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

Biochemistry ◽  
1995 ◽  
Vol 34 (38) ◽  
pp. 12426-12434 ◽  
Author(s):  
V. Lauvergeat ◽  
K. Kennedy ◽  
C. Feuillet ◽  
J. H. McKie ◽  
L. Gorrichon ◽  
...  
Keyword(s):  
Alcohol Dehydrogenase ◽  
Cinnamyl Alcohol Dehydrogenase ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Cinnamyl Alcohol ◽  
Serine Residue

Site-directed mutagenesis of glycine-14 and two "critical" cysteinyl residues in Drosophila alcohol dehydrogenase

Biochemistry ◽  
1990 ◽  
Vol 29 (5) ◽  
pp. 1112-1118 ◽  
Author(s):  
Zhuo Chen ◽  
Ling Lu ◽  
Michelle Shirley ◽  
William R. Lee ◽  
Simon H. Chang
Keyword(s):  
Alcohol Dehydrogenase ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis

scholarly journals Threonine 57 is required for the post-translational activation ofEscherichia coliaspartate α-decarboxylase

2014 ◽  
Vol 70 (4) ◽  
pp. 1166-1172 ◽  
Author(s):  
Michael E. Webb ◽  
Briony A. Yorke ◽  
Tom Kershaw ◽  
Sarah Lovelock ◽  
Carina M. C. Lobley ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Active Site ◽  
Site Directed Mutagenesis ◽  
Intramolecular Rearrangement ◽  
Directed Mutagenesis ◽  
Vitamin B ◽  
Biosynthesis Pathway ◽  
Serine Residue ◽  
Translational Activation

Aspartate α-decarboxylase is a pyruvoyl-dependent decarboxylase required for the production of β-alanine in the bacterial pantothenate (vitamin B5) biosynthesis pathway. The pyruvoyl group is formedviathe intramolecular rearrangement of a serine residue to generate a backbone ester intermediate which is cleaved to generate an N-terminal pyruvoyl group. Site-directed mutagenesis of residues adjacent to the active site, including Tyr22, Thr57 and Tyr58, reveals that only mutation of Thr57 leads to changes in the degree of post-translational activation. The crystal structure of the site-directed mutant T57V is consistent with a non-rearranged backbone, supporting the hypothesis that Thr57 is required for the formation of the ester intermediate in activation.

Comparative efficiency of different constructs for down regulation of tobacco cinnamyl alcohol dehydrogenase

1998 ◽  
Vol 49 (2) ◽  
pp. 295-306 ◽  
Author(s):  
Nabila Yahiaoui, Christiane Marque ◽  
Hélène Corbière ◽  
Alain Michel Boudet
Keyword(s):  
Alcohol Dehydrogenase ◽  
Cinnamyl Alcohol Dehydrogenase ◽  
Cinnamyl Alcohol ◽  
Down Regulation ◽  
Comparative Efficiency
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