Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.24.27 (thermolysin)
 1,894 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Tick-borne encephalitis virus was treated with pronase or thermolysin. The resulting particles were banded in sucrose gradients and analyzed for polypeptide composition. Both enzymes caused a reduction in particle density from 1.19 to 1.15--1.16 g/cm3. No loss of viral lipid or nucleic acid could be observed. SDS-polyacrylamidegel electrophoresis showed that only the core protein V2 was unchanged whereas the envelope proteins V3 and V1 had disappeared from their original positions in the PAGE profile. Instead a new peptide(s) with molecular weight of 4000--6000 was found in which hydrophobic amino-acids were enriched. Crosslinking by dimethyl-3.3'-dithiobispropionimidate (DTBP) made the virus resistent to solubilization of the envelope proteins by TX-100. This could be interpreted by the formation of a dense envelope protein network around the nucleocapsid preventing its liberation by TX-100. Some data however indicate that direct crosslinking of at least one of the envelope proteins with the core cannot be excluded.
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PMID:Protease treatment and chemical crosslinking of a flavivirus: tick borne encephalitis virus. 50 94

The primary structure of the core protein of Semliki Forest virus has been established by protein chemical characterization of 102 peptides, generated by digestion with trypsin, pepsin, thermolysin, and by partial acid cleavage of the protein. Besides a difference in one position, the sequence as established by these experiments is in agreement with the sequence predicted from the nucleotide sequence of the mRNA [Garoff et al. (1980) Proc. Natl Acad. Sci. USA, 77, 6376-6380]. The core protein has a blocked N terminus, consists of 267 amino acid residues, and has the following amino acid composition: Asp12, Asn9, Thr16, Ser10, Glu11, Gln15, Pro23, Gly20, Ala23, Val19, Met8, Ile11, Leu9, Tyr7, Phe6, His7, Lys37, Arg15, Trp5, Cys4, and an Mr of 29919. It contains 22.1% basic amino acids, mainly lysines, compared with a total of 8.6% acidic residues. The resulting surplus of positive charge is located in the N-terminal half of the protein (predominantly arginines at positions 12-21 and lysines at positions 66-114). Other amino acids are also unevenly distributed; proline and glutamine are accumulated in the N-terminal half of the sequence whereas histidine, glycine and the acidic residues are mainly present in the C-terminal part. This distribution suggests that the virus core protein consists of two or more structural domains.
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PMID:The core protein of alphaviruses. 1. Purification of peptides and complete amino-acid sequence of Semliki Forest virus core protein. 685 50

The primary structure of the core protein of Sindbis virus has been established by protein chemical characterization of peptides derived by enzymatic digestion with trypsin, pepsin and thermolysin and by chemical cleavage with cyanogen bromide. The peptide chain consists of 264 amino acids and has the composition Asp8, Asn8, Thr17, Ser12, Glu12, Gln14, Pro28, Gly24, Ala22, Val16, Met10, Ile8, Leu14, Tyr4, Phe9, His6, Lys25, Arg23 and Trp4 and an Mr of 29 382. Comparison of this structure with the primary structure of the SF virus core protein revealed several important common characteristics of alphavirus core proteins. 1. The N-terminal halves (1-110) of the proteins are rich in basic amino acids and proline. 2. The C-terminal part (approximately equal to 110-264/267) is highly conserved: 70% of the amino acid residues are in identical positions. 3. The conserved part contains a possible catalytic centre for the presumed protease activity of the core protein. The similarities between the primary structures of both core proteins are reflected in their predicted secondary structures.
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PMID:The core protein of alphaviruses. 2. Purification of peptides and complete amino-acid sequence of Sindbis virus core protein. 685 51

Vaccinia virus maturation into infectious particles appears to be dependent on the proteolytic processing of at least five viral proteins, each containing a conserved AG*X cleavage motif and each requiring proper association with the previrion particle. To identify the responsible proteinase, a transcriptionally controlled trans-processing assay was developed to monitor cleavage at the permissive AG*S site of the P25K core protein precursor. This assay led to the putative identification of a VV proteinase encoded by open reading frame G1L. The predicted protein contains an HXXEH sequence which is a direct inversion of the active site consensus sequence present in thermolysin and other metalloendopeptidases. Site-directed mutation of this consensus sequence suggests that the G1L protein may be a novel, virus-encoded metalloendoproteinase, although confirmation of this activity must await the development of a suitable cell-free processing assay.
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PMID:A transcriptionally controlled trans-processing assay: putative identification of a vaccinia virus-encoded proteinase which cleaves precursor protein P25K. 793 50