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N-hydroxy-N-isopropyloxamate

Known as: IpOHA 
National Institutes of Health

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Hydroxamic Acids

Papers overview

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2020
2020
Inhibition studies of ketol-acid reductoisomerases from pathogenic microorganisms.
2000
2000
Structure of spinach acetohydroxyacid isomeroreductase complexed with its reaction product dihydroxymethylvalerate, manganese and (phospho)-ADP-ribose.
Acetohydroxyacid isomeroreductase catalyses a two-step reaction composed of an alkyl migration followed by an NADPH-dependent… 
1999
1999
Characterization of the conformational changes of acetohydroxy acid isomeroreductase induced by the binding of Mg2+ ions, NADPH, and a competitive inhibitor.
Acetohydroxy acid isomeroreductase (EC 1.1.1.86), the second enzyme of the parallel branched chain amino acid pathway, is a… 
1999
1999
Stepwise building of a 115-kDa macromolecular edifice monitored by electrospray mass spectrometry. The case of acetohydroxy acid isomeroreductase.
The macromolecular complexes formed by the enzyme acetohydroxy acid isomeroreductase with NADPH, magnesium ions and the… 
1994
1994
Interactions of plant acetohydroxy acid isomeroreductase with reaction intermediate analogues: correlation of the slow, competitive, inhibition kinetics of enzyme activity and herbicidal effects.
N-Hydroxy-N-isopropyloxamate (IpOHA) is known to inhibit extremely tightly (Ki of 22 pM) the bacterial acetohydroxy acid… 
1994
1994
Crystallization and preliminary crystallographic data for acetohydroxy acid isomeroreductase from Spinacia oleracea.
Acetohydroxy acid isomeroreductase (EC 1.1.1.86) is one of the enzymes involved in branched-chain amino acid biosynthesis. The… 
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