PROSITE documentation PDOC00534

Histidinol dehydrogenase signature




Description

Histidinol dehydrogenase (EC 1.1.1.23) (HDH) catalyzes the terminal step in the biosynthesis of histidine in bacteria, fungi, and plants, the four-electron oxidation of L-histidinol to histidine.

In bacteria HDH is a single chain polypeptide; in fungi it is the C-terminal domain of a multifunctional enzyme which catalyzes three different steps of histidine biosynthesis; and in plants it is expressed as nuclear encoded protein precursor which is exported to the chloroplast [1].

As a signature pattern we selected a highly conserved region located in the central part of HDH. This region does not correspond to the part of the enzyme that, in most, but not all HDH sequences contains a cysteine residue which, in Salmonella typhimurium, has been said [2] to be important for the catalytic activity of the enzyme.

Last update:

April 2006 / Pattern revised.

Technical section

PROSITE method (with tools and information) covered by this documentation:

HISOL_DEHYDROGENASE, PS00611; Histidinol dehydrogenase signature  (PATTERN)


References

1AuthorsNagai A., Ward E., Beck J., Tada S., Chang J.-Y., Scheidegger A., Ryals J.
TitleStructural and functional conservation of histidinol dehydrogenase between plants and microbes.
SourceProc. Natl. Acad. Sci. U.S.A. 88:4133-4137(1991).
PubMed ID2034659

2AuthorsGrubmeyer C.T., Gray W.R.
TitleA cysteine residue (cysteine-116) in the histidinol binding site of histidinol dehydrogenase.
SourceBiochemistry 25:4778-4784(1986).
PubMed ID3533140



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