EC Number   |
|---|
    1.1.1.85 | - |
| 1.1.1.85 | ammonium sulfate precipitation, crystals diffract beyond 2.5 A resolution and are quite stable against X-rays, recombinant enzyme expressed in Escherichia coli |
| 1.1.1.85 | apo-form without substrate and in complex with the divalent metalion, in complexes with both Mn2+ and 3-isopropylmalate, as well as with both Mn2+ and NADH, at resolutions ranging from 1.8 to 2.5 A. Identification of two hinges at the interdomain region, hinge 1 between alphad and betaF as well as hinge 2 between alphah and betaE with a possible operational mechanism upon the action of the substrates. The interactions of the protein with Mn2+ and isopropylmalate are mainly responsible for the domain closure. Upon binding into the cleft of the interdomain region, the substrate isopropylmalate induces a relative movement of the secondary structural elements betaE, betaF, betaG, alphad and alphah. A movement of the loop bearing the amino acid Tyr139 precedes the interacting arm of the subunit. The tyrosyl ring rotates and moves by at least 5 A upon substrate binding. Thereby, new hydrophobic interactions are formed above the buried isopropyl-group of isopropylmalate. Domain closure is then completed only through subunit interactions. A loop of one subunit that is inserted into the interdomain cavity of the other subunit extends the area with the hydrophobic interactions, providing an example of the cooperativity between interdomain and intersubunit interactions |
| 1.1.1.85 | crystal structure of mutant H15Y/E57V/S72I/R85M/Y86A/M208T/F217Y/V238M/R310M is determined at 2.4 A |
| 1.1.1.85 | crystal structure of the enzyme in complex with the inhibitor O-isobutenyl oxalylhydroxamate and with the cofactor NAD+ at 2.1 A resolution |
| 1.1.1.85 | crystal structure of Thermus thermophilus IPMDH in a ternary complex with NAD+ and the inhibitor ((2S,3S)-3-methylmercaptomalate) is determined at 2.8 A resolution. The inhibitor exists as a decarboxylated product with an enol/enolate form in the active site. The product interacts with Arg94, Asn102, Ser259, Glu270, and a water molecule hydrogen-bonding with Arg132. All interactions between the product and the enzyme are observed in the position associated with keto-enol tautomerization |
| 1.1.1.85 | crystal structures of Escherichia coli and Salmonella typhimurium 3-isopropylmalate dehydrogenase and comparison with their thermophilic counterpart from Thermus thermophilus |
| 1.1.1.85 | crystallized by the vapor-diffusion method, space group P2221. The crystallization requires 2-methyl-2,4-pentanediol to avoid twinning of the crystals |
| 1.1.1.85 | enzyme in complex with 3-isopropylmalate |
| 1.1.1.85 | enzyme in complex with NAD+ |
