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1. Full Text Site-directed mutagenesis of methionine residues for improving the oxidative stability of α-amylase from Thermotoga maritima
by Ozturk, Handan and Ece, Selin and Gundeger, Ersin and Evran, Serap
Journal of Bioscience and Bioengineering, ISSN 1389-1723, 10/2013, Volume 116, Issue 4, pp. 449 - 451
The oxidative stability of α-amylase (AmyC) from was improved by mutating the methionine residues at positions 43 and 44, 55, and 62 to oxidative-resistant... 
Protein engineering | α-Amylase | Oxidative stability | Thermotoga maritima | Site-directed mutagenesis of methionine | REPLACEMENT | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | ENZYMES | FOOD SCIENCE & TECHNOLOGY | RESISTANCE | alpha-Amylase | HYDROGEN-PEROXIDE | Mutagenesis, Site-Directed | Methionine - metabolism | Hydrogen Peroxide - pharmacology | Models, Molecular | Alanine - metabolism | Thermotoga maritima - genetics | alpha-Amylases - metabolism | Enzyme Stability - drug effects | Thermotoga maritima - enzymology | alpha-Amylases - genetics | Alanine - genetics | alpha-Amylases - chemistry | Oxidation-Reduction - drug effects | Methionine - genetics | Index Medicus
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2. Full Text The Iron-Hydrogenase of Thermotoga maritima Utilizes Ferredoxin and NADH Synergistically: a New Perspective on Anaerobic Hydrogen Production
by Gerrit J. Schut and Michael W. W. Adams
Journal of Bacteriology, ISSN 0021-9193, 07/2009, Volume 191, Issue 13, pp. 4451 - 4457
Article Usage Stats Services JB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley... 
SP-NOV REPRESENTS | PYRUVATE | HYPERTHERMOPHILIC-BACTERIUM | CLOSTRIDIUM-KLUYVERI | OXIDOREDUCTASE | CLASSIFICATION | MICROBIOLOGY | EMBDEN-MEYERHOF | PYROCOCCUS-FURIOSUS | ENERGY-CONSERVATION | GENOME | Anaerobiosis | Hydrogenase - genetics | Ferredoxins - metabolism | Bacterial Proteins - genetics | Iron-Sulfur Proteins - genetics | Thermotoga maritima - genetics | Thermotoga maritima - enzymology | Genome, Bacterial - genetics | Hydrogenase - metabolism | Models, Biological | Bacterial Proteins - metabolism | Iron-Sulfur Proteins - metabolism | Thermotoga maritima - metabolism | Hydrogen - metabolism | NAD - metabolism | Physiological aspects | Research | Microbial metabolism | Bacteria, Thermophilic | Physiology and Metabolism
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3. Full Text Structural Insight into Partner Specificity and Phosphoryl Transfer in Two-Component Signal Transduction
by Casino, Patricia and Rubio, Vicente and Marina, Alberto
Cell, ISSN 0092-8674, 2009, Volume 139, Issue 2, pp. 325 - 336
The chief mechanism used by bacteria for sensing their environment is based on two conserved proteins: a sensor histidine kinase (HK) and an effector response... 
MICROBIO | SIGNALING | HISTIDINE KINASE ENVZ | DOMAIN | COMPLEX | PHOSPHATASE-ACTIVITY | CRYSTAL-STRUCTURE | MOLECULAR RECOGNITION | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | SELENOMETHIONYL PROTEINS | SENSOR | RESPONSE REGULATOR | CELL BIOLOGY | Amino Acid Sequence | Phosphorylation | Sequence Alignment | Signal Transduction | Bacterial Proteins - chemistry | Models, Molecular | Molecular Sequence Data | Crystallography, X-Ray | Protein Interaction Domains and Motifs | Thermotoga maritima - chemistry | Thermotoga maritima - enzymology | Thermotoga maritima - metabolism | Proteins | Phosphatases | Histidine
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4. Full Text X-ray Structure of the [FeFe]-Hydrogenase Maturase HydE from Thermotoga maritima
by Yvain Nicolet and Jon K. Rubach and Matthew C. Posewitz and Patricia Amara and Carole Mathevon and Mohamed Atta and Marc Fontecave and Juan C. Fontecilla-Camps
Journal of Biological Chemistry, ISSN 0021-9258, 07/2008, Volume 283, Issue 27, pp. 18861 - 18872
Maturation of the [FeFe]-hydrogenase active site depends on at least the expression of three gene products called HydE, HydF, and HydG. We have solved the high... 
