1pjb
From Proteopedia
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'''L-ALANINE DEHYDROGENASE''' | '''L-ALANINE DEHYDROGENASE''' | ||
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[[Category: Sedelnikova, S E.]] | [[Category: Sedelnikova, S E.]] | ||
[[Category: Shibata, H.]] | [[Category: Shibata, H.]] | ||
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| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:08:55 2008'' | |
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Revision as of 02:08, 3 May 2008
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. 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 Sat May 3 05:08:55 2008
