X
Search Filters
Format Format
Subjects Subjects
Subjects Subjects
X
Sort by Item Count (A-Z)
Filter by Count
index medicus (1428) 1428
apoenzymes - metabolism (996) 996
biochemistry & molecular biology (655) 655
kinetics (542) 542
animals (512) 512
apoenzymes - chemistry (494) 494
binding sites (434) 434
models, molecular (319) 319
protein conformation (308) 308
protein binding (287) 287
humans (269) 269
molecular sequence data (237) 237
amino acid sequence (236) 236
crystallography, x-ray (218) 218
enzymes (199) 199
apoenzymes - genetics (194) 194
apoenzymes (172) 172
catalysis (172) 172
escherichia-coli (166) 166
escherichia coli - enzymology (164) 164
rats (164) 164
biophysics (161) 161
hydrogen-ion concentration (159) 159
research (155) 155
substrate specificity (155) 155
recombinant proteins - metabolism (150) 150
crystal-structure (145) 145
proteins (138) 138
recombinant proteins - chemistry (122) 122
apoenzymes - isolation & purification (121) 121
structure-activity relationship (121) 121
enzyme activation (119) 119
apoproteins - metabolism (113) 113
analysis (112) 112
catalytic domain (112) 112
spectrophotometry (112) 112
binding (109) 109
male (108) 108
molecular weight (105) 105
purification (105) 105
oxidation-reduction (103) 103
protein structure, secondary (100) 100
mutation (98) 98
protein structure, tertiary (98) 98
cattle (97) 97
mechanism (89) 89
mutagenesis, site-directed (86) 86
spectrometry, fluorescence (86) 86
liver - enzymology (85) 85
macromolecular substances (85) 85
circular dichroism (82) 82
holoenzymes - metabolism (82) 82
structure (82) 82
escherichia coli - genetics (81) 81
ligands (80) 80
bacterial proteins - metabolism (78) 78
cell biology (75) 75
physiological aspects (75) 75
enzyme stability (74) 74
swine (74) 74
apoenzyme (72) 72
enzyme (72) 72
pyridoxal phosphate - metabolism (72) 72
crystal structure (71) 71
thermodynamics (71) 71
zinc - metabolism (70) 70
bacterial proteins - chemistry (69) 69
biochemistry (69) 69
protein (69) 69
protein folding (68) 68
sequence homology, amino acid (68) 68
base sequence (66) 66
dimerization (65) 65
holoenzymes - chemistry (65) 65
nad - metabolism (64) 64
active-site (63) 63
coenzymes - metabolism (62) 62
sequence alignment (61) 61
article (60) 60
hydrogen bonding (60) 60
temperature (60) 60
aspartate aminotransferases - metabolism (58) 58
chemical properties (58) 58
crystals (58) 58
crystallization (57) 57
electrophoresis, polyacrylamide gel (57) 57
escherichia coli (57) 57
bacterial proteins - genetics (55) 55
biosynthesis (55) 55
cloning, molecular (55) 55
microbiology (55) 55
spectrophotometry, ultraviolet (54) 54
multidisciplinary sciences (52) 52
chemistry (51) 51
expression (51) 51
saccharomyces cerevisiae - enzymology (51) 51
amino acid substitution (50) 50
copper - metabolism (50) 50
heme - metabolism (50) 50
protein structure, quaternary (50) 50
more...
Language Language
Language Language
X
Sort by Item Count (A-Z)
Filter by Count
English (1424) 1424
Russian (27) 27
German (4) 4
Japanese (4) 4
Italian (2) 2
Polish (2) 2
Spanish (2) 2
French (1) 1
Ukrainian (1) 1
more...
Publication Date Publication Date
Click on a bar to filter by decade
Slide to change publication date range


Nature, ISSN 0028-0836, 08/2010, Volume 466, Issue 7309, pp. 935 - 940
Despite the success of genomics in identifying new essential bacterial genes, there is a lack of sustainable leads in antibacterial drug discovery to address... 
