Site-Directed Mutagenesis of a Serine Residue in Cinnamyl Alcohol Dehydrogenase, a Plant NADPH-Dependent Dehydrogenase, Affects the Specificity for the Coenzyme-Reference-Cited by-同舟云学术

Site-Directed Mutagenesis of a Serine Residue in Cinnamyl Alcohol Dehydrogenase, a Plant NADPH-Dependent Dehydrogenase, Affects the Specificity for the Coenzyme

Published:1995-09-26 Issue:38 Volume:34 Page:12426-12434
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Lauvergeat V.,Kennedy K.,Feuillet C.,McKie J. H.,Gorrichon L.,Baltas M.,Boudet A. M.,Grima-Pettenati J.,Douglas K. T.

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi00038a041

Reference46 articles.

1. Sulphinamoylacetates as sulphine precursors. Mechanism of basic hydrolysis and scheme of irreversible inactivation of cinnamoyl alcohol dehydrogenase, an enzyme of the lignification process

2. Creation of an NADP-dependent pyruvate dehydrogenase multienzyme complex by protein engineering

3. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

4. Role of aspartic acid 38 in the cofactor specificity of Drosophila alcohol dehydrogenase

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