The catalytically active form of histidinol dehydrogenase from Salmonella typhimurium.

The Biochemical journal ·Vol. 181 ·No. 3 ·1979-09-01 ·Pages 771-4

Bürger E, Görisch H, Lingens F

Abstract

The active-enzyme-sedimentation procedure was used to identify the catalytically competent form of histidinol dehydrogenase (EC 1.1.1.23) isolated from Salmonella typhimurium. At pH 9.4 the active species has a sedimentation coefficient S20,W of 5.4S, indicating that the dimer with a mol.wt. of approx. 83 000 is the enzymically active form.

MeSH Terms

Alcohol Oxidoreductases/metabolism Centrifugation, Density Gradient Histidinol Macromolecular Substances Salmonella typhimurium/enzymology

Chemicals

Macromolecular Substances Histidinol Alcohol Oxidoreductases

Authors & Affiliations

3 authors, click to expand affiliations / ORCID

Bürger E

Görisch H

Lingens F

References (15)

15 references, click to expand

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Article Info

Journal

The Biochemical journal

Abbr.

Biochem J

ISSN

0264-6021

DOI

10.1042/bj1810771

Published

1979-09-01

Pages

771-4

Language

English

Region

England

NLM ID

2984726R

PMCID

PMC1161219

Subset

External Links

PubMed source DOI: 10.1042/bj1810771 PMC Full Text View journal details

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The catalytically active form of histidinol dehydrogenase from Salmonella typhimurium.

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