BREAKAGE-REUNION DOMAIN | B-PROTEIN | BAD BUGS | MECHANISM | COLI DNA GYRASE | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | FUSION PROTEIN | INFECTIOUS-DISEASES-SOCIETY | CLEAVAGE | Staphylococcus aureus - enzymology | Crystallography, X-Ray | Structure-Activity Relationship | Quinolines - pharmacology | Quinolones - chemistry | Anti-Bacterial Agents - chemistry | Topoisomerase II Inhibitors | Apoenzymes - metabolism | DNA, Superhelical - chemistry | Drug Design | Binding Sites | Ciprofloxacin - metabolism | Drug Resistance | Catalytic Domain | Escherichia coli - enzymology | DNA Gyrase - chemistry | Quinolines - chemistry | Quinolones - metabolism | Models, Molecular | Anti-Bacterial Agents - metabolism | DNA - metabolism | Quinolines - metabolism | DNA Gyrase - metabolism | DNA - chemistry | Manganese - metabolism | Apoenzymes - chemistry | Ciprofloxacin - chemistry | Aspartic Acid - metabolism | Protein Conformation | Anti-Bacterial Agents - pharmacology | DNA, Superhelical - metabolism | Arginine - metabolism | DNA Cleavage | Antimitotic agents | Enzymes | Drug resistance in microorganisms | Topoisomerases | DNA | Genes | Research | Properties | Antineoplastic agents | Antibacterial agents | Staphylococcus aureus | Bacteria | Mutation | E coli | Deoxyribonucleic acid--DNA | Streptococcus infections | Index Medicus
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 08/2017, Volume 292, Issue 34, pp. 14039 - 14049
Flavin-based electron transfer bifurcation is emerging as a fundamental and powerful mechanism for conservation and deployment of electrochemical energy in... 
electron bifurcation | FLAVODOXIN | PROTEIN | ACID | NITROREDUCTASE | transient absorption spectroscopy | BIOCHEMISTRY & MOLECULAR BIOLOGY | EXCITED-STATE DYNAMICS | flavin | DESULFOVIBRIO-VULGARIS | NADH OXIDASE | electron transfer | fluorescence | flavoprotein | PURIFICATION | PHOTOACTIVATION | BINDING | energetics | Flavin-Adenine Dinucleotide - chemistry | Nitroreductases - genetics | Electron Transport | ortho-Aminobenzoates - chemistry | Flavodoxin - genetics | Nitroreductases - chemistry | Enterobacter cloacae - enzymology | Bacterial Proteins - chemistry | Flavodoxin - chemistry | Multienzyme Complexes - metabolism | Holoenzymes - chemistry | Oxidoreductases - chemistry | Recombinant Fusion Proteins - metabolism | Flavin-Adenine Dinucleotide - metabolism | Silent Mutation | Holoenzymes - metabolism | Apoenzymes - metabolism | NADH, NADPH Oxidoreductases - chemistry | NADH, NADPH Oxidoreductases - metabolism | Pyrococcus furiosus - enzymology | Recombinant Proteins - metabolism | NADH, NADPH Oxidoreductases - genetics | Thermus thermophilus - enzymology | Flavodoxin - metabolism | Biocatalysis | Oxidation-Reduction | Oxidoreductases - metabolism | Oxidoreductases - genetics | Benzoic Acid - metabolism | Bacterial Proteins - genetics | Models, Molecular | Recombinant Proteins - chemistry | Flavin-Adenine Dinucleotide - analogs & derivatives | Multienzyme Complexes - genetics | Recombinant Fusion Proteins - chemistry | Multienzyme Complexes - chemistry | Nitroreductases - metabolism | Apoenzymes - genetics | Apoenzymes - chemistry | Benzoic Acid - chemistry | Bacterial Proteins - metabolism | Desulfovibrio vulgaris - enzymology | Holoenzymes - genetics | ortho-Aminobenzoates - metabolism | Index Medicus | solar (fuels), biofuels (including algae and biomass), bio-inspired, hydrogen and fuel cells | Bioenergetics
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 2017, Volume 292, Issue 44, pp. 18290 - 18302
Strain SYK-6 of the bacterium Sphingobium sp. catabolizes lignin-derived biphenyl via a meta-cleavage pathway. In this pathway, LigY is proposed to catalyze... 
