Three-dimensional structure of a highly thermostable enzyme, 3-isopropylmalate dehydrogenase of Thermus thermophilus at 2.2 A resolution
about
NAD(+)-dependent formate dehydrogenaseNondecarboxylating and decarboxylating isocitrate dehydrogenases: oxalosuccinate reductase as an ancestral form of isocitrate dehydrogenaseModeling substrate binding in Thermus thermophilus isopropylmalate dehydrogenaseCrystal structure of the monomeric isocitrate dehydrogenase in the presence of NADP+: insight into the cofactor recognition, catalysis, and evolutionCrystal structure of Escherichia coli PdxA, an enzyme involved in the pyridoxal phosphate biosynthesis pathwayNMR structure of the KaiC-interacting C-terminal domain of KaiA, a circadian clock protein: Implications for KaiA-KaiC interactionAllosteric Motions in Structures of Yeast NAD+-specific Isocitrate DehydrogenaseCrystallization and crystal-packing studies ofChlorellavirus deoxyuridine triphosphataseAtomic level description of the domain closure in a dimeric enzyme: thermus thermophilus 3-isopropylmalate dehydrogenaseCrystal structure of N-domain of FKBP22 from Shewanella sp. SIB1: Dimer dissociation by disruption of Val-Leu knotStructure of a highly NADP+-specific isocitrate dehydrogenaseCrystal structure of homoisocitrate dehydrogenase from Schizosaccharomyces pombeStructural analysis of 3-isopropylmalate dehydrogenase from the obligate piezophileShewanella benthicaDB21MT-2 and the nonpiezophileShewanella oneidensisMR-1Structural and energetic basis of isopropylmalate dehydrogenase enzyme catalysisCrystal structure of glycyl-tRNA synthetase from Thermus thermophilusPervasive cryptic epistasis in molecular evolutionStructural characterization of neutral and acidic glycolipids from Thermus thermophilus HB8Molecular cloning and deduced amino acid sequences of the gamma-subunits of rat and monkey NAD(+)-isocitrate dehydrogenasesAdenine recognition: a motif present in ATP-, CoA-, NAD-, NADP-, and FAD-dependent proteins.Structure and Mechanism of Isopropylmalate Dehydrogenase from Arabidopsis thaliana: INSIGHTS ON LEUCINE AND ALIPHATIC GLUCOSINOLATE BIOSYNTHESIS.Structural and functional insights into thermally stable cytochrome c' from a thermophile.Clusters of charged residues in protein three-dimensional structuresRedesigning secondary structure to invert coenzyme specificity in isopropylmalate dehydrogenase.Structural trees for protein superfamilies.The initial step of the thermal unfolding of 3-isopropylmalate dehydrogenase detected by the temperature-jump Laue method.Pressure adaptation of 3-isopropylmalate dehydrogenase from an extremely piezophilic bacterium is attributed to a single amino acid substitution.Mirror image mutations reveal the significance of an intersubunit ion cluster in the stability of 3-isopropylmalate dehydrogenase.Crystallization and preliminary X-ray diffraction analysis of various enzyme-substrate complexes of isopropylmalate dehydrogenase from Thermus thermophilusThermostable repair enzyme for oxidative DNA damage from extremely thermophilic bacterium, Thermus thermophilus HB8.Construction and analyses of tetrameric forms of yeast NAD+-specific isocitrate dehydrogenaseSequence and mutational analysis of a tartrate utilization operon from Agrobacterium vitis.Intra-chain 3D segment swapping spawns the evolution of new multidomain protein architectures.Deciphering the Dynamics of Non-Covalent Interactions Affecting Thermal Stability of a Protein: Molecular Dynamics Study on Point Mutant of Thermus thermophilus Isopropylmalate DehydrogenaseProtein engineering reveals ancient adaptive replacements in isocitrate dehydrogenase.The role of glutamate 87 in the kinetic mechanism of Thermus thermophilus isopropylmalate dehydrogenase.Second-site suppression of regulatory phosphorylation in Escherichia coli isocitrate dehydrogenase.Functional prediction: identification of protein orthologs and paralogsAdjustment of conformational flexibility is a key event in the thermal adaptation of proteins.Expression and biochemical characterization of two small heat shock proteins from the thermoacidophilic crenarchaeon Sulfolobus tokodaii strain 7.Cloning of a cDNA encoding bovine mitochondrial NADP(+)-specific isocitrate dehydrogenase and structural comparison with its isoenzymes from different species.
