Literature summary 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)
EC Number |
Cloned (Comment) |
Organism |
---|
1.1.1.23 |
gene hisD, expression as glutathione S-transferase fusion protein with a thrombin cleavage site between tag and enzyme |
Escherichia coli |
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
1.1.1.23 |
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
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
1.1.1.23 |
Zn2+ |
binding site structure |
Escherichia coli |
|
Natural Substrates/ Products (Substrates)
EC Number |
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
---|
1.1.1.23 |
L-histidinol + 2 NAD+ + H2O |
Escherichia coli |
part of L-histidine biosynthesis |
L-histidine + 2 NADH + 2 H+ |
- |
? |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
1.1.1.23 |
Escherichia coli |
P06988 |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
1.1.1.23 |
recombinant enzyme fusion protein |
Escherichia coli |
Reaction
EC Number |
Reaction |
Comment |
Organism |
Reaction ID |
---|
1.1.1.23 |
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 |
|
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
1.1.1.23 |
L-histidinol + 2 NAD+ + H2O |
part of L-histidine biosynthesis |
Escherichia coli |
L-histidine + 2 NADH + 2 H+ |
- |
? |
|
1.1.1.23 |
L-histidinol + NAD+ |
- |
Escherichia coli |
L-histidinal + NADH + H+ |
- |
ir |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
1.1.1.23 |
dimer |
dynamic light scattering |
Escherichia coli |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
1.1.1.23 |
HisD |
- |
Escherichia coli |
Cofactor
EC Number |
Cofactor |
Comment |
Organism |
Structure |
---|
1.1.1.23 |
NAD+ |
binding site structure |
Escherichia coli |
|