CATABOLISM | 2-HYDROXY-6-KETO-NONA-2,4-DIENE-1,9-DIOIC ACID 5,6-HYDROLASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | C BOND HYDROLASE | CRYSTAL-STRUCTURES | metalloenzyme | meta-cleavage | amidohydrolase superfamily | bacterial metabolism | LIGNIN-DERIVED BIPHENYL | DATABASE | hydrolase | SPHINGOMONAS-PAUCIMOBILIS SYK-6 | DEGRADATION | lignin degradation | CATALYTIC MECHANISM | zinc | EPSILON-SEMIALDEHYDE-DECARBOXYLASE | C-C hydrolase | aromatic compound | Hydrolases - genetics | Zinc - metabolism | Bacterial Proteins - chemistry | Substrate Specificity | Apoenzymes - classification | Crystallography, X-Ray | Phylogeny | Parabens - metabolism | Vanillic Acid - analogs & derivatives | Apoenzymes - metabolism | Caproates - metabolism | Hydrolases - classification | Binding Sites | Amidohydrolases - metabolism | Hydrolases - metabolism | Recombinant Proteins - metabolism | Biocatalysis | Mutagenesis, Site-Directed | Amidohydrolases - genetics | Bacterial Proteins - genetics | Models, Molecular | Recombinant Proteins - chemistry | Vanillic Acid - metabolism | Amidohydrolases - chemistry | Recombinant Proteins - classification | Hydrolysis | Sequence Homology, Amino Acid | Sphingomonadaceae - enzymology | Apoenzymes - genetics | Phthalic Acids - metabolism | Apoenzymes - chemistry | Bacterial Proteins - metabolism | Ligands | Protein Conformation | Bacterial Proteins - classification | Glutarates - metabolism | Hydrolases - chemistry | Structural Homology, Protein | Mutation | Amidohydrolases - classification | Amino Acid Substitution | Index Medicus | Enzymology
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 2017, Volume 292, Issue 35, pp. 14556 - 14565
Urease is a ubiquitous nickel metalloenzyme. In plants, its activation requires three urease accessory proteins (UAPs), UreD, UreF, and UreG. In bacteria, the... 
APOPROTEIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | IN-VIVO | PURIFICATION | FUNCTIONAL-ANALYSIS | METALLOCHAPERONE | ARABIDOPSIS | IDENTIFICATION | CHAPERONE | HELICOBACTER-PYLORI | BINDING | Recombinant Fusion Proteins - isolation & purification | Arabidopsis - enzymology | Plants, Genetically Modified - growth & development | Oryza - metabolism | Protein Multimerization | Apoenzymes - isolation & purification | Recombinant Fusion Proteins - metabolism | Urease - chemistry | Arabidopsis Proteins - metabolism | Recombinant Proteins - isolation & purification | Plant Proteins - chemistry | Gene Deletion | Apoenzymes - metabolism | Conserved Sequence | Clone Cells | Plant Proteins - metabolism | Recombinant Proteins - metabolism | Amino Acid Sequence | Arabidopsis Proteins - genetics | Plants, Genetically Modified - genetics | Tobacco - metabolism | Cells, Cultured | Models, Molecular | Recombinant Proteins - chemistry | Tobacco - growth & development | Recombinant Fusion Proteins - chemistry | Oryza - enzymology | Plant Leaves - cytology | Arabidopsis - metabolism | Tobacco - cytology | Arabidopsis Proteins - isolation & purification | Plant Proteins - genetics | Plants, Genetically Modified - metabolism | Arabidopsis Proteins - chemistry | Plant Leaves - genetics | Plant Leaves - metabolism | Plant Leaves - growth & development | Tobacco - genetics | Apoenzymes - genetics | Hydroponics | Apoenzymes - chemistry | Urease - isolation & purification | Plants, Genetically Modified - cytology | Urease - metabolism | Enzyme Activation | Mutation | Nickel - metabolism | Urease - genetics | Index Medicus | Plant Biology | nickel | chaperone | enzyme processing | protein complex | metalloenzyme | metal ion-protein interaction
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 2017, Volume 292, Issue 35, pp. 14617 - 14624
Using the energy of ATP hydrolysis, ABC transporters catalyze the trans-membrane transport of molecules. In bacteria, these transporters partner with a... 
