Enzymatic mechanism of creatine amidinohydrolase as deduced from crystal structures
Crystal structures of the enzyme creatine amidinohydrolase (creatinase, EC 3.5.3.3) with two different inhibitors, the reaction product sarcosine and the substrate creatine, bound have been analyzed by X-ray diffraction methods. With the inhibitor carbamoyl sarcosine, two different crystal forms at...
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| Sprache: |
Englisch |
| Erschienen: |
1990 |
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Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
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in: Journal of Molecular Biology - Amsterdam : Elsevier, 214(1990), 2, Seite 597-610 |
| Übergeordnetes Werk: |
volume:214 ; year:1990 ; number:2 ; pages:597-610 |
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| 245 | 1 | 0 | |a Enzymatic mechanism of creatine amidinohydrolase as deduced from crystal structures |
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| 520 | |a Crystal structures of the enzyme creatine amidinohydrolase (creatinase, EC 3.5.3.3) with two different inhibitors, the reaction product sarcosine and the substrate creatine, bound have been analyzed by X-ray diffraction methods. With the inhibitor carbamoyl sarcosine, two different crystal forms at different pH values have been determined. An enzymatic mechanism is proposed on the basis of the eight structures analyzed. The enzyme binds substrate and inhibitor in a distorted geometry where the urea resonance is broken. His232 is the general base and acid, and acts as a proton shuttle. It withdraws a proton from water 377 and donates it to the N"("3") atom of the guanidinium group. OH^- 377 adds to the C"("1") atom of the guanidinium group to form a urea hydrate. Proton withdrawal by His232 leads to products. The reaction product sarcosine binds to the active site in a reverse orientation. The free enzyme was found to have a bicarbonate bound to the active site. | ||
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(DE-627)NLEJ18540068X (DE-599)GBVNLZ18540068X DE-627 ger DE-627 rakwb eng Enzymatic mechanism of creatine amidinohydrolase as deduced from crystal structures 1990 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Crystal structures of the enzyme creatine amidinohydrolase (creatinase, EC 3.5.3.3) with two different inhibitors, the reaction product sarcosine and the substrate creatine, bound have been analyzed by X-ray diffraction methods. With the inhibitor carbamoyl sarcosine, two different crystal forms at different pH values have been determined. An enzymatic mechanism is proposed on the basis of the eight structures analyzed. The enzyme binds substrate and inhibitor in a distorted geometry where the urea resonance is broken. His232 is the general base and acid, and acts as a proton shuttle. It withdraws a proton from water 377 and donates it to the N"("3") atom of the guanidinium group. OH^- 377 adds to the C"("1") atom of the guanidinium group to form a urea hydrate. Proton withdrawal by His232 leads to products. The reaction product sarcosine binds to the active site in a reverse orientation. The free enzyme was found to have a bicarbonate bound to the active site. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Coll, M. oth Knof, S.H. oth Ohga, Y. oth Messerschmidt, A. oth Huber, R. oth Moellering, H. oth Russmann, L. oth Schumacher, G. oth in Journal of Molecular Biology Amsterdam : Elsevier 214(1990), 2, Seite 597-610 (DE-627)NLEJ176863974 (DE-600)1355192-9 0022-2836 nnns volume:214 year:1990 number:2 pages:597-610 http://dx.doi.org/10.1016/0022-2836(90)90201-V GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 214 1990 2 597-610 |
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(DE-627)NLEJ18540068X (DE-599)GBVNLZ18540068X DE-627 ger DE-627 rakwb eng Enzymatic mechanism of creatine amidinohydrolase as deduced from crystal structures 1990 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Crystal structures of the enzyme creatine amidinohydrolase (creatinase, EC 3.5.3.3) with two different inhibitors, the reaction product sarcosine and the substrate creatine, bound have been analyzed by X-ray diffraction methods. With the inhibitor carbamoyl sarcosine, two different crystal forms at different pH values have been determined. An enzymatic mechanism is proposed on the basis of the eight structures analyzed. The enzyme binds substrate and inhibitor in a distorted geometry where the urea resonance is broken. His232 is the general base and acid, and acts as a proton shuttle. It withdraws a proton from water 377 and donates it to the N"("3") atom of the guanidinium group. OH^- 377 adds to the C"("1") atom of the guanidinium group to form a urea hydrate. Proton withdrawal by His232 leads to products. The reaction product sarcosine binds to the active site in a reverse orientation. The free enzyme was found to have a bicarbonate bound to the active site. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Coll, M. oth Knof, S.H. oth Ohga, Y. oth Messerschmidt, A. oth Huber, R. oth Moellering, H. oth Russmann, L. oth Schumacher, G. oth in Journal of Molecular Biology Amsterdam : Elsevier 214(1990), 2, Seite 597-610 (DE-627)NLEJ176863974 (DE-600)1355192-9 0022-2836 nnns volume:214 year:1990 number:2 pages:597-610 http://dx.doi.org/10.1016/0022-2836(90)90201-V GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 214 1990 2 597-610 |