BIOTIN SYNTHASE | RADICAL MECHANISMS | S-ADENOSYLMETHIONINE | IRON-SULFUR-CLUSTER | FE-ONLY HYDROGENASE | ACTIVE-SITE FE | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | DESULFOVIBRIO-DESULFURICANS | MOLECULAR GRAPHICS | Bacterial Proteins - chemistry | Iron-Sulfur Proteins - genetics | Crystallography, X-Ray | Iron-Sulfur Proteins - chemistry | Thermotoga maritima - enzymology | Adenosine - genetics | Binding Sites - physiology | Water - chemistry | Free Radicals - metabolism | Adenosine - chemistry | Clostridium acetobutylicum - enzymology | Ethionine - analogs & derivatives | Recombinant Proteins - metabolism | Clostridium acetobutylicum - genetics | Free Radicals - chemistry | Ethionine - genetics | Iron - chemistry | Bacterial Proteins - genetics | Water - metabolism | Recombinant Proteins - chemistry | Ethionine - chemistry | Recombinant Proteins - genetics | Thermotoga maritima - genetics | Iron - metabolism | Ethionine - metabolism | Adenosine - analogs & derivatives | Adenosine - metabolism | Bacterial Proteins - metabolism | Iron-Sulfur Proteins - metabolism | Structural Homology, Protein | Protein Structure, Tertiary - physiology | Index Medicus | Inorganic chemistry | Chemical Sciences
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5. Full Text The Three-dimensional Structure of Invertase (β-Fructosidase) from Thermotoga maritima Reveals a Bimodular Arrangement and an Evolutionary Relationship between Retaining and Inverting Glycosidases
by François Alberto and Christophe Bignon and Gerlind Sulzenbacher and Bernard Henrissat and Mirjam Czjzek
Journal of Biological Chemistry, ISSN 0021-9258, 04/2004, Volume 279, Issue 18, pp. 18903 - 18910
Thermotoga maritima invertase (β-fructosidase) hydrolyzes sucrose to release fructose and glucose, which are major carbon and energy sources for both... 
FOLD | NEURAMINIDASE | GENE | ACTIVE-SITE | CRYSTAL-STRUCTURE | DENSITY MODIFICATION | YEAST INVERTASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | SEQUENCE | MECHANISMS | GLYCOSYL HYDROLASES | Amino Acid Sequence | Catalytic Domain | Sequence Alignment | beta-Fructofuranosidase - chemistry | Glycoside Hydrolases - genetics | Glycoside Hydrolases - chemistry | Crystallography, X-Ray | Protein Conformation | Molecular Structure | Thermotoga maritima - enzymology | Evolution, Molecular | beta-Fructofuranosidase - genetics | Life Sciences | Biomolecules | Biochemistry, Molecular Biology
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6. Full Text Structural basis of enzyme encapsulation into a bacterial nanocompartment
by Sutter, Markus and Boehringer, Daniel and Gutmann, Sascha and Günther, Susanne and Prangishvili, David and Loessner, Martin J and Stetter, Karl O and Weber-Ban, Eilika and Ban, Nenad
Nature Structural and Molecular Biology, ISSN 1545-9993, 09/2008, Volume 15, Issue 9, pp. 939 - 947
Compartmentalization is an important organizational feature of life. It occurs at varying levels of complexity ranging from eukaryotic organelles and the... 
