Suicide Inactivation of Human Prostatic Acid Phosphatase and a Phosphotyrosine Phosphatase
4-Difluoromethylphenyl bis(cyclohexylammonium) phosphate was synthesized in 4 steps starting from dibenzyl phosphite and shown to be a time-dependent suicide inactivator of human prostatic acid phosphatase and the SHP protein tyrosine phosphatase. The inactivation of human prostatic acid phosphatase...
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| Autor*in: |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1994 |
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| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
|---|---|
| Übergeordnetes Werk: |
in: Biochemical and Biophysical Research Communications - Amsterdam : Elsevier, 200(1994), 1, Seite 577-583 |
| Übergeordnetes Werk: |
volume:200 ; year:1994 ; number:1 ; pages:577-583 |
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NLEJ183469410 |
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| 520 | |a 4-Difluoromethylphenyl bis(cyclohexylammonium) phosphate was synthesized in 4 steps starting from dibenzyl phosphite and shown to be a time-dependent suicide inactivator of human prostatic acid phosphatase and the SHP protein tyrosine phosphatase. The inactivation of human prostatic acid phosphatase followed pseudo-first-order kinetics with inactivation constants of K"i = 1.0 mM; k"i = 0.15 min^-^1 (t"1"2 = 4.6 min at saturation). Phenyl phosphate protected the enzyme against inactivation, indicating that inactivation occurs in the active site. The inactivation of SHP also followed pseudo-first-order kinetics, with a t"1"2 = ~15 min in the presence of 8.2 mM inhibitor. The mechanism of inactivation likely involves the enzymatic release of difluoromethyl phenol which rapidly eliminates fluoride,generating a quinone methide. This potent electrophile then reacts with residues at the active site of the enzyme. This inhibitor and peptidic derivatives thereof have excellent potential for selective inactivation and labeling of protein tyrosine phosphatases. | ||
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(DE-627)NLEJ183469410 (DE-599)GBVNLZ183469410 DE-627 ger DE-627 rakwb eng Suicide Inactivation of Human Prostatic Acid Phosphatase and a Phosphotyrosine Phosphatase 1994 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 4-Difluoromethylphenyl bis(cyclohexylammonium) phosphate was synthesized in 4 steps starting from dibenzyl phosphite and shown to be a time-dependent suicide inactivator of human prostatic acid phosphatase and the SHP protein tyrosine phosphatase. The inactivation of human prostatic acid phosphatase followed pseudo-first-order kinetics with inactivation constants of K"i = 1.0 mM; k"i = 0.15 min^-^1 (t"1"2 = 4.6 min at saturation). Phenyl phosphate protected the enzyme against inactivation, indicating that inactivation occurs in the active site. The inactivation of SHP also followed pseudo-first-order kinetics, with a t"1"2 = ~15 min in the presence of 8.2 mM inhibitor. The mechanism of inactivation likely involves the enzymatic release of difluoromethyl phenol which rapidly eliminates fluoride,generating a quinone methide. This potent electrophile then reacts with residues at the active site of the enzyme. This inhibitor and peptidic derivatives thereof have excellent potential for selective inactivation and labeling of protein tyrosine phosphatases. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Wang, Q.P. oth Dechert, U. oth Jirik, F. oth Withers, S.G. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 200(1994), 1, Seite 577-583 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:200 year:1994 number:1 pages:577-583 http://dx.doi.org/10.1006/bbrc.1994.1487 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 200 1994 1 577-583 |
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(DE-627)NLEJ183469410 (DE-599)GBVNLZ183469410 DE-627 ger DE-627 rakwb eng Suicide Inactivation of Human Prostatic Acid Phosphatase and a Phosphotyrosine Phosphatase 1994 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 4-Difluoromethylphenyl bis(cyclohexylammonium) phosphate was synthesized in 4 steps starting from dibenzyl phosphite and shown to be a time-dependent suicide inactivator of human prostatic acid phosphatase and the SHP protein tyrosine phosphatase. The inactivation of human prostatic acid phosphatase followed pseudo-first-order kinetics with inactivation constants of K"i = 1.0 mM; k"i = 0.15 min^-^1 (t"1"2 = 4.6 min at saturation). Phenyl phosphate protected the enzyme against inactivation, indicating that inactivation occurs in the active site. The inactivation of SHP also followed pseudo-first-order kinetics, with a t"1"2 = ~15 min in the presence of 8.2 mM inhibitor. The mechanism of inactivation likely involves the enzymatic release of difluoromethyl phenol which rapidly eliminates fluoride,generating a quinone methide. This potent electrophile then reacts with residues at the active site of the enzyme. This inhibitor and peptidic derivatives thereof have excellent potential for selective inactivation and labeling of protein tyrosine phosphatases. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Wang, Q.P. oth Dechert, U. oth Jirik, F. oth Withers, S.G. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 200(1994), 1, Seite 577-583 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:200 year:1994 number:1 pages:577-583 http://dx.doi.org/10.1006/bbrc.1994.1487 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 200 1994 1 577-583 |
