Double Duty for a Conserved Glutamate in Pyruvate Decarboxylase: Evidence of the Participation in Stereoelectronically Controlled Decarboxylation and in Protonation of the Nascent Carbanion/Enamine Intermediate,-Reference-Cited by-同舟云学术

Double Duty for a Conserved Glutamate in Pyruvate Decarboxylase: Evidence of the Participation in Stereoelectronically Controlled Decarboxylation and in Protonation of the Nascent Carbanion/Enamine Intermediate,

Published:2010-08-25 Issue:37 Volume:49 Page:8197-8212
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Meyer Danilo¹²,Neumann Piotr²,Parthier Christoph²,Friedemann Rudolf³,Nemeria Natalia⁴,Jordan Frank⁴,Tittmann Kai¹²

Affiliation:

1. Albrecht-von-Haller-Institute for Plant Sciences and Göttingen Center for Molecular Biosciences, Georg-August-University Göttingen, Ernst-Caspari-Haus, Justus-von-Liebig-Weg 11, D-37077 Göttingen, Germany

2. Institute of Biochemistry and Biotechnology, Martin-Luther-University Halle-Wittenberg, Kurt-Mothes-Strasse 3, D-06120 Halle/Saale, Germany

3. Institute of Organic Chemistry, Martin-Luther-University Halle-Wittenberg, Kurt-Mothes-Strasse 3, D-06120 Halle/Saale, Germany

4. Department of Chemistry, Rutgers University, Newark, New Jersey 07102

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi100828r

Reference43 articles.

1. Structure and properties of pyruvate decarboxylase and site-directed mutagenesis of the Zymomonas mobilis enzyme

2. Pyruvate decarboxylase: a key enzyme for the oxidative metabolism of lactic acid by Acetobacter pasteurianus