Histidinol dehydrogenase loses its catalytic function through the mutation of His261-->Asn due to its inability to ligate the essential Zn.

Abstract:

:Histidinol dehydrogenase (HDH), a Zn-metalloenzyme, produces His from histidinol through two successive oxidation reactions with NAD+ as a coenzyme. A mutation, His261-->Asn, caused the complete loss of the Zn, thereby inactivating the enzyme, without significant structural perturbation. The ability to oxidize an intermediate, histidinaldehyde, was restored to about 4% of that of the wild-type enzyme by adding 0.5 mM MnCl2, whereas the histidinol oxidation activity could not be recovered with the mental addition. We concluded that the His residue at position 261 is essential for the ligation of the Zn of cabbage HDH.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Nagai A,Ohta D

doi

10.1093/oxfordjournals.jbchem.a124298

subject

Has Abstract

pub_date

1994-01-01 00:00:00

pages

22-5

issue

1

eissn

0021-924X

issn

1756-2651

journal_volume

115

pub_type

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