Acid-Base Catalyst Discriminates between a Fructose 6-Phosphate Aldolase and a Transaldolase-Reference-Cited by-同舟云学术

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Acid-Base Catalyst Discriminates between a Fructose 6-Phosphate Aldolase and a Transaldolase

Published:2015-08-06 Issue:19 Volume:7 Page:3140-3151
ISSN:1867-3880
Container-title:ChemCatChem
language:en
Short-container-title:ChemCatChem

Author:

Stellmacher Lena¹,Sandalova Tatyana²,Leptihn Sebastian³,Schneider Gunter⁴,Sprenger Georg A.¹,Samland Anne K.¹

Affiliation:

1. Institut für Mikrobiologie; Universität Stuttgart; Allmandring 31 70550 Stuttgart Germany

2. Science for Life Laboratory, Department of Medicine, Solna; Karolinska Institutet; 17165 Stockholm Sweden

3. Institut für Mikrobiologie; Universität Hohenheim; Garbenstrasse 30 70599 Stuttgart Germany

4. Department of Medical Biochemistry and Biophysics; Karolinska Institutet; 17177 Stockholm Sweden

Funder

Karolinska Institutet

Deutsche Forschungsgemeinschaft (DFG)

Erwin-Riesch-Stiftung, Tübingen

Swedish Science Council

Publisher

Wiley

Subject

Inorganic Chemistry,Organic Chemistry,Physical and Theoretical Chemistry,Catalysis

Reference54 articles.

1. Transaldolase: From biochemistry to human disease

2. The Transaldolase Family: New Synthetic Opportunities from an Ancient Enzyme Scaffold

3. Fructose-6-phosphate Aldolase Is a Novel Class I Aldolase from Escherichia coli and Is Related to a Novel Group of Bacterial Transaldolases

4. FSAB: A new fructose-6-phosphate aldolase from Escherichia coli. Cloning, over-expression and comparative kinetic characterization with FSAA

5. Transaldolase B of Escherichia coli K-12: cloning of its gene, talB, and characterization of the enzyme from recombinant strains

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