Literature summary for 1.1.1.95 extracted from

Dey, S.; Hu, Z.; Xu, X.L.; Sacchettini, J.C.; Grant, G.A.
The effect of hinge mutations on effector binding and domain rotation in Escherichia coli D-3-phosphoglycerate dehydrogenase (2007), J. Biol. Chem., 282, 18418-18426.

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Protein Variants

Protein Variants	Comment	Organism
G336V	changing glycine residues 336 and/or 337 to valine affect the sensitivity of the enzyme to inhibition by L-serine but not the extent of inhibition. The decrease in sensitivity is caused primarily by a decrease in the affinity of the enzyme for L-serine. The mutations also affect the domain rotation of the subunits in response to L-serine binding. Crystal structure of G336V demonstrates that the minimal effect of L-serine binding leading to inhibition of enzyme activity requires a domain rotation of approximately only 6° in just two of the four subunits of the enzyme that are oriented diagonally across from each other in the tetramer	Escherichia coli
G336V/G337V	changing glycine residues 336 and 337 to valine affect the sensitivity of the enzyme to inhibition by L-serine but not the extent of inhibition. The decrease in sensitivity is caused primarily by a decrease in the affinity of the enzyme for L-serine. The mutations also affect the domain rotation of the subunits in response to L-serine binding	Escherichia coli

Inhibitors

Inhibitors	Comment	Organism	Structure
L-serine	-	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0A9T0	-	-

Purification (Commentary)

Purification (Comment)	Organism
PGDH is expressed in Escherichia coli and purified using 5'-AMP-Sepharose affinity chromatography	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
alpha-ketoglutarate + NADH	-	Escherichia coli	2-hydroxyglutaric acid + NAD+	-	?

Synonyms

Synonyms	Comment	Organism
3-phosphoglycerate dehydrogenase	-	Escherichia coli
PGDH	-	Escherichia coli

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Release 2023.1 (January 2023)