ANTHRACIS VIRULENCE DETERMINANT | MALTOSE TRANSPORT | BTUCD-F | MECHANISM | YERSINIA-PESTIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | CASSETTE TRANSPORTER | CRYSTAL-STRUCTURES | MULTIDRUG-RESISTANCE | HISTIDINE PERMEASE | Surface Plasmon Resonance | Hemeproteins - genetics | Heme - metabolism | Protein Multimerization | Bacterial Proteins - chemistry | Holoenzymes - chemistry | Recombinant Proteins | Cell Membrane - chemistry | ATP-Binding Cassette Transporters - chemistry | Holoenzymes - metabolism | ATP-Binding Cassette Transporters - genetics | Heme - chemistry | Adenosine Triphosphate - metabolism | Hemeproteins - chemistry | Apoenzymes - metabolism | ATP-Binding Cassette Transporters - metabolism | Carrier Proteins - chemistry | Receptors, Cell Surface - chemistry | Cell Membrane - metabolism | Protein Interaction Domains and Motifs | Dimerization | Immobilized Proteins - chemistry | Yersinia pestis - metabolism | Hemeproteins - metabolism | Immobilized Proteins - genetics | Bacterial Proteins - genetics | Models, Molecular | Receptors, Cell Surface - metabolism | Hydrolysis | Carrier Proteins - genetics | Carrier Proteins - metabolism | Apoenzymes - genetics | Immobilized Proteins - metabolism | Apoenzymes - chemistry | Bacterial Proteins - metabolism | Holoenzymes - genetics | Molecular Docking Simulation | Kinetics | Adenosine Triphosphate - chemistry | Receptors, Cell Surface - genetics | Index Medicus | Membrane Biology | ATPase | membrane protein | protein-protein interaction | surface plasmon resonance (SPR) | ABC transporter | ATP
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 2017, Volume 292, Issue 32, pp. 13323 - 13332
Polycomb-group proteins control many fundamental biological processes, such as anatomical development in mammals and vernalization in plants. Polycomb... 
METHYLATION | PRC2 | RNA | HISTONE H3 | METHYLTRANSFERASES | BIOCHEMISTRY & MOLECULAR BIOLOGY | MUTATION | MARKS | H3K27ME3 | GAIN | EZH2 | Fungal Proteins - chemistry | Polycomb Repressive Complex 2 - genetics | Histones - chemistry | S-Adenosylmethionine - chemistry | Recombinant Fusion Proteins - metabolism | Xenopus Proteins - chemistry | Coenzymes - metabolism | Apoenzymes - metabolism | Conserved Sequence | Lysine - metabolism | Protein Interaction Domains and Motifs | Coenzymes - chemistry | Peptide Fragments - genetics | Enhancer of Zeste Homolog 2 Protein - chemistry | Amino Acid Sequence | Enhancer of Zeste Homolog 2 Protein - genetics | Enhancer of Zeste Homolog 2 Protein - metabolism | Peptide Fragments - metabolism | Models, Molecular | Chaetomium - enzymology | Fungal Proteins - genetics | Recombinant Fusion Proteins - chemistry | Polycomb Repressive Complex 2 - chemistry | Peptide Fragments - chemistry | Animals | Xenopus laevis - metabolism | Apoenzymes - genetics | Apoenzymes - chemistry | Xenopus Proteins - metabolism | Protein Processing, Post-Translational | Histones - metabolism | Mutation | Methylation | Polycomb Repressive Complex 2 - metabolism | S-Adenosylmethionine - metabolism | Amino Acid Substitution | Fungal Proteins - metabolism | Index Medicus | enzyme | crystal structure | Protein Structure and Folding | histone methylation | epigenetics | polycomb
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 08/2017, Volume 292, Issue 34, pp. 14026 - 14038
Hydrogen sulfide (H2S) is a signaling molecule that is toxic at elevated concentrations. In eukaryotes, it is cleared via a mitochondrial sulfide oxidation... 
