Literature summary for 1.1.1.23 extracted from

Barbosa, J.A.; Sivaraman, J.; Li, Y.; Larocque, R.; Matte, A.; Schrag, J.D.; Cygler, M.
Mechanism of action and NAD+-binding mode revealed by the crystal structure of L-histidinol dehydrogenase (2002), Proc. Natl. Acad. Sci. USA, 99, 1859-1864.

Cloned(Commentary)

Cloned (Comment)	Organism
gene hisD, expression as glutathione S-transferase fusion protein with a thrombin cleavage site between tag and enzyme	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
15.4 mg/ml purified recombinant detagged enzyme alone or complexed with L-histidinol, L-histamine, or L-histidine or Zn2+ and NAD+, in 20 mM Tris-HCl, pH 7.5, 0.2 M NaCl, 5 mM DTT, 1 mM ligand, hanging drop vapour diffusion method, 18°C, 0.002 ml protein solution with 0.004 ml reservoir solution, containing 20% w/v PEG 3350, 7% v/v glycerol, 0.1 M imidazole-malic acid, pH 5.5, 0.2 M ammonium sulfate, 2 weeks, macroseeding for larger crystals, transfer to sodium acetate, pH 5.5, to eliminate the inhibiting imidazole, X-ray diffraction structure determination and analysis at 2.2 A resolution, modelling	Escherichia coli

Crystallization (Comment)

Organism

15.4 mg/ml purified recombinant detagged enzyme alone or complexed with L-histidinol, L-histamine, or L-histidine or Zn2+ and NAD+, in 20 mM Tris-HCl, pH 7.5, 0.2 M NaCl, 5 mM DTT, 1 mM ligand, hanging drop vapour diffusion method, 18°C, 0.002 ml protein solution with 0.004 ml reservoir solution, containing 20% w/v PEG 3350, 7% v/v glycerol, 0.1 M imidazole-malic acid, pH 5.5, 0.2 M ammonium sulfate, 2 weeks, macroseeding for larger crystals, transfer to sodium acetate, pH 5.5, to eliminate the inhibiting imidazole, X-ray diffraction structure determination and analysis at 2.2 A resolution, modelling

Escherichia coli

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Zn2+	binding site structure	Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
L-histidinol + 2 NAD+ + H2O	Escherichia coli	part of L-histidine biosynthesis	L-histidine + 2 NADH + 2 H+	-	?

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P06988	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant enzyme fusion protein	Escherichia coli

Reaction

Reaction	Comment	Organism	Reaction ID
L-histidinol + 2 NAD+ + H2O = L-histidine + 2 NADH + 2 H+	reaction mechanism, amino acid residues Glu326 and His327 are involved in catalysis	Escherichia coli	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-histidinol + 2 NAD+ + H2O	part of L-histidine biosynthesis	Escherichia coli	L-histidine + 2 NADH + 2 H+	-	?
L-histidinol + NAD+	-	Escherichia coli	L-histidinal + NADH + H+	-	ir

Subunits

Subunits	Comment	Organism
dimer	dynamic light scattering	Escherichia coli

Synonyms

Synonyms	Comment	Organism
HisD	-	Escherichia coli

Cofactor

Cofactor	Comment	Organism	Structure
NAD+	binding site structure	Escherichia coli