Literature summary for 1.1.1.95 extracted from

Liberles, J.S.; Thorolfsson, M.; Martinez, A.
Allosteric mechanisms in ACT domain containing enzymes involved in amino acid metabolism (2005), Amino Acids, 28, 1-12.

Search for more literature for 1.1.1.95

Inhibitors

Inhibitors	Comment	Organism	Structure
L-serine	feedback regulation, positive and negative cooperativity in absence of NADH, positive in presence of NADH, overview	Escherichia coli
additional information	the enzyme contains an ACT domain, which is involved in the allosteric regulation mechanism	Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
3-phospho-D-glycerate + NAD+	Escherichia coli	first step in biosynthesis of L-serine, the enzyme contains an ACT domain, which is involved in the allosteric regulation mechanism, residue W139 is involved	3-phosphohydroxypyruvate + NADH	-	?

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0A9T0	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
3-phospho-D-glycerate + NAD+	first step in biosynthesis of L-serine, the enzyme contains an ACT domain, which is involved in the allosteric regulation mechanism, residue W139 is involved	Escherichia coli	3-phosphohydroxypyruvate + NADH	-	?
3-phospho-D-glycerate + NAD+	D-isomer-specific	Escherichia coli	3-phosphohydroxypyruvate + NADH	-	?

Subunits

Subunits	Comment	Organism
More	the enzyme contains an ACT domain, which is involved in the allosteric regulation mechanism	Escherichia coli

Synonyms

Synonyms	Comment	Organism
3PGDH	-	Escherichia coli
More	the enzyme belongs to the D-isomer-specific 2-hydroxyacid dehydrogenase family	Escherichia coli

Cofactor

Cofactor	Comment	Organism	Structure
NAD+	cofactor binding structure	Escherichia coli

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Release 2023.1 (January 2023)