Reaction participants Show >> << Hide
- Name help_outline (2R,3S)-3-isopropylmalate Identifier CHEBI:35121 Charge -2 Formula C7H10O5 InChIKeyhelp_outline RNQHMTFBUSSBJQ-CRCLSJGQSA-L SMILEShelp_outline CC(C)[C@@H]([C@@H](O)C([O-])=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 5 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 2-isopropylmaleate Identifier CHEBI:58085 Charge -2 Formula C7H8O4 InChIKeyhelp_outline NJMGRJLQRLFQQX-HYXAFXHYSA-L SMILEShelp_outline CC(C)C(\C([O-])=O)=C\C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,264 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:10676 | RHEA:10677 | RHEA:10678 | RHEA:10679 | |
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Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Absolute configuration of alpha isopropylmalate and the mechanism of its conversion to beta isopropylmalate in the biosynthesis of leucine.
Cole F.E., Kalyanpur M.G., Stevens C.M.
Biochemistry 12:3346-3350(1973) [PubMed] [EuropePMC]
This publication is cited by 3 other entries.
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Micromolar intracellular hydrogen peroxide disrupts metabolism by damaging iron-sulfur enzymes.
Jang S., Imlay J.A.
An Escherichia coli strain that cannot scavenge hydrogen peroxide has been used to identify the cell processes that are most sensitive to this oxidant. Low micromolar concentrations of H2O2 completely blocked the biosynthesis of leucine. The defect was tracked to the inactivation of isopropylmalat ... >> More
An Escherichia coli strain that cannot scavenge hydrogen peroxide has been used to identify the cell processes that are most sensitive to this oxidant. Low micromolar concentrations of H2O2 completely blocked the biosynthesis of leucine. The defect was tracked to the inactivation of isopropylmalate isomerase. This enzyme belongs to a family of [4Fe-4S] dehydratases that are notoriously sensitive to univalent oxidation, and experiments confirmed that other members were also inactivated. In vitro and in vivo analyses showed that H2O2 directly oxidized their solvent-exposed clusters in a Fenton-like reaction. The oxidized cluster then degraded to a catalytically inactive [3Fe-4S] form. Experiments indicated that H2O2 accepted two consecutive electrons during the oxidation event. As a consequence, hydroxyl radicals were not released; the polypeptide was undamaged; and the enzyme was competent for reactivation by repair processes. Strikingly, in scavenger-deficient mutants, the H2O2 that was generated as an adventitious by-product of metabolism (<1 microm) was sufficient to damage these [4Fe-4S] enzymes. This result demonstrates that aerobic organisms must synthesize H2O2 scavengers to avoid poisoning their own pathways. The extreme vulnerability of these enzymes may explain why many organisms, including mammals, deploy H2O2 to suppress microbial growth. << Less
J. Biol. Chem. 282:929-937(2007) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.
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THE BIOSYNTHESIS OF LEUCINE. II. THE ENZYMIC ISOMERIZATION OF BETA-CARBOXY-BETA-HYDROXYISOCAPROATE AND ALPHA-HYDROXY-BETA-CARBOXYISOCAPROATE.
GROSS S.R., BURNS R.O., UMBARGER H.E.
Biochemistry 2:1046-1052(1963) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.
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THE ABSOLUTE CONFIGURATION OF ALPHA-HYDROXY-BETA-CARBOXYISOCAPROIC ACID (3-ISOPROPYLMALIC ACID), AN INTERMEDIATE IN LEUCINE BIOSYNTHESIS.
CALVO J.M., STEVENS C.M., KALYANPUR M.G., UMBARGER H.E.
Biochemistry 3:2024-2027(1964) [PubMed] [EuropePMC]
This publication is cited by 4 other entries.
Comments
RHEA:10676 part of RHEA:32287