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Staphylococcal Protease: A Proteolytic Enzyme Specific for Glutamoyl Bonds
Open accessAbstract
An extracellular protease of Staphylococcus aureus , strain V8, previously shown to cleave specifically the peptide bonds on the carboxyl-terminal side of either aspartate or glutamate residues in phosphate buffer (pH 7.8) hydrolyzes only glutamoyl bonds in either ammonium bicarbonate (pH 7.8) or ammonium acetate (pH 4.0). Of all aspartoyl bonds tested, only the Asp-Gly linkage is cleaved at a detectable rate. The staphylococcal protease hydrolyzes all of the seventeen different glutamoyl bonds studied, although those involving hydrophobic aminoacid residues with bulky side chains are cleaved at a lower rate.
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Cited by
Human lactotransferrin: amino acid sequence and structural comparisons with other transferrins
METZ-BOUTIGUE, M.-H., JOLLES, J., MAZURIER, J., SCHOENTGEN, F., LEGRAND, D., SPIK, G., MONTREUIL, J., & JOLLES, P. (1984) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1984.tb08607.x · Cited by 538
Engelman, A., & Craigie, R. (1992) · Journal of Virology · doi:10.1128/jvi.66.11.6361-6369.1992 · Cited by 519
Nagy, E., & Rigby, W. F. C. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.6.2755 · Cited by 361
Schiff, R. D., & Grandgenett, D. P. (1978) · Journal of Virology · doi:10.1128/jvi.28.1.279-291.1978 · Cited by 76
Metadata
- Authors
- Houmard, J., & Drapeau, G. R.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1972-12
- Volume
- 69
- Issue
- 12
- Pages
- 3506-3509
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2082522919
- Cited by
- 696
- References
- 0
- FWCI
- 25.15
- Type
- journal article
- Language
- en
- Open access
- green
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- CoChat. (2026). Citation check: Staphylococcal Protease: A Proteolytic Enzyme Specific for Glutamoyl Bonds. https://app.cochat.ai/papers/10.1073/pnas.69.12.3506
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- Houmard, J., & Drapeau, G. R. (1972). Staphylococcal Protease: A Proteolytic Enzyme Specific for Glutamoyl Bonds. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.69.12.3506
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
