Histidinol dehydrogenase

From Wikipedia, the free encyclopedia

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

L-histidinol + 2 NAD⁺ $\rightleftharpoons$ L-histidine + 2 NADH + 2 H⁺

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. This enzyme participates in histidine metabolism.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 1K75, 1KAE, 1KAH, and 1KAR.

[edit] References

IUBMB entry for 1.1.1.23
BRENDA references for 1.1.1.23 (Recommended.)
PubMed references for 1.1.1.23
PubMed Central references for 1.1.1.23
Google Scholar references for 1.1.1.23
Adams E (1954). "Enzymatic synthesis of histidine from histidinol". J. Biol. Chem. 209: 829–846.
Adams E (1955). "L-Histidinal, a biosynthetic precursor of histidine". J. Biol. Chem. 217: 325–344.
Yourno J, Ino I (1968). "Purification and crystallization of histidinol dehydrogenase from Salmonella typhimurium LT-2". J. Biol. Chem. 243: 3273–6. PMID 4872177.
Loper JC (1968). "Histidinol dehydrogenase from Salmonella typhimurium Crystallization and composition studies". J. Biol. Chem. 243: 3264–72. PMID 4872176.