ANGULAR RECONSTITUTION | PROTEIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | RESOLUTION | CRYSTAL-STRUCTURES | CELL BIOLOGY | PEROXIDASE | BIOPHYSICS | BREVIBACTERIUM LINENS | SEQUENCE | THERMOTOGA-MARITIMA | FERRITIN | CARBOXYSOME SHELL | Amino Acid Sequence | Brevibacterium - genetics | Bacterial Proteins - chemistry | Bacterial Proteins - genetics | Models, Molecular | Molecular Sequence Data | Recombinant Proteins - chemistry | Crystallography, X-Ray | Brevibacterium - enzymology | Recombinant Proteins - genetics | Thermotoga maritima - genetics | Thermotoga maritima - enzymology | Thermotoga maritima - ultrastructure | Brevibacterium - ultrastructure | Sequence Homology, Amino Acid | Multiprotein Complexes - chemistry | Organelles - ultrastructure | Organelles - enzymology | Binding Sites | Enzymes | Bacterial proteins | Physiological aspects | Cell physiology | Research | Structure | Properties | Bacteria | Molecular biology | Binding sites | Crystal structure
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7. Full Text Structural Dissection of the Active Site of Thermotoga maritima β-Galactosidase Identifies Key Residues for Transglycosylating Activity
by Talens-Perales, David and Polaina, Julio and Marín-Navarro, Julia
Journal of Agricultural and Food Chemistry, ISSN 0021-8561, 04/2016, Volume 64, Issue 14, pp. 2917 - 2924
Glycoside hydrolases, specifically beta-galactosidases, can be used to synthesize galacto-oligosaccharides (GOS) due to the transglycosylating (secondary)... 
enzyme engineering | prebiotics | GH2 glycoside hydrolase | galacto-oligosaccharides | BACILLUS-CIRCULANS | FOOD SCIENCE & TECHNOLOGY | ESCHERICHIA-COLI | SULFOLOBUS-SOLFATARICUS | LACTOSE | ENZYMATIC-SYNTHESIS | TRANSITION-STATE | ASPERGILLUS-ORYZAE | PYROCOCCUS-FURIOSUS | OLIGOSACCHARIDE PRODUCTION | AGRICULTURE, MULTIDISCIPLINARY | LAC OPERON INDUCER | CHEMISTRY, APPLIED | Catalytic Domain | Galactose - metabolism | Mutagenesis, Site-Directed | Bacterial Proteins - chemistry | Bacterial Proteins - genetics | Glycosylation | Thermotoga maritima - genetics | Oligosaccharides - metabolism | Thermotoga maritima - enzymology | Amino Acid Motifs | beta-Galactosidase - metabolism | Bacterial Proteins - metabolism | beta-Galactosidase - chemistry | beta-Galactosidase - genetics | Thermotoga maritima - chemistry | Index Medicus
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8. Full Text The latch modulates nucleotide and DNA binding to the helicase-like domain of Thermotoga maritima reverse gyrase and is required for positive DNA supercoiling
by Ganguly, Agneyo and Del Toro Duany, Yoandris and Rudolph, Markus G and Klostermeier, Dagmar
Nucleic Acids Research, ISSN 0305-1048, 03/2011, Volume 39, Issue 5, pp. 1789 - 1800
Reverse gyrase is the only topoisomerase that can introduce positive supercoils into DNA in an ATP-dependent process. It has a modular structure and harnesses... 
