Structural and Kinetic Studies on Native Intermediates and an Intermediate Analogue in Benzoylformate Decarboxylase Reveal a Least Motion Mechanism with an Unprecedented Short-Lived Predecarboxylation Intermediate-Reference-Cited by-同舟云学术

Structural and Kinetic Studies on Native Intermediates and an Intermediate Analogue in Benzoylformate Decarboxylase Reveal a Least Motion Mechanism with an Unprecedented Short-Lived Predecarboxylation Intermediate

Published:2009-03-25 Issue:15 Volume:48 Page:3258-3268
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Bruning Marc¹,Berheide Marco¹,Meyer Danilo¹,Golbik Ralph¹,Bartunik Hans¹,Liese Andreas¹,Tittmann Kai¹

Affiliation:

1. Institute of Technical Biocatalysis, Hamburg University of Technology, Denickestrasse 15, D-21073 Hamburg, Germany, Albrecht-von-Haller-Institute and Göttingen Center for Molecular Biosciences, Georg-August-University Göttingen, Ernst-Caspari-Haus, Justus-von-Liebig-Weg 11, D-37077 Göttingen, Germany, Institute of Biochemistry and Biotechnology, Martin-Luther-University Halle-Wittenberg, Kurt-Mothes-Strasse 3, D-06120 Halle/Saale, Germany, and Max-Planck-Gesellschaft, Arbeitsgruppen für strukturelle...

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi801957d

Reference43 articles.

1. THE ENZYMATIC CONVERSION OF MANDELIC ACID TO BENZOIC ACID I

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3. Synthesis of the Enzymes of the Mandelate Pathway by Pseudomonas putida II. Isolation and Properties of Blocked Mutants

4. Synthesis of the Enzymes of the Mandelate Pathway by Pseudomonas putida III. Isolation and Properties of Constitutive Mutants

5. Mandelic acid racemase from Pseudomonas putida. Purification and properties of the enzyme

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