Substrate phosphorylation can inhibit proteolysis by trypsin-like enzymes
The effect of substrate phosphorylation on the susceptibility to proteolytic cleavage by trypsin-like enzymes was investigated using the model heptapeptide Leu-Arg-Arg-Ala-Ser-Leu-Gly, a peptide representing the endogenous phosphorylation site of pyruvate kinase. Phosphorylation of Ser 5 altered the...
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| Autor*in: |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1989 |
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| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
|---|---|
| Übergeordnetes Werk: |
in: Archives of Biochemistry and Biophysics - Amsterdam : Elsevier, 272(1989), 2, Seite 274-280 |
| Übergeordnetes Werk: |
volume:272 ; year:1989 ; number:2 ; pages:274-280 |
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NLEJ183405080 |
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| 520 | |a The effect of substrate phosphorylation on the susceptibility to proteolytic cleavage by trypsin-like enzymes was investigated using the model heptapeptide Leu-Arg-Arg-Ala-Ser-Leu-Gly, a peptide representing the endogenous phosphorylation site of pyruvate kinase. Phosphorylation of Ser 5 altered the kinetics of proteolysis by two proteases, trypsin and rat plasma kallikrein, both of which cleaved between Arg 3 and Ala 4. In the case of trypsin, phosphorylation decreased the rate of cleavage 47-fold. In the case of rat plasma kallikrein, phosphorylation decreased proteolysis 13-fold. Phosphorylation resulted in an apparent redirection of the preferential site from Arg 3 to Arg 2. Because sequences analogous to this model peptide are commonly found in exposed domains of globular proteins, and since these regions are susceptible to both phosphorylation and protease attack, the results indicate that substrate phosphorylation may selectively influence protein processing and turnover. | ||
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(DE-627)NLEJ183405080 (DE-599)GBVNLZ183405080 DE-627 ger DE-627 rakwb eng Substrate phosphorylation can inhibit proteolysis by trypsin-like enzymes 1989 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The effect of substrate phosphorylation on the susceptibility to proteolytic cleavage by trypsin-like enzymes was investigated using the model heptapeptide Leu-Arg-Arg-Ala-Ser-Leu-Gly, a peptide representing the endogenous phosphorylation site of pyruvate kinase. Phosphorylation of Ser 5 altered the kinetics of proteolysis by two proteases, trypsin and rat plasma kallikrein, both of which cleaved between Arg 3 and Ala 4. In the case of trypsin, phosphorylation decreased the rate of cleavage 47-fold. In the case of rat plasma kallikrein, phosphorylation decreased proteolysis 13-fold. Phosphorylation resulted in an apparent redirection of the preferential site from Arg 3 to Arg 2. Because sequences analogous to this model peptide are commonly found in exposed domains of globular proteins, and since these regions are susceptible to both phosphorylation and protease attack, the results indicate that substrate phosphorylation may selectively influence protein processing and turnover. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Benore-Parsons, M. oth Seidah, N.G. oth Wennogle, L.P. oth in Archives of Biochemistry and Biophysics Amsterdam : Elsevier 272(1989), 2, Seite 274-280 (DE-627)NLEJ177020539 (DE-600)1461378-5 0003-9861 nnns volume:272 year:1989 number:2 pages:274-280 http://dx.doi.org/10.1016/0003-9861(89)90220-8 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 272 1989 2 274-280 |
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(DE-627)NLEJ183405080 (DE-599)GBVNLZ183405080 DE-627 ger DE-627 rakwb eng Substrate phosphorylation can inhibit proteolysis by trypsin-like enzymes 1989 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The effect of substrate phosphorylation on the susceptibility to proteolytic cleavage by trypsin-like enzymes was investigated using the model heptapeptide Leu-Arg-Arg-Ala-Ser-Leu-Gly, a peptide representing the endogenous phosphorylation site of pyruvate kinase. Phosphorylation of Ser 5 altered the kinetics of proteolysis by two proteases, trypsin and rat plasma kallikrein, both of which cleaved between Arg 3 and Ala 4. In the case of trypsin, phosphorylation decreased the rate of cleavage 47-fold. In the case of rat plasma kallikrein, phosphorylation decreased proteolysis 13-fold. Phosphorylation resulted in an apparent redirection of the preferential site from Arg 3 to Arg 2. Because sequences analogous to this model peptide are commonly found in exposed domains of globular proteins, and since these regions are susceptible to both phosphorylation and protease attack, the results indicate that substrate phosphorylation may selectively influence protein processing and turnover. