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phosphoglycolohydroxamate

Known as: Acetamide, N-hydroxy-2-(phosphonooxy)- 
National Institutes of Health

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1 relation

Broader (1)

Hydroxamic Acids

Papers overview

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2016
2016
Crystal Structures of Quinolinate Synthase in Complex with a Substrate Analogue, the Condensation Intermediate, and Substrate-Derived Product.
The enzyme NadA catalyzes the synthesis of quinolinic acid (QA), the precursor of the universal nicotinamide adenine dinucleotide… 
2011
2011
Binding thermodynamics of phosphorylated inhibitors to triosephosphate isomerase and the contribution of electrostatic interactions.
2010
2010
Atomic resolution crystallography of a complex of triosephosphate isomerase with a reaction‐intermediate analog: New insight in the proton transfer reaction mechanism
Enzymes achieve their catalytic proficiency by precisely positioning the substrate and catalytic residues with respect to each… 
2001
2001
Structural determinants for ligand binding and catalysis of triosephosphate isomerase.
The crystal structure of leishmania triosephosphate isomerase (TIM) complexed with 2-(N-formyl-N-hydroxy)-aminoethyl phosphonate… 
Highly Cited
1996
Highly Cited
1996
Catalytic mechanism of the metal-dependent fuculose aldolase from Escherichia coli as derived from the structure.
The structure of L-fuculose-1-phosphate aldolase in a cubic crystal form has been determined with and without the inhibitor… 
Highly Cited
1996
Highly Cited
1996
Active site properties of monomeric triosephosphate isomerase (monoTIM) as deduced from mutational and structural studies
MonoTIM is a stable monomeric variant of the dimeric trypanosomal enzyme triose phosphate isomerase (TIM) with less, but… 
1996
1996
The structural basis for pseudoreversion of the H95N lesion by the secondary S96P mutation in triosephosphate isomerase.
The structural basis for the 3000-fold decrease in catalytic efficiency of the H95N mutant chicken triosephosphate isomerase and… 
1995
1995
The structural basis for pseudoreversion of the E165D lesion by the secondary S96P mutation in triosephosphate isomerase depends on the positions of active site water molecules.
The structural basis for the improvement in catalytic efficiency of the mutant E165D chicken triosephosphate isomerase by the… 
1994
1994
Crystal structure of the mutant yeast triosephosphate isomerase in which the catalytic base glutamic acid 165 is changed to aspartic acid.
The three-dimensional structure of the E165D mutant of the glycolytic enzyme yeast triosephosphate isomerase has been determined… 
Highly Cited
1974
Highly Cited
1974
An activated intermediate analogue. The use of phosphoglycolohydroxamate as a stable analogue of a transiently occurring dihydroxyacetone phosphate-derived enolate in enzymatic catalysis.
Abstract At pH 7.5 and 25°, P-glycolohydroxamic acid is an effective inhibitor, competitive with dihydroxyacetone-P, of rabbit… 
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