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Structure paper

TitleStructure and Mechanism of Isopropylmalate Dehydrogenase from Arabidopsis thaliana: INSIGHTS ON LEUCINE AND ALIPHATIC GLUCOSINOLATE BIOSYNTHESIS.
Journal, issue, pagesJ. Biol. Chem., Vol. 291, Page 13421-13430, Year 2016
Publish dateMar 30, 2016 (structure data deposition date)
AuthorsLee, S.G. / Nwumeh, R. / Jez, J.M.
External linksJ. Biol. Chem. / PubMed:27137927
MethodsX-ray diffraction
Resolution1.827 - 3.492 Å
Structure data

PDB-5j32:
Isopropylmalate dehydrogenase in complex with isopropylmalate
Method: X-RAY DIFFRACTION / Resolution: 1.933 Å

PDB-5j33:
Isopropylmalate dehydrogenase in complex with NAD+
Method: X-RAY DIFFRACTION / Resolution: 3.492 Å

PDB-5j34:
Isopropylmalate dehydrogenase K232M mutant
Method: X-RAY DIFFRACTION / Resolution: 1.827 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-IPM:
3-ISOPROPYLMALIC ACID

ChemComp-HOH:
WATER

ChemComp-NAD:
NICOTINAMIDE-ADENINE-DINUCLEOTIDE / NAD*YM

ChemComp-SO4:
SULFATE ION

Source
  • arabidopsis thaliana (thale cress)
KeywordsOXIDOREDUCTASE / dehydrogenase / leucine biosynthesis / glucosinolate biosynthesis

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