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Your search keyword '"Pseudomonas putida -- Physiological aspects"' showing total 3 results
Start Over Descriptor "Pseudomonas putida -- Physiological aspects" Journal journal of the american chemical society
3 results on '"Pseudomonas putida -- Physiological aspects"'

1. Stereospecific ketonization of 2-hydroxymuconate by 4-oxalocrotonate tautomerase and 5-(carboxymethyl)-2-hydroxymuconate isomerase

Author

Whitman, Christian P., Hajipour, Gholamhossein, Watson, Robert J., Johnson, William H., Jr., Bembenek, Michael E., and Stolowich, Neal J.

Subjects
Ketones -- Research, Microbial enzymes -- Research, Pseudomonas putida -- Physiological aspects, Chemistry
Abstract

The stereospecificity of 4-oxalocrotonate tautomerase from Pseudomonas putida mt-2 and 5-(carboxymethyl)-2-hydroxymuconate isomerase from Escherichia coli C was determined. The product, 2-oxo-3-(E)-hexenedioate was trapped and processed to (2-2H1)glutaric acid by chemical degradative procedures. It was found that both enzymes ketonize 2-hydroxymuconate stereospecifically to (S)-2-oxo-3-(E)-(5-2H1)hexenedioate.

Published
1992

2. Solvation response along the reaction coordinate in the active site of ketosteroid isomerase

Author

Childs, William and Boxer, Steven G.

Subjects
Catalysis -- Analysis, Coumarins -- Chemical properties, Coumarins -- Electric properties, Electrostatic interactions -- Analysis, Pseudomonas putida -- Physiological aspects, Solvation -- Analysis, Chemistry
Abstract

Several studies are conducted to explain the protein salvation response observed along the reaction coordinate present in the active site of ketosteroid isomerase. The catalytic cycle is shown to have no impact on the electrostatic environment of the active site.

Published
2010

3. Active-site engineering of benzaldehyde lyase shows that a point mutation can confer both new reactivity and susceptibility to mechanism-based inhibition

Author

Brandt, Gabriel S., Kneen, Malea M., Petsko, Gregory A., Ringe, Dagmar, and McLeish, Michael J.

Subjects
Decarboxylases -- Chemical properties, Gene mutations -- Analysis, Phosphates -- Chemical properties, Phosphates -- Structure, Pseudomonas putida -- Genetic aspects, Pseudomonas putida -- Physiological aspects, Benzene -- Chemical properties, Benzene -- Structure, Chemistry
Abstract

A point mutant, benzaldehyde lyase (BAL) from Pseudomonas putida A28S which is able to catalyze the decarboxylation of benzoylformate and is inactivated by the benzoylformate analogues methyl benzoylphosphonate (MBP) and benzoylphosphonate (BP), similar to benzoylformate decarboxylase (BFDC) is reported. The findings suggested that an appropriately placed nucleophile facilitated the expulsion of carbon dioxide from the active site in many thiamin diphosphate (ThDP-dependent decarboxylases.

Published
2010

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