(Q27641663)

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Crystal structure of the monomeric isocitrate dehydrogenase in the presence of NADP+: insight into the cofactor recognition, catalysis, and evolution

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Crystal structure of the monomeric isocitrate dehydrogenase in the presence of NADP+: insight into the cofactor recognition, catalysis, and evolution (English)

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crystal structure

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author name string

Yoshiaki Yasutake

1

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Seiya Watanabe

2

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Min Yao

3

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Yasuhiro Takada

4

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Noriyuki Fukunaga

5

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Isao Tanaka

6

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language of work or name

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publication date

19 September 2003

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Journal of Biological Chemistry

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278

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38

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36897-904

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Three-dimensional structure of a highly thermostable enzyme, 3-isopropylmalate dehydrogenase of Thermus thermophilus at 2.2 A resolution

1 reference

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21 January 2018

Structure of 3-isopropylmalate dehydrogenase in complex with NAD+: ligand-induced loop closing and mechanism for cofactor specificity

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21 January 2018

Crystal structures of Escherichia coli and Salmonella typhimurium 3-isopropylmalate dehydrogenase and comparison with their thermophilic counterpart from Thermus thermophilus

1 reference

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21 January 2018

Structure of 3-isopropylmalate dehydrogenase in complex with 3-isopropylmalate at 2.0 A resolution: the role of Glu88 in the unique substrate-recognition mechanism

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21 January 2018

Functional prediction: identification of protein orthologs and paralogs

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Identification of enzymes homologous to isocitrate dehydrogenase that are involved in coenzyme B and leucine biosynthesis in methanoarchaea

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Characterization of homoisocitrate dehydrogenase involved in lysine biosynthesis of an extremely thermophilic bacterium, Thermus thermophilus HB27, and evolutionary implication of beta-decarboxylating dehydrogenase

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Structure of a bacterial enzyme regulated by phosphorylation, isocitrate dehydrogenase

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Regulation of an enzyme by phosphorylation at the active site

1 reference

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Catalytic mechanism of NADP(+)-dependent isocitrate dehydrogenase: implications from the structures of magnesium-isocitrate and NADP+ complexes

1 reference

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21 January 2018

Structure of isocitrate dehydrogenase with isocitrate, nicotinamide adenine dinucleotide phosphate, and calcium at 2.5-A resolution: a pseudo-Michaelis ternary complex

1 reference

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Structure of isocitrate dehydrogenase with alpha-ketoglutarate at 2.7-A resolution: conformational changes induced by decarboxylation of isocitrate

1 reference

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Mutagenesis and Laue structures of enzyme intermediates: isocitrate dehydrogenase

1 reference

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Determinants of cofactor specificity in isocitrate dehydrogenase: structure of an engineered NADP+ --> NAD+ specificity-reversal mutant

1 reference

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Access to phosphorylation in isocitrate dehydrogenase may occur by domain shifting

1 reference

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Orbital steering in the catalytic power of enzymes: small structural changes with large catalytic consequences

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Millisecond Laue structures of an enzyme-product complex using photocaged substrate analogs

1 reference

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Active site water molecules revealed in the 2.1 A resolution structure of a site-directed mutant of isocitrate dehydrogenase

1 reference

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Structural basis for a change in substrate specificity: crystal structure of S113E isocitrate dehydrogenase in a complex with isopropylmalate, Mg2+, and NADP

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Crystal structure of porcine mitochondrial NADP+-dependent isocitrate dehydrogenase complexed with Mn2+ and isocitrate. Insights into the enzyme mechanism

1 reference

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Corynebacterium efficiens sp. nov., a glutamic-acid-producing species from soil and vegetables

1 reference

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A highly specific monomeric isocitrate dehydrogenase from Corynebacterium glutamicum

1 reference

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Genes encoding two isocitrate dehydrogenase isozymes of a psychrophilic bacterium, Vibrio sp. strain ABE-1.

1 reference

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Differential expression in Escherichia coli of the Vibrio sp. strain ABE-1 icdI and icdII genes encoding structurally different isocitrate dehydrogenase isozymes

1 reference

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Crystallization and preliminary X-ray diffraction studies of monomeric isocitrate dehydrogenase by the MAD method using Mn atoms.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M304091200

21 January 2018

Structure of the monomeric isocitrate dehydrogenase: evidence of a protein monomerization by a domain duplication

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M304091200

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The CCP4 suite: programs for protein crystallography

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M304091200

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AMoRe: an automated package for molecular replacement

1 reference

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Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

1 reference

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Improved methods for building protein models in electron density maps and the location of errors in these models

1 reference

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PROCHECK: a program to check the stereochemical quality of protein structures

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M304091200

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Solvent content of protein crystals

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M304091200

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Ligand-induced changes in the conformation of 3-isopropylmalate dehydrogenase from Thermus thermophilus

1 reference

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Crystal structure of the ternary complex of mouse lung carbonyl reductase at 1.8 A resolution: the structural origin of coenzyme specificity in the short-chain dehydrogenase/reductase family

1 reference

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Crystal structures of the binary and ternary complexes of 7 alpha-hydroxysteroid dehydrogenase from Escherichia coli

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A link between protein structure and enzyme catalyzed hydrogen tunneling

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Mechanism of coenzyme recognition and binding revealed by crystal structure analysis of ferredoxin-NADP+ reductase complexed with NADP+

1 reference

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Protein engineering reveals ancient adaptive replacements in isocitrate dehydrogenase

1 reference

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Biochemical and phylogenetic characterization of isocitrate dehydrogenase from a hyperthermophilic archaeon, Archaeoglobus fulgidus

1 reference

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Comparison of isocitrate dehydrogenase from three hyperthermophiles reveals differences in thermostability, cofactor specificity, oligomeric state, and phylogenetic affiliation

1 reference

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Crystal structure of Bacillus subtilis isocitrate dehydrogenase at 1.55 A. Insights into the nature of substrate specificity exhibited by Escherichia coli isocitrate dehydrogenase kinase/phosphatase

1 reference

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Protein structure comparison by alignment of distance matrices

1 reference

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MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

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Raster3D: photorealistic molecular graphics

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Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons

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CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice

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Conformations of the coenzymes and the allosteric activator, ADP, bound to NAD(+)-dependent isocitrate dehydrogenase from pig heart

1 reference

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Kinetic analysis on the substrate specificity of 3-isopropylmalate dehydrogenase

1 reference

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Oxidized triphosphopyridine nucleotide specific isocitrate dehydrogenase from Azotobacter vinelandii. Isolation and characterization

1 reference

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Characterization of the highly active isocitrate (NADP+) dehydrogenase of Azotobacter vinelandii

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Isozymes of isocitrate dehydrogenase from an obligately psychrophilic bacterium, Vibrio sp. strain ABE-1: purification, and modulation of activities by growth conditions

1 reference

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Isocitrate dehydrogenase from Azotobacter vinelandii. Order of substrate addition and product release

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Oxidized triphosphopyridine nucleotide specific isocitrate dehydrogenase from Azotobacter vinelandii. 3. The path of hydrogen in the enzymatic reaction

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10.1074/JBC.M304091200

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