Literature summary for 1.17.1.8 extracted from

Ge, X.; Olson, A.; Cai, S.; Sem, D.S.
Binding synergy and cooperativity in dihydrodipicolinate reductase: implications for mechanism and the design of biligand inhibitors (2008), Biochemistry, 47, 9966-9980.

Activating Compound

Activating Compound	Comment	Organism	Structure
NADH	-	Escherichia coli
NADPH	similar affinity as NADH	Escherichia coli

Application

Application	Comment	Organism
drug development	enzyme is a potential target for new antimicrobial and herbicidal compounds	Escherichia coli

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli (BL21)	Escherichia coli
expression of pET11a expression construct in Escherichia coli (BL21)	Escherichia coli

Inhibitors

Inhibitors	Comment	Organism	Structure
2,6-pyridine dicarboxylate	stable analog of the dihydrodipicolinate substrate, the binding affinity is not affected by the presence of NADH or NAD+	Escherichia coli
catechol rhodanine acetic acid	binds to the NADH cofactor site	Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
28000	-	SDS-PAGE	Escherichia coli
28820	-	by MALDI-TOF mass spectrometry	Escherichia coli
28820	-	MALDI-TOF, 28756 Da expected	Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
2,3-dihydrodipicolinate + NAD(P)H	Escherichia coli	enzyme is a part of the biosynthetic pathway leading to meso-diaminopimelic acid and L-lysine in bacteria and higher plants	2,3,4,5-tetrahydrodipicolinate + NAD(P)+	-	?
dihydrodipicolinate + NADH + H+	Escherichia coli	substrate dihydrodipicolinate is instable	tetrahydrodipicolinate + NAD+	-	?

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
cells grown in M9 medium containing 2H, 15N, and 13C-labeled sources, collected, lysed, and protein purified with a QA52 anion exchange column and a Blue Trisacryl affinity column with gravity gradient chromatography, fractions with activity pooled and concentrated using an Amicon ultrafiltration device with YM10 membrane, desalted and loaded onto the Blue Trisacryl affinity column and eluted with a linear gradient of 0-2 M NaCl, 25 mM Tris buffer, pH 7.5, pooled, concentrated and buffer ecxchanged	Escherichia coli
protein is purified using a QA52 anion exchange column and a Blue Trisacryl affinity column with gravity gradient chromatography	Escherichia coli

Purification (Comment)

Organism

cells grown in M9 medium containing 2H, 15N, and 13C-labeled sources, collected, lysed, and protein purified with a QA52 anion exchange column and a Blue Trisacryl affinity column with gravity gradient chromatography, fractions with activity pooled and concentrated using an Amicon ultrafiltration device with YM10 membrane, desalted and loaded onto the Blue Trisacryl affinity column and eluted with a linear gradient of 0-2 M NaCl, 25 mM Tris buffer, pH 7.5, pooled, concentrated and buffer ecxchanged

Escherichia coli

protein is purified using a QA52 anion exchange column and a Blue Trisacryl affinity column with gravity gradient chromatography

Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
2,3-dihydrodipicolinate + NAD(P)H	enzyme is a part of the biosynthetic pathway leading to meso-diaminopimelic acid and L-lysine in bacteria and higher plants	Escherichia coli	2,3,4,5-tetrahydrodipicolinate + NAD(P)+	-	?
dihydrodipicolinate + NADH + H+	substrate dihydrodipicolinate is instable	Escherichia coli	tetrahydrodipicolinate + NAD+	-	?
pyridine dicarboxylate + NADH + H+	stable substrate analog, 25 mM phosphate D2O (deuterium water) buffer, pH 7.8 for NMR analysis of binding interactions with saturation transfer difference titration studies at 298 K (25°C)	Escherichia coli	reduced pyridine dicarboxylate + NAD+	-	?

Subunits

Subunits	Comment	Organism
homotetramer	native state	Escherichia coli

Synonyms

Synonyms	Comment	Organism
DHPR	-	Escherichia coli
dihydrodipicolinate reductase	-	Escherichia coli

Cofactor

Cofactor	Comment	Organism	Structure
NADH	dihydrodipicolinate reductase activity requires NADH binding at only one of the four monomers	Escherichia coli
NADPH	-	Escherichia coli

General Information

General Information	Comment	Organism
metabolism	part of the biosynthetic pathway leading to meso-diaminopimelic acid and L-lysine, only NADH binding at one of the 4 monomers is required to activate the dihydrodipicolinate reductase, a model of sequential conformational change in each monomer upon NADH binding is proposed	Escherichia coli