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 2.1Å" /> '''L-ALANINE DEHYDROGENA...)
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Revision as of 00:27, 25 November 2007
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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
Page seeded by OCA on Sun Nov 25 02:35:07 2007
