Literature summary for 1.4.1.4 extracted from

deLuna, A.; Quezada, H.; Gomez-Puyou, A.; Gonzalez, A.
Asparaginyl deamidation in two glutamate dehydrogenase isoenzymes from Saccharomyces cerevisiae (2005), Biochem. Biophys. Res. Commun., 328, 1083-1090.

Search for more literature for 1.4.1.4

General Stability

General Stability	Organism
Gdh3-encoded enzyme undergoes in vitro deamination at a particular asparaginyl residue which is absent in homologous isoenzyme, Gdh1p. Deamination of Asn54 is observed in vitro when Gdh3p is incubated at alkaline pH. The specific deamination of Asn54, could account, in part, for the relative lower stability of the GDH3-encoded protein	Saccharomyces cerevisiae

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	-	-	-

Synonyms

Synonyms	Comment	Organism
NADP-glutamate dehydrogenase	two isoenzymes: Gdh3P and Gdh1p	Saccharomyces cerevisiae

pH Stability

pH Stability	pH Stability Maximum	Comment	Organism
additional information	-	Gdh3-encoded enzyme undergoes in vitro deamination at a particular asparaginyl residue which is absent in homologous isoenzyme, Gdh1p. Deamination of Asn54 is observed in vitro when Gdh3p is incubated at alkaline pH. The specific deamination of Asn54, could account, in part, for the relative lower stability of the GDH3-encoded protein	Saccharomyces cerevisiae

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Release 2023.1 (January 2023)