Replacement of a Phenylalanine by a Tyrosine in the Active Site Confers Fructose-6-phosphate Aldolase Activity to the Transaldolase of Escherichia coli and Human Origin-Reference-Cited by-同舟云学术

Replacement of a Phenylalanine by a Tyrosine in the Active Site Confers Fructose-6-phosphate Aldolase Activity to the Transaldolase of Escherichia coli and Human Origin

Published:2008-10 Issue:44 Volume:283 Page:30064-30072
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Schneider Sarah,Sandalova Tatyana,Schneider Gunter,Sprenger Georg A.,Samland Anne K.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference46 articles.

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

2. Transaldolase B: Trapping of Schiff Base Intermediate between Dihydroxyacetone and ε-Amino Group of Active-Site Lysine Residue by Borohydride Reduction

3. Disruption of Escherichia coli transaldolase into catalytically active monomers: evidence against half-of-the-sites mechanism

4. Identification of catalytically important residues in the active site ofEscherichia colitransaldolase

5. Crystal structure of transaldolase B from Escherichia coli suggests a circular permutation of the α/β barrel within the class I aldolase family

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