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(DE-627)NLEJ18540068X (DE-599)GBVNLZ18540068X DE-627 ger DE-627 rakwb eng Enzymatic mechanism of creatine amidinohydrolase as deduced from crystal structures 1990 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Crystal structures of the enzyme creatine amidinohydrolase (creatinase, EC 3.5.3.3) with two different inhibitors, the reaction product sarcosine and the substrate creatine, bound have been analyzed by X-ray diffraction methods. With the inhibitor carbamoyl sarcosine, two different crystal forms at different pH values have been determined. An enzymatic mechanism is proposed on the basis of the eight structures analyzed. The enzyme binds substrate and inhibitor in a distorted geometry where the urea resonance is broken. His232 is the general base and acid, and acts as a proton shuttle. It withdraws a proton from water 377 and donates it to the N"("3") atom of the guanidinium group. OH^- 377 adds to the C"("1") atom of the guanidinium group to form a urea hydrate. Proton withdrawal by His232 leads to products. The reaction product sarcosine binds to the active site in a reverse orientation. The free enzyme was found to have a bicarbonate bound to the active site. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Coll, M. oth Knof, S.H. oth Ohga, Y. oth Messerschmidt, A. oth Huber, R. oth Moellering, H. oth Russmann, L. oth Schumacher, G. oth in Journal of Molecular Biology Amsterdam : Elsevier 214(1990), 2, Seite 597-610 (DE-627)NLEJ176863974 (DE-600)1355192-9 0022-2836 nnns volume:214 year:1990 number:2 pages:597-610 http://dx.doi.org/10.1016/0022-2836(90)90201-V GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 214 1990 2 597-610 |
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(DE-627)NLEJ18540068X (DE-599)GBVNLZ18540068X DE-627 ger DE-627 rakwb eng Enzymatic mechanism of creatine amidinohydrolase as deduced from crystal structures 1990 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Crystal structures of the enzyme creatine amidinohydrolase (creatinase, EC 3.5.3.3) with two different inhibitors, the reaction product sarcosine and the substrate creatine, bound have been analyzed by X-ray diffraction methods. With the inhibitor carbamoyl sarcosine, two different crystal forms at different pH values have been determined. An enzymatic mechanism is proposed on the basis of the eight structures analyzed. The enzyme binds substrate and inhibitor in a distorted geometry where the urea resonance is broken. His232 is the general base and acid, and acts as a proton shuttle. It withdraws a proton from water 377 and donates it to the N"("3") atom of the guanidinium group. OH^- 377 adds to the C"("1") atom of the guanidinium group to form a urea hydrate. Proton withdrawal by His232 leads to products. The reaction product sarcosine binds to the active site in a reverse orientation. The free enzyme was found to have a bicarbonate bound to the active site. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Coll, M. oth Knof, S.H. oth Ohga, Y. oth Messerschmidt, A. oth Huber, R. oth Moellering, H. oth Russmann, L. oth Schumacher, G. oth in Journal of Molecular Biology Amsterdam : Elsevier 214(1990), 2, Seite 597-610 (DE-627)NLEJ176863974 (DE-600)1355192-9 0022-2836 nnns volume:214 year:1990 number:2 pages:597-610 http://dx.doi.org/10.1016/0022-2836(90)90201-V GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 214 1990 2 597-610 |
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(DE-627)NLEJ18540068X (DE-599)GBVNLZ18540068X DE-627 ger DE-627 rakwb eng Enzymatic mechanism of creatine amidinohydrolase as deduced from crystal structures 1990 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Crystal structures of the enzyme creatine amidinohydrolase (creatinase, EC 3.5.3.3) with two different inhibitors, the reaction product sarcosine and the substrate creatine, bound have been analyzed by X-ray diffraction methods. With the inhibitor carbamoyl sarcosine, two different crystal forms at different pH values have been determined. An enzymatic mechanism is proposed on the basis of the eight structures analyzed. The enzyme binds substrate and inhibitor in a distorted geometry where the urea resonance is broken. His232 is the general base and acid, and acts as a proton shuttle. It withdraws a proton from water 377 and donates it to the N"("3") atom of the guanidinium group. OH^- 377 adds to the C"("1") atom of the guanidinium group to form a urea hydrate. Proton withdrawal by His232 leads to products. The reaction product sarcosine binds to the active site in a reverse orientation. The free enzyme was found to have a bicarbonate bound to the active site. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Coll, M. oth Knof, S.H. oth Ohga, Y. oth Messerschmidt, A. oth Huber, R. oth Moellering, H. oth Russmann, L. oth Schumacher, G. oth in Journal of Molecular Biology Amsterdam : Elsevier 214(1990), 2, Seite 597-610 (DE-627)NLEJ176863974 (DE-600)1355192-9 0022-2836 nnns volume:214 year:1990 number:2 pages:597-610 http://dx.doi.org/10.1016/0022-2836(90)90201-V GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 214 1990 2 597-610 |
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Enzymatic mechanism of creatine amidinohydrolase as deduced from crystal structures |
| abstract |
