Inhibition of the catalytic activity of human transaldolase by antibodies and site‐directed mutagenesis

FEBS Letters

Perl, Andras¹  Banki, Katalin² 

[1] Department of Medicine, State University of New York, College of Medicine, Syracuse, NY 13210, USA;Department of Pathology, State University of New York, College of Medicine, Syracuse, NY 13210, USA

关键词: Transaldolase;    Antibody-mediated inhibition;    Site-directed mutagenesis;    PPP;    pentose phosphate pathway;    TAL-H;    human transaldolase;    rTAL-H;    recombinant TAL-H;    mTAL-H;    mutant TAL-H;    GST;    glutathione S-transferase;   

DOI  :  10.1016/0014-5793(95)01446-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Transaldolase is a key enzyme of the pentose phosphate pathway. While antibody (Ab) 169, directed against the N-terminal 139 residues of human transaldolase (TAL-H), had no effect on enzyme activity, Ab 12484 raised against full length and functional recombinant TAL-H inhibited catalytic activity. This tentatively mapped the catalytic site to the C-terminal 140–336 amino acid portion of TAL-H. Dihydroxyacetone transfer reactions catalyzed by transaldolase depend on Schiff base formation by a lysine residue. Replacement of lysine-142 by glutamine using site-directed mutagenesis resulted in a complete loss of enzyme activity, suggesting that lysine-142 is essential for the catalytic activity of TAL-H.

【 授权许可】

Unknown