P2860
Q24528257-7BC17A02-F769-421D-B58B-E1DFCE66CCF5Q24658004-21745640-0DAE-45A3-BD31-17A732479729Q24675416-23EEFFA7-7C82-47F3-BDCF-00E3EC5EA11EQ27641663-E5E12901-9132-4AF2-A4C7-028C02A81766Q27641771-1AEB2F92-1A2A-4D25-9418-6BA1D1126906Q27643053-5DB4E6AB-9931-4724-97F7-889835A09DA4Q27649801-11A77D32-6DC6-4838-BE81-DB61B07E35DEQ27657942-CF06E230-5990-4D34-ABFC-FC122D9A9BCDQ27666894-3E298703-9B3B-480A-B4BA-F5A530436F6DQ27671701-AA420520-EFFC-4D58-B149-2884267CF34BQ27674272-BB90088B-1D0F-476B-A7DA-183610D6E5DAQ27675741-200C2619-759A-46C6-B9E6-2ECF61D0577FQ27678173-75B0FB2D-1B79-4CE7-BA32-10A227902982Q27695606-2139E93D-BFD5-4D47-A008-DC46756FDF85Q27729481-5014B312-49E9-4B35-B4CC-9C2C70BB1060Q28475868-A173F646-43B8-4453-937B-833A35EF7768Q28481348-CFDEFF95-5F73-47F4-AAB3-79499A91CB81Q28567882-9493F92A-2097-4422-9A9B-10532B0B1FACQ30328398-C1F19469-BA0D-4A37-B0F1-2B1C2E298A2BQ30387563-9DC3F6E4-142D-44C2-BC40-E3F09825B04BQ30397632-5F164F09-93FC-42F8-94C0-881AA0BBE2ACQ30424416-426D35C5-1E3C-4CCE-B073-0047662732D5Q30425730-7D1ED3E1-5BA3-46BA-BDC1-DD7C34C05050Q30427554-8CAF1064-7835-4EF1-B0DC-860E1C7E8FABQ30913341-C81D7FED-F065-40AC-81CD-49CACCB13932Q33467135-95033C0E-B8CA-4738-AABC-0B00A7928083Q33890874-713C87A8-EC62-4B8B-BD01-F5C84F7B89DCQ33902180-77184502-90B0-44BD-B406-50EC1C7F0453Q34656935-211A4620-3520-4D82-BF4C-4957B593C3D6Q35109427-BE31DC90-1DB6-4229-8FB7-FC12BA3B4D3DQ35598591-134938B8-4051-4ED8-B19B-B6F2971AB2C4Q35645389-632E288F-44A3-4758-9D3E-F67658C7EC4AQ35866553-466CB236-AD45-40E8-829E-E127E61FBDFBQ36078939-3A9C7FFA-59CB-4A9F-B2EE-F245534C9E62Q36278889-68B281A3-6987-407F-A359-3D5E2711F43CQ36279640-B0C3E612-A16A-4BE0-B0DA-1D1CF6309322Q36281800-E37A4321-958E-426B-BF2F-945C22433936Q36489561-78A9378A-443A-4076-8AF0-7652D678B053Q36526201-0520F2DF-1EBD-4318-AED5-A9DFAC27877FQ36763690-8985E69A-56C8-437E-8DAF-EEBA674CA5FB
P2860
Three-dimensional structure of a highly thermostable enzyme, 3-isopropylmalate dehydrogenase of Thermus thermophilus at 2.2 A resolution
description
1991 nî lūn-bûn
@nan
1991 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1991 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1991年の論文
@ja
1991年論文
@yue
1991年論文
@zh-hant
1991年論文
@zh-hk
1991年論文
@zh-mo
1991年論文
@zh-tw
1991年论文
@wuu
name
Three-dimensional structure of ...... ermophilus at 2.2 A resolution
@ast
Three-dimensional structure of ...... ermophilus at 2.2 A resolution
@en
Three-dimensional structure of ...... ermophilus at 2.2 A resolution
@nl
type
label
Three-dimensional structure of ...... ermophilus at 2.2 A resolution
@ast
Three-dimensional structure of ...... ermophilus at 2.2 A resolution
@en
Three-dimensional structure of ...... ermophilus at 2.2 A resolution
@nl
prefLabel
Three-dimensional structure of ...... ermophilus at 2.2 A resolution
@ast
Three-dimensional structure of ...... ermophilus at 2.2 A resolution
@en
Three-dimensional structure of ...... ermophilus at 2.2 A resolution
@nl
P2093
P1476
Three-dimensional structure of ...... ermophilus at 2.2 A resolution
@en
P2093
P304
P356
10.1016/0022-2836(91)90508-4
P407
P577
1991-12-05T00:00:00Z