Crystal structures of the enzyme creatine amidinohydrolase (creatinase, EC 3.5.3.3) with two different inhibitors, the reaction product sarcosine and the substrate creatine, bound have been analyzed by X-ray diffraction methods. With the inhibitor carbamoyl sarcosine, two different crystal forms at different pH values have been determined. An enzymatic mechanism is proposed on the basis of the eight structures analyzed. The enzyme binds substrate and inhibitor in a distorted geometry where the urea resonance is broken. His232 is the general base and acid, and acts as a proton shuttle. It withdraws a proton from water 377 and donates it to the N"("3") atom of the guanidinium group. OH^- 377 adds to the C"("1") atom of the guanidinium group to form a urea hydrate. Proton withdrawal by His232 leads to products. The reaction product sarcosine binds to the active site in a reverse orientation. The free enzyme was found to have a bicarbonate bound to the active site. |
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Crystal structures of the enzyme creatine amidinohydrolase (creatinase, EC 3.5.3.3) with two different inhibitors, the reaction product sarcosine and the substrate creatine, bound have been analyzed by X-ray diffraction methods. With the inhibitor carbamoyl sarcosine, two different crystal forms at different pH values have been determined. An enzymatic mechanism is proposed on the basis of the eight structures analyzed. The enzyme binds substrate and inhibitor in a distorted geometry where the urea resonance is broken. His232 is the general base and acid, and acts as a proton shuttle. It withdraws a proton from water 377 and donates it to the N"("3") atom of the guanidinium group. OH^- 377 adds to the C"("1") atom of the guanidinium group to form a urea hydrate. Proton withdrawal by His232 leads to products. The reaction product sarcosine binds to the active site in a reverse orientation. The free enzyme was found to have a bicarbonate bound to the active site. |
| abstract_unstemmed |
Crystal structures of the enzyme creatine amidinohydrolase (creatinase, EC 3.5.3.3) with two different inhibitors, the reaction product sarcosine and the substrate creatine, bound have been analyzed by X-ray diffraction methods. With the inhibitor carbamoyl sarcosine, two different crystal forms at different pH values have been determined. An enzymatic mechanism is proposed on the basis of the eight structures analyzed. The enzyme binds substrate and inhibitor in a distorted geometry where the urea resonance is broken. His232 is the general base and acid, and acts as a proton shuttle. It withdraws a proton from water 377 and donates it to the N"("3") atom of the guanidinium group. OH^- 377 adds to the C"("1") atom of the guanidinium group to form a urea hydrate. Proton withdrawal by His232 leads to products. The reaction product sarcosine binds to the active site in a reverse orientation. The free enzyme was found to have a bicarbonate bound to the active site. |
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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">NLEJ18540068X</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210707014920.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070506s1990 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ18540068X</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)GBVNLZ18540068X</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">Enzymatic mechanism of creatine amidinohydrolase as deduced from crystal structures</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1990</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">Crystal structures of the enzyme creatine amidinohydrolase (creatinase, EC 3.5.3.3) with two different inhibitors, the reaction product sarcosine and the substrate creatine, bound have been analyzed by X-ray diffraction methods. With the inhibitor carbamoyl sarcosine, two different crystal forms at different pH values have been determined. An enzymatic mechanism is proposed on the basis of the eight structures analyzed. The enzyme binds substrate and inhibitor in a distorted geometry where the urea resonance is broken. His232 is the general base and acid, and acts as a proton shuttle. It withdraws a proton from water 377 and donates it to the N"("3") atom of the guanidinium group. OH^- 377 adds to the C"("1") atom of the guanidinium group to form a urea hydrate. Proton withdrawal by His232 leads to products. The reaction product sarcosine binds to the active site in a reverse orientation. The free enzyme was found to have a bicarbonate bound to the active site.</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">Coll, M.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Knof, S.H.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Ohga, Y.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Messerschmidt, A.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Huber, R.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Moellering, H.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Russmann, L.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Schumacher, G.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">in</subfield><subfield code="t">Journal of Molecular Biology</subfield><subfield code="d">Amsterdam : Elsevier</subfield><subfield code="g">214(1990), 2, Seite 597-610</subfield><subfield code="w">(DE-627)NLEJ176863974</subfield><subfield code="w">(DE-600)1355192-9</subfield><subfield code="x">0022-2836</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:214</subfield><subfield code="g">year:1990</subfield><subfield code="g">number:2</subfield><subfield code="g">pages:597-610</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1016/0022-2836(90)90201-V</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">214</subfield><subfield code="j">1990</subfield><subfield code="e">2</subfield><subfield code="h">597-610</subfield></datafield></record></collection>
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