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(DE-627)NLEJ183469410 (DE-599)GBVNLZ183469410 DE-627 ger DE-627 rakwb eng Suicide Inactivation of Human Prostatic Acid Phosphatase and a Phosphotyrosine Phosphatase 1994 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 4-Difluoromethylphenyl bis(cyclohexylammonium) phosphate was synthesized in 4 steps starting from dibenzyl phosphite and shown to be a time-dependent suicide inactivator of human prostatic acid phosphatase and the SHP protein tyrosine phosphatase. The inactivation of human prostatic acid phosphatase followed pseudo-first-order kinetics with inactivation constants of K"i = 1.0 mM; k"i = 0.15 min^-^1 (t"1"2 = 4.6 min at saturation). Phenyl phosphate protected the enzyme against inactivation, indicating that inactivation occurs in the active site. The inactivation of SHP also followed pseudo-first-order kinetics, with a t"1"2 = ~15 min in the presence of 8.2 mM inhibitor. The mechanism of inactivation likely involves the enzymatic release of difluoromethyl phenol which rapidly eliminates fluoride,generating a quinone methide. This potent electrophile then reacts with residues at the active site of the enzyme. This inhibitor and peptidic derivatives thereof have excellent potential for selective inactivation and labeling of protein tyrosine phosphatases. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Wang, Q.P. oth Dechert, U. oth Jirik, F. oth Withers, S.G. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 200(1994), 1, Seite 577-583 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:200 year:1994 number:1 pages:577-583 http://dx.doi.org/10.1006/bbrc.1994.1487 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 200 1994 1 577-583 |
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(DE-627)NLEJ183469410 (DE-599)GBVNLZ183469410 DE-627 ger DE-627 rakwb eng Suicide Inactivation of Human Prostatic Acid Phosphatase and a Phosphotyrosine Phosphatase 1994 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 4-Difluoromethylphenyl bis(cyclohexylammonium) phosphate was synthesized in 4 steps starting from dibenzyl phosphite and shown to be a time-dependent suicide inactivator of human prostatic acid phosphatase and the SHP protein tyrosine phosphatase. The inactivation of human prostatic acid phosphatase followed pseudo-first-order kinetics with inactivation constants of K"i = 1.0 mM; k"i = 0.15 min^-^1 (t"1"2 = 4.6 min at saturation). Phenyl phosphate protected the enzyme against inactivation, indicating that inactivation occurs in the active site. The inactivation of SHP also followed pseudo-first-order kinetics, with a t"1"2 = ~15 min in the presence of 8.2 mM inhibitor. The mechanism of inactivation likely involves the enzymatic release of difluoromethyl phenol which rapidly eliminates fluoride,generating a quinone methide. This potent electrophile then reacts with residues at the active site of the enzyme. This inhibitor and peptidic derivatives thereof have excellent potential for selective inactivation and labeling of protein tyrosine phosphatases. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Wang, Q.P. oth Dechert, U. oth Jirik, F. oth Withers, S.G. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 200(1994), 1, Seite 577-583 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:200 year:1994 number:1 pages:577-583 http://dx.doi.org/10.1006/bbrc.1994.1487 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 200 1994 1 577-583 |
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(DE-627)NLEJ183469410 (DE-599)GBVNLZ183469410 DE-627 ger DE-627 rakwb eng Suicide Inactivation of Human Prostatic Acid Phosphatase and a Phosphotyrosine Phosphatase 1994 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 4-Difluoromethylphenyl bis(cyclohexylammonium) phosphate was synthesized in 4 steps starting from dibenzyl phosphite and shown to be a time-dependent suicide inactivator of human prostatic acid phosphatase and the SHP protein tyrosine phosphatase. The inactivation of human prostatic acid phosphatase followed pseudo-first-order kinetics with inactivation constants of K"i = 1.0 mM; k"i = 0.15 min^-^1 (t"1"2 = 4.6 min at saturation). Phenyl phosphate protected the enzyme against inactivation, indicating that inactivation occurs in the active site. The inactivation of SHP also followed pseudo-first-order kinetics, with a t"1"2 = ~15 min in the presence of 8.2 mM inhibitor. The mechanism of inactivation likely involves the enzymatic release of difluoromethyl phenol which rapidly eliminates fluoride,generating a quinone methide. This potent electrophile then reacts with residues at the active site of the enzyme. This inhibitor and peptidic derivatives thereof have excellent potential for selective inactivation and labeling of protein tyrosine phosphatases. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Wang, Q.P. oth Dechert, U. oth Jirik, F. oth Withers, S.G. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 200(1994), 1, Seite 577-583 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:200 year:1994 number:1 pages:577-583 http://dx.doi.org/10.1006/bbrc.1994.1487 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 200 1994 1 577-583 |
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Suicide Inactivation of Human Prostatic Acid Phosphatase and a Phosphotyrosine Phosphatase |
| abstract |
4-Difluoromethylphenyl bis(cyclohexylammonium) phosphate was synthesized in 4 steps starting from dibenzyl phosphite and shown to be a time-dependent suicide inactivator of human prostatic acid phosphatase and the SHP protein tyrosine phosphatase. The inactivation of human prostatic acid phosphatase followed pseudo-first-order kinetics with inactivation constants of K"i = 1.0 mM; k"i = 0.15 min^-^1 (t"1"2 = 4.6 min at saturation). Phenyl phosphate protected the enzyme against inactivation, indicating that inactivation occurs in the active site. The inactivation of SHP also followed pseudo-first-order kinetics, with a t"1"2 = ~15 min in the presence of 8.2 mM inhibitor. The mechanism of inactivation likely involves the enzymatic release of difluoromethyl phenol which rapidly eliminates fluoride,generating a quinone methide. This potent electrophile then reacts with residues at the active site of the enzyme. This inhibitor and peptidic derivatives thereof have excellent potential for selective inactivation and labeling of protein tyrosine phosphatases. |
