Literature summary for 1.4.1.3 extracted from

Nassar, O.; Li, C.; Stanley, C.; Pettitt, B.; Smith, T.
Glutamate dehydrogenase Structure of a hyperinsulinism mutant, corrections to the atomic model, and insights into a regulatory site (2019), Proteins, 87, 41-50 .

Search for more literature for 1.4.1.3

Crystallization (Commentary)

Crystallization (Comment)	Organism
mutant H454Y, to 2.7 A resolution, and comparison with human GDH	Bos taurus

Protein Variants

Protein Variants	Comment	Organism
HH454Y	mutation causes the hyperinsulinism/hyperammonemia syndrome (HHS) where insulin is hypersecreted upon consumption of protein due to loss of GLZD1 function. Mutation lies in the GTP binding pocket	Bos taurus

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
mitochondrion	-	Bos taurus	5739	-

Organism

Organism	UniProt	Comment	Textmining
Bos taurus	P00366	-	-

Synonyms

Synonyms	Comment	Organism
GLUD1	-	Bos taurus

General Information

General Information	Comment	Organism
metabolism	the original published sequence of bovine GDH contains a few mistakes. Lysine is the correct amino acid identity of residue 387 in the allosteric NADH binding site, not asparagine. The thermodynamic impact of this mistake is shown to be +5 kcal/mol per NADH binding site. Four other residues are corrected in the bovine GDH sequence, specifically G47S, A248V, V271I, and A272T. Allostery at site R459 depends upon the expansion and contraction between subunits within the trimer as the catalytic site closes and opens, respectively	Bos taurus

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Release 2023.1 (January 2023)