User:Cameron Evans/Sandbox 1
From Proteopedia
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| - | <scene name='User:Cameron_Evans/Sandbox_1/1bgv_spec_pocket/2'>The Specificity pocket of | + | <scene name='User:Cameron_Evans/Sandbox_1/1bgv_spec_pocket/2'>The Specificity pocket of ''Clostridium symbiosum'' GluDH</scene> is made up of polar interactions from K89 and S380 and hydrophobic interactions from G90, V377 and A163. The last three residues that make this interaction are highly conserved among amino acid dehydrogenases. <ref name="1bgv">PMID:8263917</ref> |
The polar residues make specific contacts with the glutamine substrate. | The polar residues make specific contacts with the glutamine substrate. | ||
Revision as of 03:49, 1 April 2010
Glutamate Dehydrogenase
Contents |
Prokaryote
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General Structure
Specificity
is made up of polar interactions from K89 and S380 and hydrophobic interactions from G90, V377 and A163. The last three residues that make this interaction are highly conserved among amino acid dehydrogenases. [1] The polar residues make specific contacts with the glutamine substrate.
Eukaryote
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References
- ↑ Stillman TJ, Baker PJ, Britton KL, Rice DW. Conformational flexibility in glutamate dehydrogenase. Role of water in substrate recognition and catalysis. J Mol Biol. 1993 Dec 20;234(4):1131-9. PMID:8263917 doi:http://dx.doi.org/10.1006/jmbi.1993.1665
