scholarly journals Investigation on the Structure of the Active Site of Monoamine Oxidase-B by Affinity Labeling with the Selective Inhibitor Lazabemide and by Site-Directed Mutagenesis

1996 ◽  
Vol 236 (3) ◽  
pp. 996-1002 ◽  
Author(s):  
Andrea M. Cesura ◽  
Jurgen Gottowik ◽  
Hans-Werner Lahm ◽  
Gabrielle Lang ◽  
Rene Imhof ◽  
...  
Keyword(s):  
Monoamine Oxidase ◽  
Active Site ◽  
Selective Inhibitor ◽  
Site Directed Mutagenesis ◽  
Affinity Labeling ◽  
Directed Mutagenesis ◽  
Monoamine Oxidase B

Lys631 residue in the active site of the bacteriophage T7 RNA polymerase. Affinity labeling and site-directed mutagenesis

1991 ◽  
Vol 195 (3) ◽  
pp. 841-847 ◽  
Author(s):  
Tatyana G. MAKSIMOVA ◽  
Arkady A. MUSTAYEV ◽  
Evgeny F. ZAYCHIKOV ◽  
Dmitry L. LYAKHOV ◽  
Vera L. TUNITSKAYA ◽  
...  
Keyword(s):  
Rna Polymerase ◽  
Active Site ◽  
Site Directed Mutagenesis ◽  
T7 Rna Polymerase ◽  
Bacteriophage T7 ◽  
Affinity Labeling ◽  
Directed Mutagenesis

Identification of the active site residues in dipeptidyl peptidase IV by affinity labeling and site-directed mutagenesis

Biochemistry ◽  
1992 ◽  
Vol 31 (9) ◽  
pp. 2582-2587 ◽  
Author(s):  
Shigenori Ogata ◽  
Yoshio Misumi ◽  
Emiko Tsuji ◽  
Noboru Takami ◽  
Kimimitsu Oda ◽  
...  
Keyword(s):  
Active Site ◽  
Dipeptidyl Peptidase ◽  
Dipeptidyl Peptidase Iv ◽  
Site Directed Mutagenesis ◽  
Affinity Labeling ◽  
Directed Mutagenesis ◽  
Active Site Residues

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.

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