LIVER RHODANESE | SULFURTRANSFERASE | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | H2S | HYDROGEN-SULFIDE | enzyme kinetics | X-ray crystallography | hydrogen sulfide | ETHE1 | iron | sulfur | STAPHYLOCOCCUS-AUREUS | MUTATIONS | ELECTROSTATICS | ETHYLMALONIC ENCEPHALOPATHY | Disulfides - metabolism | Hydrogen Sulfide - metabolism | Burkholderiaceae - enzymology | Glutathione - metabolism | Mutant Chimeric Proteins - genetics | Thiosulfate Sulfurtransferase - genetics | Bacterial Proteins - chemistry | Crystallography, X-Ray | Mutant Chimeric Proteins - chemistry | Thiosulfate Sulfurtransferase - chemistry | Quinone Reductases - chemistry | Thiosulfate Sulfurtransferase - metabolism | Mutant Chimeric Proteins - metabolism | Apoenzymes - metabolism | Peptide Fragments - genetics | Recombinant Proteins - metabolism | Quinone Reductases - metabolism | Catalytic Domain | Peptide Fragments - metabolism | Biocatalysis | Glutathione - analogs & derivatives | Bacterial Proteins - genetics | Computational Biology | Enzyme Stability | Models, Molecular | Recombinant Proteins - chemistry | Cysteine - chemistry | Thiosulfates - metabolism | Peptide Fragments - chemistry | Apoenzymes - genetics | Apoenzymes - chemistry | Bacterial Proteins - metabolism | Protein Conformation | Quinone Reductases - genetics | Glutathione - chemistry | Mutation | Amino Acid Substitution | Index Medicus | BASIC BIOLOGICAL SCIENCES | Enzymology
Journal Article
Science, ISSN 0036-8075, 6/2006, Volume 312, Issue 5782, pp. 1954 - 1958
The formation of glutaminyl transfer RNA ( ) differs among the three domains of life. Most bacteria employ an indirect pathway to produce by a heterotrimeric... 
Hydrolysis | Proteins | Ammonia | Molecules | Enzymes | Active sites | Amides | Reports | Biochemistry | Transfer RNA | Crystal structure | PROTEIN | GLN-TRNA(GLN) | MULTIDISCIPLINARY SCIENCES | ESCHERICHIA-COLI | GLU-TRNA(GLN) AMIDOTRANSFERASE | TRANSLATION | SOFTWARE | TRANSFER-RNA-SYNTHETASE | REVEALS | Protein Subunits | Staphylococcus aureus - enzymology | RNA, Transfer, Amino Acyl - chemistry | Glutamine - metabolism | Molecular Sequence Data | Crystallography, X-Ray | RNA, Transfer, Gln - metabolism | Apoenzymes - metabolism | Protein Structure, Quaternary | RNA, Transfer, Amino Acyl - metabolism | Glutamine - chemistry | Nucleic Acid Conformation | RNA, Bacterial - metabolism | Staphylococcus aureus - metabolism | Protein Structure, Tertiary | Staphylococcus aureus - genetics | Amino Acid Sequence | Catalytic Domain | RNA, Transfer, Gln - chemistry | Protein Structure, Secondary | Ammonia - metabolism | Models, Molecular | Magnesium - metabolism | Glutaminase - metabolism | Manganese - metabolism | Base Pairing | Hydrogen Bonding | Asparagine - metabolism | RNA, Bacterial - chemistry | Apoenzymes - chemistry | Hydrophobic and Hydrophilic Interactions | Aminoacyltransferases - metabolism | Adenosine Diphosphate - metabolism | Mutation | Genetic code | Research | Analysis | Bacteria | Chemical reactions | Index Medicus
Journal Article
Nature, ISSN 0028-0836, 04/2016, Volume 533, Issue 7602, pp. 260 - 264
Journal Article
JOURNAL OF BIOLOGICAL CHEMISTRY, ISSN 0021-9258, 01/2016, Volume 291, Issue 3, pp. 1175 - 1197
The recent classification of glycoside hydrolase family 5 (GH5) members into subfamilies enhances the prediction of substrate specificity by phylogenetic... 