| abstractGer |
4-Difluoromethylphenyl bis(cyclohexylammonium) phosphate was synthesized in 4 steps starting from dibenzyl phosphite and shown to be a time-dependent suicide inactivator of human prostatic acid phosphatase and the SHP protein tyrosine phosphatase. The inactivation of human prostatic acid phosphatase followed pseudo-first-order kinetics with inactivation constants of K"i = 1.0 mM; k"i = 0.15 min^-^1 (t"1"2 = 4.6 min at saturation). Phenyl phosphate protected the enzyme against inactivation, indicating that inactivation occurs in the active site. The inactivation of SHP also followed pseudo-first-order kinetics, with a t"1"2 = ~15 min in the presence of 8.2 mM inhibitor. The mechanism of inactivation likely involves the enzymatic release of difluoromethyl phenol which rapidly eliminates fluoride,generating a quinone methide. This potent electrophile then reacts with residues at the active site of the enzyme. This inhibitor and peptidic derivatives thereof have excellent potential for selective inactivation and labeling of protein tyrosine phosphatases. |
| abstract_unstemmed |
4-Difluoromethylphenyl bis(cyclohexylammonium) phosphate was synthesized in 4 steps starting from dibenzyl phosphite and shown to be a time-dependent suicide inactivator of human prostatic acid phosphatase and the SHP protein tyrosine phosphatase. The inactivation of human prostatic acid phosphatase followed pseudo-first-order kinetics with inactivation constants of K"i = 1.0 mM; k"i = 0.15 min^-^1 (t"1"2 = 4.6 min at saturation). Phenyl phosphate protected the enzyme against inactivation, indicating that inactivation occurs in the active site. The inactivation of SHP also followed pseudo-first-order kinetics, with a t"1"2 = ~15 min in the presence of 8.2 mM inhibitor. The mechanism of inactivation likely involves the enzymatic release of difluoromethyl phenol which rapidly eliminates fluoride,generating a quinone methide. This potent electrophile then reacts with residues at the active site of the enzyme. This inhibitor and peptidic derivatives thereof have excellent potential for selective inactivation and labeling of protein tyrosine phosphatases. |
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<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">NLEJ183469410</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210706203216.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070506s1994 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ183469410</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)GBVNLZ183469410</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Suicide Inactivation of Human Prostatic Acid Phosphatase and a Phosphotyrosine Phosphatase</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1994</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">z</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zu</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">4-Difluoromethylphenyl bis(cyclohexylammonium) phosphate was synthesized in 4 steps starting from dibenzyl phosphite and shown to be a time-dependent suicide inactivator of human prostatic acid phosphatase and the SHP protein tyrosine phosphatase. The inactivation of human prostatic acid phosphatase followed pseudo-first-order kinetics with inactivation constants of K"i = 1.0 mM; k"i = 0.15 min^-^1 (t"1"2 = 4.6 min at saturation). Phenyl phosphate protected the enzyme against inactivation, indicating that inactivation occurs in the active site. The inactivation of SHP also followed pseudo-first-order kinetics, with a t"1"2 = ~15 min in the presence of 8.2 mM inhibitor. The mechanism of inactivation likely involves the enzymatic release of difluoromethyl phenol which rapidly eliminates fluoride,generating a quinone methide. This potent electrophile then reacts with residues at the active site of the enzyme. This inhibitor and peptidic derivatives thereof have excellent potential for selective inactivation and labeling of protein tyrosine phosphatases.</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="f">Elsevier Journal Backfiles on ScienceDirect 1907 - 2002</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Wang, Q.P.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Dechert, U.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Jirik, F.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Withers, S.G.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">in</subfield><subfield code="t">Biochemical and Biophysical Research Communications</subfield><subfield code="d">Amsterdam : Elsevier</subfield><subfield code="g">200(1994), 1, Seite 577-583</subfield><subfield code="w">(DE-627)NLEJ176855645</subfield><subfield code="w">(DE-600)1461396-7</subfield><subfield code="x">0006-291X</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:200</subfield><subfield code="g">year:1994</subfield><subfield code="g">number:1</subfield><subfield code="g">pages:577-583</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1006/bbrc.1994.1487</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_H</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">ZDB-1-SDJ</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_NL_ARTICLE</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">200</subfield><subfield code="j">1994</subfield><subfield code="e">1</subfield><subfield code="h">577-583</subfield></datafield></record></collection>
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7.401163 |