AbstractThe effect of p-hydroxyphenylpyruvate, a natural analogue of transketolase substrate, on the catalytic activity of the enzyme was investigated. p-Hydroxyphenylpyruvate proved to be a reversible and competitive inhibitor of transketolase with respect to substrate; it was also able to displace thiamine diphosphate from holotransketolase. The data suggest that p-hydroxyphenylpyruvate participates in the regulation of tyrosine biosynthesis by influencing the catalytic activity of transketolase
A structural model for thiamine‐diphosphate (ThDP)‐dependent transketolase (TK) was developed to ana...
Enzymes catalyzing asymmetric carboligation reactions typically show very high specificity for their...
AbstractThe mechanism of regulatory phosphorylation of the pyruvate dehydrogenase component (E1) of ...
AbstractThe effect of p-hydroxyphenylpyruvate, a natural analogue of transketolase substrate, on the...
The enzyme transketolase is found in nature as part of the Pentose Phosphate Pathway to rearrange la...
AbstractHere we summarize evidence for non-equivalence of two structurally similar active sites in t...
AbstractTransketolase catalyzes the transfer of an aldehyde residue from keto sugars to aldo sugars....
AbstractPhosphorylation of the pyruvate dehydrogenase component (E1) of the muscle pyruvate dehydrog...
AbstractData from site-directed mutagenesis and X-ray crystallography show that His103 of holotransk...
Transketolase (TK) is an important metabolic enzyme in all organisms. The enantioselective carbon-ca...
The enzyme transketolase is found in nature as part of the Pentose Phosphate Pathway to rearrange la...
This review highlights recent research on the properties and functions of the enzyme transketolase, ...
The enzyme transketolase (TK; E.C. 2.2.1.1) from Escherichia coli occupies a pivotal place in metabo...
In previous studies' with a dialyzed supernatant fraction from rat liver it was observed that the fo...
The molecule of transketolase is a dimer with structurally and functionally identical subunits. Its ...
A structural model for thiamine‐diphosphate (ThDP)‐dependent transketolase (TK) was developed to ana...
Enzymes catalyzing asymmetric carboligation reactions typically show very high specificity for their...
AbstractThe mechanism of regulatory phosphorylation of the pyruvate dehydrogenase component (E1) of ...
AbstractThe effect of p-hydroxyphenylpyruvate, a natural analogue of transketolase substrate, on the...
The enzyme transketolase is found in nature as part of the Pentose Phosphate Pathway to rearrange la...
AbstractHere we summarize evidence for non-equivalence of two structurally similar active sites in t...
AbstractTransketolase catalyzes the transfer of an aldehyde residue from keto sugars to aldo sugars....
AbstractPhosphorylation of the pyruvate dehydrogenase component (E1) of the muscle pyruvate dehydrog...
AbstractData from site-directed mutagenesis and X-ray crystallography show that His103 of holotransk...
Transketolase (TK) is an important metabolic enzyme in all organisms. The enantioselective carbon-ca...
The enzyme transketolase is found in nature as part of the Pentose Phosphate Pathway to rearrange la...
This review highlights recent research on the properties and functions of the enzyme transketolase, ...
The enzyme transketolase (TK; E.C. 2.2.1.1) from Escherichia coli occupies a pivotal place in metabo...
In previous studies' with a dialyzed supernatant fraction from rat liver it was observed that the fo...
The molecule of transketolase is a dimer with structurally and functionally identical subunits. Its ...
A structural model for thiamine‐diphosphate (ThDP)‐dependent transketolase (TK) was developed to ana...
Enzymes catalyzing asymmetric carboligation reactions typically show very high specificity for their...
AbstractThe mechanism of regulatory phosphorylation of the pyruvate dehydrogenase component (E1) of ...