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Peptidoglycan Remodeling in Gram-Negative Bacteria: From Stress Adaptation to Antibiotic Tolerance and Therapeutic Targeting. [PDF]
Antibiotics (Basel)Strohhammer T, Martorana AM, Polissi A.
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Identification of peptidases in Nicotiana tabacum leaf intercellular fluid
Proteomics, 2008 Peptidases in the extracellular space might affect the integrity of recombinant proteins expressed in, and secreted from, plant cells. To identify extracellular peptidases, we recovered the leaf intercellular fluid from Nicotiana tabacum plants by an ...
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Equine peptidases: Correspondence with human peptidases and polymorphism for erythrocyte peptidase a
Biochemical Genetics, 1979Equine erythrocyte peptidases were compared to the six human erythrocyte peptidases, A, B, C, D, E, and F, regarding substrate specificity, relative activity, and electrophoretic mobility. Five equine erythrocyte peptidases appeared homologous to human peptidases A, B, D, E, and F.
L R Weitkamp, Lowell R Weitkamp
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bchm, 2007
Abstract A good system for the naming and classification of peptidases can contribute much to the study of these enzymes. Having already described the building of families and clans in the MEROPS system, we here focus on the lowest level in the hierarchy, in which the huge number of individual peptidase proteins are assigned to a lesser ...
Alan J, Barrett, Neil D, Rawlings
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Abstract A good system for the naming and classification of peptidases can contribute much to the study of these enzymes. Having already described the building of families and clans in the MEROPS system, we here focus on the lowest level in the hierarchy, in which the huge number of individual peptidase proteins are assigned to a lesser ...
Alan J, Barrett, Neil D, Rawlings
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Experimental Eye Research, 1969
Peptidase activity, operative at neutral pH, was found in bovine cornea and conjunctiva with a synthetic substrate assay. The same peptidase was found previously in commercial bacterial collagenase preparations. Cell fractionation of homogenates revealed the activity to be maximal in the high-speed supernatant of the corneal and conjunctival epithelium,
H H, Slansky +4 more
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Peptidase activity, operative at neutral pH, was found in bovine cornea and conjunctiva with a synthetic substrate assay. The same peptidase was found previously in commercial bacterial collagenase preparations. Cell fractionation of homogenates revealed the activity to be maximal in the high-speed supernatant of the corneal and conjunctival epithelium,
H H, Slansky +4 more
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ChemInform, 2002
AbstractFor Abstract see ChemInform Abstract in Full Text.
Mark, Paetzel +3 more
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AbstractFor Abstract see ChemInform Abstract in Full Text.
Mark, Paetzel +3 more
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Tripeptidyl-peptidase II: A multi-purpose peptidase
The International Journal of Biochemistry & Cell Biology, 2005Tripeptidyl-peptidase II is a high-molecular weight peptidase with a widespread distribution in eukaryotic cells. The enzyme sequentially removes tripeptides from a free N-terminus of longer peptides and also displays a low endopeptidase activity. A role for tripeptidyl-peptidase II in the formation of peptides for antigen presentation has recently ...
Birgitta, Tomkinson +1 more
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Chorionic peptidase inactivates GnRH as a post‐proline peptidase
International Journal of Gynecology & Obstetrics, 1992Recently, we have described a chorionic peptidase (C-ase-1) which inactivates gonadotropin releasing hormone (GnRH), oxytocin, angiotensin II and thyrotropin releasing hormone. Since all these hormones contain a proline residue, we proposed that C-ase-1 may act as a post-proline peptidase.
I S, Kang, T M, Siler-Khodr
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Molecular Microbiology, 1991
SummaryThe Escherichia coli leader peptidase has been vital for unravelling problems in membrane assembly and protein export. The role of this essential peptidase is to remove amino‐terminal leader peptides from exported proteins after they have crossed the plasma membrane.
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SummaryThe Escherichia coli leader peptidase has been vital for unravelling problems in membrane assembly and protein export. The role of this essential peptidase is to remove amino‐terminal leader peptides from exported proteins after they have crossed the plasma membrane.
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