RHO | MECHANISM | BIOCHEMISTRY & MOLECULAR BIOLOGY | TOPOISOMERASE | Protein Structure, Tertiary | DNA Helicases - chemistry | Sequence Deletion | DNA Topoisomerases, Type I - metabolism | DNA, Single-Stranded - metabolism | Bacterial Proteins - chemistry | Bacterial Proteins - genetics | DNA Topoisomerases, Type I - chemistry | DNA Topoisomerases, Type I - genetics | DNA - metabolism | Nucleotides - metabolism | Thermotoga maritima - enzymology | Protein Binding | Bacterial Proteins - metabolism | DNA, Superhelical - metabolism | Nucleic Acid Enzymes
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9. Full Text Novel inositol catabolic pathway in Thermotoga maritima
by Rodionova, Irina A and Leyn, Semen A and Burkart, Michael D and Boucher, Nathalie and Noll, Kenneth M and Osterman, Andrei L and Rodionov, Dmitry A
Environmental Microbiology, ISSN 1462-2912, 08/2013, Volume 15, Issue 8, pp. 2254 - 2266
Summary myo‐inositol (MI) is a key sugar alcohol component of various metabolites, e.g. phosphatidylinositol‐based phospholipids that are abundant in animal... 
ORGANIZATION | PROTEIN | EVOLUTION | MYOINOSITOL CATABOLISM | BACILLUS-SUBTILIS | BIOSYNTHESIS | MICROBIOLOGY | 3-EPIMERASE | ABC TRANSPORTERS | OPERON | IDENTIFICATION | Multigene Family | Inositol - metabolism | Substrate Specificity | Bacillus subtilis - enzymology | Thermotoga maritima - genetics | Thermotoga maritima - enzymology | Bacillus subtilis - genetics | Hydrolysis | Inositol - chemistry | Enzymes - genetics | Protein Binding | Gene Order | Thermotoga maritima - metabolism | Enzymes - metabolism | Phosphates | Enzymes | Inositol | Metabolites | Blood lipids | Plant lipids | Recombinant proteins | Soil microbiology | Microbiology | Bacteriology | Dehydrogenases
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10. Full Text Constitutive high-level expression of a codon-optimized β-fructosidase gene from the hyperthermophile Thermotoga maritima in Pichia pastoris
by Menéndez, Carmen and Martínez, Duniesky and Trujillo, Luis E and Mazola, Yuliet and González, Ernesto and Pérez, Enrique R and Hernández, Lázaro
Applied Microbiology and Biotechnology, ISSN 0175-7598, 2/2013, Volume 97, Issue 3, pp. 1201 - 1212
Enzymes for use in the sugar industry are preferred to be thermotolerant. In this study, a synthetic codon-optimized gene encoding a highly thermostable... 
Biotechnology | Chemistry | GAP promoter | Microbiology | Microbial Genetics and Genomics | Thermotoga maritima | Invertase | Fructosidase | Invert sugar | Pichia pastoris | PLANT | METHYLOTROPHIC YEAST | ESCHERICHIA-COLI | HYDROLYSIS | LEVANASE | GLYCOSYLATION | SACCHAROMYCES-CEREVISIAE | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | SUCROSE | SECRETION | Carbon - metabolism | Gene Expression | Temperature | beta-Fructofuranosidase - chemistry | Carbohydrate Metabolism | Enzyme Stability | Substrate Specificity | Gene Dosage | Recombinant Proteins - genetics | Thermotoga maritima - genetics | Biomass | Recombinant Proteins - biosynthesis | Fermentation | Thermotoga maritima - enzymology | Pichia - enzymology | beta-Fructofuranosidase - genetics | Pichia - metabolism | Codon | beta-Fructofuranosidase - biosynthesis | Pichia - genetics | Kinetics | Pichia - growth & development | Index Medicus | A-factor
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11. Full Text Biomimetic assembly and activation of [FeFe]-hydrogenases
by Berggren, G and Adamska, A and Lambertz, C and Simmons, T.R and Esselborn, J and Atta, M and Gambarelli, S and Mouesca, J.-M and Reijerse, E and Lubitz, W and Happe, T and Artero, V and Fontecave, M
Nature, ISSN 0028-0836, 2013, Volume 499, Issue 7456, pp. 66 - 69
Hydrogenases are the most active molecular catalysts for hydrogen production and uptake(1,2), and could therefore facilitate the development of new types of... 
