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N-hydroxy-N-isopropyloxamate
Known as:
IpOHA
National Institutes of Health
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Related topics
Related topics
1 relation
Broader (1)
Hydroxamic Acids
Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
2020
2020
Inhibition studies of ketol-acid reductoisomerases from pathogenic microorganisms.
S. Wun
,
Lambro A. Johnson
,
+4 authors
L. Guddat
Archives of Biochemistry and Biophysics
2020
Corpus ID: 220965502
2000
2000
Structure of spinach acetohydroxyacid isomeroreductase complexed with its reaction product dihydroxymethylvalerate, manganese and (phospho)-ADP-ribose.
K. Thomazeau
,
R. Dumas
,
F. Halgand
,
E. Forest
,
R. Douce
,
V. Biou
Acta Crystallographica Section D: Biological…
2000
Corpus ID: 25777069
Acetohydroxyacid isomeroreductase catalyses a two-step reaction composed of an alkyl migration followed by an NADPH-dependent…
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1999
1999
Characterization of the conformational changes of acetohydroxy acid isomeroreductase induced by the binding of Mg2+ ions, NADPH, and a competitive inhibitor.
F. Halgand
,
R. Dumas
,
+5 authors
E. Forest
Biochemistry
1999
Corpus ID: 2187029
Acetohydroxy acid isomeroreductase (EC 1.1.1.86), the second enzyme of the parallel branched chain amino acid pathway, is a…
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1999
1999
Stepwise building of a 115-kDa macromolecular edifice monitored by electrospray mass spectrometry. The case of acetohydroxy acid isomeroreductase.
O. Laprévote
,
L. Sérani
,
B. Das
,
F. Halgand
,
E. Forest
,
R. Dumas
European Journal of Biochemistry
1999
Corpus ID: 8826608
The macromolecular complexes formed by the enzyme acetohydroxy acid isomeroreductase with NADPH, magnesium ions and the…
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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.
R. Dumas
,
C. Cornillon-Bertrand
,
P. Guigue-Talet
,
P. Génix
,
R. Douce
,
D. Job
Biochemical Journal
1994
Corpus ID: 21016847
N-Hydroxy-N-isopropyloxamate (IpOHA) is known to inhibit extremely tightly (Ki of 22 pM) the bacterial acetohydroxy acid…
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1994
1994
Crystallization and preliminary crystallographic data for acetohydroxy acid isomeroreductase from Spinacia oleracea.
R. Dumas
,
D. Job
,
R. Douce
,
E. Pebay‐Peyroula
,
C. Cohen-addad
Journal of Molecular Biology
1994
Corpus ID: 45816574
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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