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phosphoglycolohydroxamate

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

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Broader (1)

Hydroxamic Acids

Papers overview

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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… 
Highly Cited
2007
Highly Cited
2007
Characterization, Kinetics, and Crystal Structures of Fructose-1,6-bisphosphate Aldolase from the Human Parasite, Giardia lamblia*
Class I and class II fructose-1,6-bisphosphate aldolases (FBPA), glycolytic pathway enzymes, exhibit no amino acid sequence… 
2006
2006
Stereoselectivity of fructose-1,6-bisphosphate aldolase in Thermus caldophilus.
Highly Cited
2003
Highly Cited
2003
Structure and catalytic mechanism of L-rhamnulose-1-phosphate aldolase.
The structure of L-rhamnulose-1-phosphate aldolase has been established at 1.35 A resolution in a crystal form that was obtained… 
Highly Cited
1999
Highly Cited
1999
The crystal structure of Escherichia coli class II fructose-1, 6-bisphosphate aldolase in complex with phosphoglycolohydroxamate reveals details of mechanism and specificity.
The structure of a class II fructose-1,6-bisphosphate aldolase in complex with the substrate analogue and inhibitor… 
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… 
Highly Cited
1994
Highly Cited
1994
Triosephosphate isomerase requires a positively charged active site: the role of lysine-12.
The role of lysine-12 at the active site of yeast triosephosphate isomerase has been elucidated by a combination of site-directed… 
Highly Cited
1991
Highly Cited
1991
Structure of the triosephosphate isomerase-phosphoglycolohydroxamate complex: an analogue of the intermediate on the reaction pathway.
The glycolytic enzyme triosephosphate isomerase (TIM) catalyzes the interconversion of the three-carbon sugars dihydroxyacetone… 
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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