S-ADENOSYLMETHIONINE | FE-ONLY HYDROGENASE | ACTIVE-SITE | CHLAMYDOMONAS-REINHARDTII | MULTIDISCIPLINARY SCIENCES | DESULFOVIBRIO-DESULFURICANS | COORDINATION | IRON | LINKAGE ISOMERISM | BIOFUEL CELL | H-CLUSTER | Apoproteins - chemistry | Biomimetic Materials - chemical synthesis | Catalytic Domain | Clostridium acetobutylicum - genetics | Biocatalysis | Electron Spin Resonance Spectroscopy | Spectroscopy, Fourier Transform Infrared | Thermotoga maritima - enzymology | Biomimetic Materials - metabolism | Hydrogenase - metabolism | Biomimetics | Clostridium acetobutylicum - metabolism | Chlamydomonas reinhardtii - enzymology | Ligands | Enzyme Activation | Apoproteins - metabolism | Research | Hydrogenation | Enzyme activation | Proteins | Fourier transforms | E coli | Mutagenesis | Spectrum analysis | Nitrogen | Experiments | Binding sites | Inorganic chemistry | Material chemistry | Chemical Sciences | Naturvetenskap | Natural Sciences
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12. Full Text Semi-rational engineering of a thermostable aldo-keto reductase from Thermotoga maritima for synthesis of enantiopure ethyl-2-hydroxy-4-phenylbutyrate (EHPB)
by Wang, Zhiguo and Zhou, Shuo and Zhang, Shuangling and Zhang, Sa and Zhu, Fangmeng and Jin, Xiaolu and Chen, Zhenming and Xu, Xiaoling
Scientific Reports, ISSN 2045-2322, 12/2017, Volume 7, Issue 1, pp. 4007 - 11
A novel aldo-keto reductase Tm1743 characterized from Thermotoga maritima was explored as an effective biocatalyst in chiral alcohol production. Natural Tm1743... 
CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | CHIRAL ALCOHOLS | INTERMEDIATE | INHIBITORS | MODEL | CATALYTIC MECHANISM | SELECTIVITY | Enzymes - chemistry | Aldo-Keto Reductases - genetics | Aldo-Keto Reductases - chemistry | Enzyme Stability | Substrate Specificity | Crystallography, X-Ray | Thermotoga maritima - genetics | Hot Temperature | Thermotoga maritima - enzymology | Mutagenesis | Enzymes - genetics | Phenylbutyrates - chemistry | Protein Engineering | Molecular modelling | Catalysts | Angiotensin | Exploration | NADP | Saturation mutagenesis | Enantiomers | Biocatalysts | Phenylbutyric acid | Aldo-keto reductase | Crystal structure
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13. Full Text Reduction of Folate by Dihydrofolate Reductase from Thermotoga maritima
by Loveridge, E Joel and Hroch, Lukas and Hughes, Robert L and Williams, Thomas and Davies, Rhidian L and Angelastro, Antonio and Luk, Louis Y P and Maglia, Giovanni and Allemann, Rudolf K
Biochemistry, ISSN 0006-2960, 03/2017, Volume 56, Issue 13, pp. 1879 - 1886
Mammalian dihydrofolate reductases (DHFR) catalyse the reduction of folate more efficiently than the equivalent bacterial enzymes, despite typically having... 