SUBSTRATE-SPECIFICITY | POLYSACCHARIDE LYASES | SITE NUCLEOPHILE | BIOCHEMISTRY & MOLECULAR BIOLOGY | CARBOHYDRATE-ACTIVE ENZYMES | ENZYMATIC-HYDROLYSIS | XYLOGLUCAN | ENDOGLUCANASE GENE | MASS-SPECTROMETRY | CELL-WALLS | CLOSTRIDIUM-CELLULOLYTICUM | Cellulase - chemistry | Xylans - metabolism | Cellulase - antagonists & inhibitors | Cellulase - genetics | Endo-1,3-beta-Glucanase - chemistry | Glycoside Hydrolases - genetics | Bacterial Proteins - chemistry | Substrate Specificity | Endo-1,3-beta-Glucanase - antagonists & inhibitors | Phylogeny | Cellulose - chemistry | Cellulase - metabolism | Enzyme Inhibitors - chemistry | Apoenzymes - metabolism | Glycoside Hydrolases - chemistry | Glucans - metabolism | Apoenzymes - antagonists & inhibitors | Glycoside Hydrolases - antagonists & inhibitors | Recombinant Proteins - metabolism | Bacterial Proteins - antagonists & inhibitors | Catalytic Domain | Biocatalysis | Enzyme Inhibitors - metabolism | Bacterial Proteins - genetics | Enzyme Inhibitors - pharmacology | Endo-1,3-beta-Glucanase - metabolism | Models, Molecular | Recombinant Proteins - chemistry | Hot Temperature | Endo-1,3-beta-Glucanase - genetics | Xylans - chemistry | Apoenzymes - genetics | Apoenzymes - chemistry | Bacterial Proteins - metabolism | Protein Conformation | Glucans - chemistry | Glycoside Hydrolases - metabolism | Mutation | Prevotella - enzymology | Amino Acid Substitution | Cellulose - metabolism | Hydrogen-Ion Concentration | Index Medicus | Life Sciences | Biomolecules | Quantitative Methods | Biochemistry, Molecular Biology
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 2017, Volume 292, Issue 32, pp. 13154 - 13167
In many Gram-negative bacteria, including Rhodobacter capsulatus, cytochrome c maturation (Ccm) is carried out by a membrane-integral machinery composed of... 