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Benore-Parsons, M. oth Seidah, N.G. oth Wennogle, L.P. oth in Archives of Biochemistry and Biophysics Amsterdam : Elsevier 272(1989), 2, Seite 274-280 (DE-627)NLEJ177020539 (DE-600)1461378-5 0003-9861 nnns volume:272 year:1989 number:2 pages:274-280 http://dx.doi.org/10.1016/0003-9861(89)90220-8 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 272 1989 2 274-280 |
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(DE-627)NLEJ183405080 (DE-599)GBVNLZ183405080 DE-627 ger DE-627 rakwb eng Substrate phosphorylation can inhibit proteolysis by trypsin-like enzymes 1989 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The effect of substrate phosphorylation on the susceptibility to proteolytic cleavage by trypsin-like enzymes was investigated using the model heptapeptide Leu-Arg-Arg-Ala-Ser-Leu-Gly, a peptide representing the endogenous phosphorylation site of pyruvate kinase. Phosphorylation of Ser 5 altered the kinetics of proteolysis by two proteases, trypsin and rat plasma kallikrein, both of which cleaved between Arg 3 and Ala 4. In the case of trypsin, phosphorylation decreased the rate of cleavage 47-fold. In the case of rat plasma kallikrein, phosphorylation decreased proteolysis 13-fold. Phosphorylation resulted in an apparent redirection of the preferential site from Arg 3 to Arg 2. Because sequences analogous to this model peptide are commonly found in exposed domains of globular proteins, and since these regions are susceptible to both phosphorylation and protease attack, the results indicate that substrate phosphorylation may selectively influence protein processing and turnover. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Benore-Parsons, M. oth Seidah, N.G. oth Wennogle, L.P. oth in Archives of Biochemistry and Biophysics Amsterdam : Elsevier 272(1989), 2, Seite 274-280 (DE-627)NLEJ177020539 (DE-600)1461378-5 0003-9861 nnns volume:272 year:1989 number:2 pages:274-280 http://dx.doi.org/10.1016/0003-9861(89)90220-8 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 272 1989 2 274-280 |
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(DE-627)NLEJ183405080 (DE-599)GBVNLZ183405080 DE-627 ger DE-627 rakwb eng Substrate phosphorylation can inhibit proteolysis by trypsin-like enzymes 1989 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The effect of substrate phosphorylation on the susceptibility to proteolytic cleavage by trypsin-like enzymes was investigated using the model heptapeptide Leu-Arg-Arg-Ala-Ser-Leu-Gly, a peptide representing the endogenous phosphorylation site of pyruvate kinase. Phosphorylation of Ser 5 altered the kinetics of proteolysis by two proteases, trypsin and rat plasma kallikrein, both of which cleaved between Arg 3 and Ala 4. In the case of trypsin, phosphorylation decreased the rate of cleavage 47-fold. In the case of rat plasma kallikrein, phosphorylation decreased proteolysis 13-fold. Phosphorylation resulted in an apparent redirection of the preferential site from Arg 3 to Arg 2. Because sequences analogous to this model peptide are commonly found in exposed domains of globular proteins, and since these regions are susceptible to both phosphorylation and protease attack, the results indicate that substrate phosphorylation may selectively influence protein processing and turnover. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Benore-Parsons, M. oth Seidah, N.G. oth Wennogle, L.P. oth in Archives of Biochemistry and Biophysics Amsterdam : Elsevier 272(1989), 2, Seite 274-280 (DE-627)NLEJ177020539 (DE-600)1461378-5 0003-9861 nnns volume:272 year:1989 number:2 pages:274-280 http://dx.doi.org/10.1016/0003-9861(89)90220-8 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 272 1989 2 274-280 |
