1pjb

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(New page: 200px<br /><applet load="1pjb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pjb, resolution 2.1&Aring;" /> '''L-ALANINE DEHYDROGENA...)
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'''L-ALANINE DEHYDROGENASE'''<br />
'''L-ALANINE DEHYDROGENASE'''<br />
==Overview==
==Overview==
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The structure of the hexameric L-alanine dehydrogenase from Phormidium, lapideum reveals that the subunit is constructed from two domains, each, having the common dinucleotide binding fold. Despite there being no, sequence similarity, the fold of alanine dehydrogenase is closely related, to that of the family of D-2-hydroxyacid dehydrogenases, with a similar, location of the active site, suggesting that these enzymes are related by, divergent evolution. L-alanine dehydrogenase and the 2-hydroxyacid, dehydrogenases also use equivalent functional groups to promote substrate, recognition and catalysis. However, they are arranged differently on the, enzyme surface, which has the effect of directing opposite faces of the, keto acid to the dinucleotide in each case, forcing a change in absolute, configuration of the product.
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The structure of the hexameric L-alanine dehydrogenase from Phormidium lapideum reveals that the subunit is constructed from two domains, each having the common dinucleotide binding fold. Despite there being no sequence similarity, the fold of alanine dehydrogenase is closely related to that of the family of D-2-hydroxyacid dehydrogenases, with a similar location of the active site, suggesting that these enzymes are related by divergent evolution. L-alanine dehydrogenase and the 2-hydroxyacid dehydrogenases also use equivalent functional groups to promote substrate recognition and catalysis. However, they are arranged differently on the enzyme surface, which has the effect of directing opposite faces of the keto acid to the dinucleotide in each case, forcing a change in absolute configuration of the product.
==About this Structure==
==About this Structure==
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1PJB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Phormidium_lapideum Phormidium lapideum]. Active as [http://en.wikipedia.org/wiki/Alanine_dehydrogenase Alanine dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.1.1 1.4.1.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PJB OCA].
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1PJB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Phormidium_lapideum Phormidium lapideum]. Active as [http://en.wikipedia.org/wiki/Alanine_dehydrogenase Alanine dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.1.1 1.4.1.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PJB OCA].
==Reference==
==Reference==
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[[Category: Phormidium lapideum]]
[[Category: Phormidium lapideum]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Baker, P.J.]]
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[[Category: Baker, P J.]]
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[[Category: Rice, D.W.]]
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[[Category: Rice, D W.]]
[[Category: Sawa, Y.]]
[[Category: Sawa, Y.]]
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[[Category: Sedelnikova, S.E.]]
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[[Category: Sedelnikova, S E.]]
[[Category: Shibata, H.]]
[[Category: Shibata, H.]]
[[Category: nad]]
[[Category: nad]]
[[Category: oxidoreductase]]
[[Category: oxidoreductase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 02:35:07 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:29:21 2008''

Revision as of 12:29, 21 February 2008


1pjb, resolution 2.1Å

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L-ALANINE DEHYDROGENASE

Overview

The structure of the hexameric L-alanine dehydrogenase from Phormidium lapideum reveals that the subunit is constructed from two domains, each having the common dinucleotide binding fold. Despite there being no sequence similarity, the fold of alanine dehydrogenase is closely related to that of the family of D-2-hydroxyacid dehydrogenases, with a similar location of the active site, suggesting that these enzymes are related by divergent evolution. L-alanine dehydrogenase and the 2-hydroxyacid dehydrogenases also use equivalent functional groups to promote substrate recognition and catalysis. However, they are arranged differently on the enzyme surface, which has the effect of directing opposite faces of the keto acid to the dinucleotide in each case, forcing a change in absolute configuration of the product.

About this Structure

1PJB is a Single protein structure of sequence from Phormidium lapideum. Active as Alanine dehydrogenase, with EC number 1.4.1.1 Full crystallographic information is available from OCA.

Reference

Analysis of the structure and substrate binding of Phormidium lapideum alanine dehydrogenase., Baker PJ, Sawa Y, Shibata H, Sedelnikova SE, Rice DW, Nat Struct Biol. 1998 Jul;5(7):561-7. PMID:9665169

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