SYSTEM | NULL MUTANTS | PROTEIN | APOCYTOCHROME-C | BIOGENESIS DEFECT | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI CCMG | THIOREDOXIN REDUCTASE | CATALYTIC MECHANISM | DISULFIDE | RHODOBACTER-CAPSULATUS | Heme - metabolism | Stereoisomerism | Protein Multimerization | Bacterial Proteins - chemistry | Recombinant Fusion Proteins - metabolism | Cystine - chemistry | Cytochromes c - chemistry | Apoenzymes - metabolism | Cysteine - metabolism | Protein Interaction Domains and Motifs | Binding Sites | Peptide Fragments - genetics | Bacterial Outer Membrane Proteins - genetics | Protein Disulfide Reductase (Glutathione) - metabolism | Recombinant Proteins - metabolism | Peptide Fragments - metabolism | Oxidation-Reduction | Rhodobacter capsulatus - enzymology | Cytochromes c - metabolism | Bacterial Proteins - genetics | Bacterial Outer Membrane Proteins - chemistry | Recombinant Proteins - chemistry | Cysteine - chemistry | Recombinant Fusion Proteins - chemistry | Protein Disulfide Reductase (Glutathione) - chemistry | Peptide Fragments - chemistry | Protein Disulfide Reductase (Glutathione) - genetics | Bacterial Outer Membrane Proteins - metabolism | Models, Biological | Cystine - metabolism | Apoenzymes - chemistry | Bacterial Proteins - metabolism | Mutation | Amino Acid Substitution | Index Medicus | Life Sciences | Biochemistry, Molecular Biology | Biochemistry & Molecular Biology | thiol | Rhodobacter capsulatus | cytochrome c maturation | thiol–disulfide exchange | Bioenergetics | disulfide | heme | thioreduction | protein–protein interaction | apocytochrome | cytochrome c
Journal Article
Acta Crystallographica Section F, ISSN 2053-230X, 10/2018, Volume 74, Issue 10, pp. 617 - 624
Malate dehydrogenase (MDH), a carbohydrate and energy metabolism enzyme in eukaryotes, catalyzes the interconversion of malate to oxaloacetate (OAA) in... 
glyoxysome | fatty‐acid β‐oxidation | malate dehydrogenase | Saccharomyces cerevisiae | X‐ray crystallography | MDH3 | X-ray crystallography | fatty-acid β-oxidation | CATALYSIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | BIOCHEMICAL RESEARCH METHODS | CRYSTALLOGRAPHY | PORCINE HEART | BACILLUS-STEAROTHERMOPHILUS | ANGSTROM RESOLUTION | TERNARY COMPLEX | BIOPHYSICS | ALIGNMENT | SEQUENCE | CITRATE | STEAROTHERMOPHILUS LACTATE-DEHYDROGENASE | REFINED CRYSTAL-STRUCTURE | fatty-acid beta-oxidation | Protein Multimerization | Substrate Specificity | Crystallography, X-Ray | Isoenzymes - chemistry | Malate Dehydrogenase - genetics | NAD - chemistry | Glyoxysomes - chemistry | Isoenzymes - metabolism | Apoenzymes - metabolism | Cloning, Molecular | Escherichia coli - metabolism | Malates - metabolism | Protein Interaction Domains and Motifs | NAD - metabolism | Malate Dehydrogenase - metabolism | Recombinant Proteins - metabolism | Amino Acid Sequence | Protein Conformation, alpha-Helical | Catalytic Domain | Gene Expression | Genetic Vectors - chemistry | Isoenzymes - genetics | Oxaloacetic Acid - metabolism | Glyoxysomes - enzymology | Genetic Vectors - metabolism | Models, Molecular | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Oxaloacetic Acid - chemistry | Saccharomyces cerevisiae Proteins - genetics | Saccharomyces cerevisiae - chemistry | Sequence Homology, Amino Acid | Malates - chemistry | Sequence Alignment | Protein Conformation, beta-Strand | Escherichia coli - genetics | Apoenzymes - genetics | Saccharomyces cerevisiae Proteins - metabolism | Apoenzymes - chemistry | Protein Binding | Saccharomyces cerevisiae - enzymology | Malate Dehydrogenase - chemistry | Saccharomyces cerevisiae Proteins - chemistry | Tricarboxylic acid cycle | Energy metabolism | Yeast | Dehydrogenases | Saccharomyces | Dehydrogenase | Eukaryotes | Mitochondria | NADH | Oxidation | Glyoxylate cycle | Crystal structure | Carbohydrates | Enzymes | Isoenzymes | Carbohydrate metabolism | Malate dehydrogenase | Reoxidation | Metabolism | Acids | Malate | Nicotinamide adenine dinucleotide | Nicotinamide | Conformation | Index Medicus
Journal Article
Journal Article