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(DE-627)NLEJ183405080 (DE-599)GBVNLZ183405080 DE-627 ger DE-627 rakwb eng Substrate phosphorylation can inhibit proteolysis by trypsin-like enzymes 1989 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The effect of substrate phosphorylation on the susceptibility to proteolytic cleavage by trypsin-like enzymes was investigated using the model heptapeptide Leu-Arg-Arg-Ala-Ser-Leu-Gly, a peptide representing the endogenous phosphorylation site of pyruvate kinase. Phosphorylation of Ser 5 altered the kinetics of proteolysis by two proteases, trypsin and rat plasma kallikrein, both of which cleaved between Arg 3 and Ala 4. In the case of trypsin, phosphorylation decreased the rate of cleavage 47-fold. In the case of rat plasma kallikrein, phosphorylation decreased proteolysis 13-fold. Phosphorylation resulted in an apparent redirection of the preferential site from Arg 3 to Arg 2. Because sequences analogous to this model peptide are commonly found in exposed domains of globular proteins, and since these regions are susceptible to both phosphorylation and protease attack, the results indicate that substrate phosphorylation may selectively influence protein processing and turnover. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Benore-Parsons, M. oth Seidah, N.G. oth Wennogle, L.P. oth in Archives of Biochemistry and Biophysics Amsterdam : Elsevier 272(1989), 2, Seite 274-280 (DE-627)NLEJ177020539 (DE-600)1461378-5 0003-9861 nnns volume:272 year:1989 number:2 pages:274-280 http://dx.doi.org/10.1016/0003-9861(89)90220-8 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 272 1989 2 274-280 |
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Substrate phosphorylation can inhibit proteolysis by trypsin-like enzymes |
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The effect of substrate phosphorylation on the susceptibility to proteolytic cleavage by trypsin-like enzymes was investigated using the model heptapeptide Leu-Arg-Arg-Ala-Ser-Leu-Gly, a peptide representing the endogenous phosphorylation site of pyruvate kinase. Phosphorylation of Ser 5 altered the kinetics of proteolysis by two proteases, trypsin and rat plasma kallikrein, both of which cleaved between Arg 3 and Ala 4. In the case of trypsin, phosphorylation decreased the rate of cleavage 47-fold. In the case of rat plasma kallikrein, phosphorylation decreased proteolysis 13-fold. Phosphorylation resulted in an apparent redirection of the preferential site from Arg 3 to Arg 2. Because sequences analogous to this model peptide are commonly found in exposed domains of globular proteins, and since these regions are susceptible to both phosphorylation and protease attack, the results indicate that substrate phosphorylation may selectively influence protein processing and turnover. |
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The effect of substrate phosphorylation on the susceptibility to proteolytic cleavage by trypsin-like enzymes was investigated using the model heptapeptide Leu-Arg-Arg-Ala-Ser-Leu-Gly, a peptide representing the endogenous phosphorylation site of pyruvate kinase. Phosphorylation of Ser 5 altered the kinetics of proteolysis by two proteases, trypsin and rat plasma kallikrein, both of which cleaved between Arg 3 and Ala 4. In the case of trypsin, phosphorylation decreased the rate of cleavage 47-fold. In the case of rat plasma kallikrein, phosphorylation decreased proteolysis 13-fold. Phosphorylation resulted in an apparent redirection of the preferential site from Arg 3 to Arg 2. Because sequences analogous to this model peptide are commonly found in exposed domains of globular proteins, and since these regions are susceptible to both phosphorylation and protease attack, the results indicate that substrate phosphorylation may selectively influence protein processing and turnover. |
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The effect of substrate phosphorylation on the susceptibility to proteolytic cleavage by trypsin-like enzymes was investigated using the model heptapeptide Leu-Arg-Arg-Ala-Ser-Leu-Gly, a peptide representing the endogenous phosphorylation site of pyruvate kinase. Phosphorylation of Ser 5 altered the kinetics of proteolysis by two proteases, trypsin and rat plasma kallikrein, both of which cleaved between Arg 3 and Ala 4. In the case of trypsin, phosphorylation decreased the rate of cleavage 47-fold. In the case of rat plasma kallikrein, phosphorylation decreased proteolysis 13-fold. Phosphorylation resulted in an apparent redirection of the preferential site from Arg 3 to Arg 2. Because sequences analogous to this model peptide are commonly found in exposed domains of globular proteins, and since these regions are susceptible to both phosphorylation and protease attack, the results indicate that substrate phosphorylation may selectively influence protein processing and turnover. |
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