents of E1-monocontaminated rats and found to consist of two antimicrobial fractions: a single peptide (RumCsp) of 4235 Da, and a mixture of two other peptides (RumCdp) with distinct molecular masses of 4324 Da and 4456 Da. Both RumCsp and RumCdp were as effective as metronidazole in combating C. perfringens and their activity spectra against different pathogens were established. Even if devoid of synergistic activity, the combination of RumCsp and RumCdp was observed to be much more resistant to acidic pH and high temperature than each fraction tested individually. N-terminal sequence analysis showed that the primary structures of these three peptides shared a high degree of homology, but were clearly distinct from previously reported amino acid sequences. Amino acid composition of the three RumC peptides did not highlight the presence of any Lanthionine residue. However, Edman degradation could not run beyond the 11th amino acid residue. Five genes encoding putative pre-RumC-like peptides were identified in the genome of strain E1, confirming that RumC was a bacteriocin. This is the first time that a bacteriocin produced in vivo by a human commensal bacterium was purified and characterized.
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PMID:Ruminococcin C, a new anti-Clostridium perfringens bacteriocin produced in the gut by the commensal bacterium Ruminococcus gnavus E1. 2158 10