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Glutamate Dehydrogenase

Contents 1 Prokaryote 1.1 General Structure 1.2 Specificity 1.3 Allosteric Interactions 2 Eukaryote 2.1 General Structure 2.2 Specificity 2.3 Allosteric Interactions 3 References

Prokaryote

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General Structure

Prokaryotic glutamate dehydrogenase (GDH) does not have any common quaternary structure among crystallized structures (1EUZ is a hexamer, 1HRD a trimer); however, every prokaryotic structure so far elucidated shows a common overall tertiary structure.^[1]

Each monomer (reguardless of quaternary structure) has two domains: a domain that is a variant of the Rossmann dinucleotide binding fold (), and a domain involved in oligomerization (when it occurs) and contains most of the substrate binding residues (). ^[1]

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.

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Domain II is in Blue and Domain I is in Purple

Allosteric Interactions

Eukaryote

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General Structure

Specificity

Allosteric Interactions

References

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1. ↑ ^{1.0 1.1 1.2} 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