Histidinol dehydrogenase

Histidinol dehydrogenase
the l-histidinol dehydrogenase (hisd) structure implicates domain swapping and gene duplication.
Identifiers
Symbol	Histidinol_dh
Pfam	PF00815
Pfam clan	CL0099
InterPro	IPR012131
PROSITE	PDOC00534
SCOP	1k75
SUPERFAMILY	1k75
Available protein structures: Pfam structures PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

In enzymology, a histidinol dehydrogenase (HIS4) (HDH) (EC 1.1.1.23) is an enzyme that catalyzes the chemical reaction

Thus, the two substrates of this enzyme are L-histidinol and NAD⁺, whereas its 3 products are L-histidine, NADH, and H⁺.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD⁺ or NADP⁺ as acceptor. The systematic name of this enzyme class is L-histidinol:NAD⁺ oxidoreductase. This enzyme is also called L-histidinol dehydrogenase.

Histidinol dehydrogenase catalyzes the terminal step in the biosynthesis of histidine in bacteria, fungi, and plants, the four-electron oxidation of L-histidinol to histidine.

In 4-electron dehydrogenases, a single active site catalyses 2 separate oxidation steps: oxidation of the substrate alcohol to an intermediate aldehyde; and oxidation of the aldehyde to the product acid, in this case His. The reaction proceeds via a tightly- or covalently-bound inter-mediate, and requires the presence of 2 NAD molecules. By contrast with most dehydrogenases, the substrate is bound before the NAD coenzyme. A Cys residue has been implicated in the catalytic mechanism of the second oxidative step.