1ura
From Proteopedia
(New page: 200px<br /> <applet load="1ura" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ura, resolution 2.04Å" /> '''ALKALINE PHOSPHATAS...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1URA is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]] with ZN and PO4 as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.1 3.1.3.1]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1URA OCA]]. | + | 1URA is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]] with ZN and PO4 as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Alkaline_phosphatase Alkaline phosphatase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.1 3.1.3.1]]. Structure known Active Sites: A and B. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1URA OCA]]. |
==Reference== | ==Reference== | ||
Kinetic and structural consequences of replacing the aspartate bridge by asparagine in the catalytic metal triad of Escherichia coli alkaline phosphatase., Tibbitts TT, Murphy JE, Kantrowitz ER, J Mol Biol. 1996 Apr 5;257(3):700-15. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8648634 8648634] | Kinetic and structural consequences of replacing the aspartate bridge by asparagine in the catalytic metal triad of Escherichia coli alkaline phosphatase., Tibbitts TT, Murphy JE, Kantrowitz ER, J Mol Biol. 1996 Apr 5;257(3):700-15. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8648634 8648634] | ||
| + | [[Category: Alkaline phosphatase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: phosphoric monoester]] | [[Category: phosphoric monoester]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 13:24:36 2007'' |
Revision as of 11:19, 30 October 2007
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ALKALINE PHOSPHATASE (D51ZN)
Overview
In each subunit of the homodimeric enzyme Escherichia coli alkaline, phosphatase, two of the three metal cofactors Zn2+ and Mg2+, are bound by, an aspartate side-chain at position 51. Using site-specific mutagenesis, Asp51 was mutated both to alanine and to asparagine to produce the D51A, and D51N enzymes, respectively. Over the range of pH values examined, the, D51A enzyme did not catalyze phosphate ester hydrolysis above non-enzymic, levels and was not activated by the addition of millimolar excess Zn2+ or, Mg2+. Replacement of Asp51 by asparagine, however, resulted in a mutant, enzyme with reduced activity and a higher pH optimum, compared with the, wild-type enzyme. At pH 8.0 the D51N enzyme showed about 1% of the, activity of the wild-type enzyme, and as the pH was raised to 9.2, ... [(full description)]
About this Structure
1URA is a [Single protein] structure of sequence from [Escherichia coli] with ZN and PO4 as [ligands]. Active as [Alkaline phosphatase], with EC number [3.1.3.1]. Structure known Active Sites: A and B. Full crystallographic information is available from [OCA].
Reference
Kinetic and structural consequences of replacing the aspartate bridge by asparagine in the catalytic metal triad of Escherichia coli alkaline phosphatase., Tibbitts TT, Murphy JE, Kantrowitz ER, J Mol Biol. 1996 Apr 5;257(3):700-15. PMID:8648634
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