MUTANTS | ENZYME CATALYSIS | CRYSTAL-STRUCTURE | STABILITY | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | DYNAMICS | CATALYTIC MECHANISM | FOLIC-ACID | MOTIONS | HYDRIDE TRANSFER | Protons | Temperature | Species Specificity | Tetrahydrofolate Dehydrogenase - chemistry | Bacterial Proteins - chemistry | NADP - chemistry | Thermotoga maritima - enzymology | Thermodynamics | NADP - metabolism | Thermotoga maritima - chemistry | Catalytic Domain | Gene Expression | Escherichia coli - enzymology | Oxidation-Reduction | Protein Structure, Secondary | Bacterial Proteins - genetics | Folic Acid - chemistry | Thermotoga maritima - genetics | Escherichia coli - chemistry | Protein Folding | Tetrahydrofolate Dehydrogenase - metabolism | Tetrahydrofolates - metabolism | Escherichia coli - genetics | Folic Acid - metabolism | Bacterial Proteins - metabolism | Tetrahydrofolates - chemistry | Kinetics | Hydrogen-Ion Concentration | Tetrahydrofolate Dehydrogenase - genetics | Usage | Nuclear magnetic resonance spectroscopy | Oxidation-reduction reaction | Catalysis | Chemical properties | Mass spectrometry | Folic acid
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14. Full Text Identification of the ATPase subunit of the primary maltose transporter in the hyperthermophilic anaerobe Thermotoga maritima
by Singh, Raghuveer and White, Derrick and Blum, Paul
Applied and Environmental Microbiology, ISSN 0099-2240, 09/2017, Volume 83, Issue 18
Thermotoga maritima is a hyperthermophilic anaerobic bacterium that produces molecular hydrogen (H-2) by fermentation. It catabolizes a broad range of... 
Genetic systems | Hyperthermophile | Maltose | Hydrogen | ABC transporter | Homologous recombination | SYSTEM | genetic systems | ESCHERICHIA-COLI | MICROBIOLOGY | NUCLEOTIDE-BINDING | GLUCOSE-TRANSPORT | hydrogen | hyperthermophile | maltose | ARCHAEON THERMOCOCCUS-LITORALIS | EXPRESSION PATTERNS | homologous recombination | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | MALK GENE | MUTATIONS | PROTEINS | Anaerobiosis | Maltose - metabolism | Bacterial Proteins - genetics | Adenosine Triphosphatases - metabolism | Thermotoga maritima - genetics | Hot Temperature | Thermotoga maritima - enzymology | Protein Subunits - metabolism | Biological Transport | Bacterial Proteins - metabolism | Adenosine Triphosphatases - genetics | Mutation | Thermotoga maritima - metabolism | Protein Subunits - genetics | Thermotogales | Research | Microbial metabolism | Sugars | Adenosine triphosphatase | Microbial mutation
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15. Full Text Structure of a bacterial ribonuclease P holoenzyme in complex with tRNA
by Reiter, Nicholas J and Osterman, Amy and Torres-Larios, Alfredo and Swinger, Kerren K and Pan, Tao and Mondragón, Alfonso
Nature, ISSN 0028-0836, 12/2010, Volume 468, Issue 7325, pp. 784 - 791
Ribonuclease (RNase) P is the universal ribozyme responsible for 5'-end tRNA processing. We report the crystal structure of the Thermotoga maritima RNase P... 
PROTEIN-COMPONENT | 2-METAL-ION MECHANISM | ACTIVE-SITE | CRYSTAL-STRUCTURE | SUBSTRATE | MULTIDISCIPLINARY SCIENCES | PRECURSOR TRANSFER-RNA | ESCHERICHIA-COLI | BINDING-SITE | THERMOTOGA-MARITIMA | CONSERVED CORE | RNA, Transfer, Phe - metabolism | Catalytic Domain | Biocatalysis | RNA, Transfer, Phe - chemistry | Genes, Bacterial - genetics | RNA, Transfer, Phe - genetics | Molecular Conformation | Ribonuclease P - chemistry | Models, Molecular | Substrate Specificity | Crystallography, X-Ray | Holoenzymes - chemistry | Structure-Activity Relationship | Thermotoga maritima - genetics | Thermotoga maritima - enzymology | Ribonuclease P - genetics | Ribonuclease P - metabolism | Metals - metabolism | Holoenzymes - metabolism | Holoenzymes - genetics | Crystals | Ribonuclease | Research | Properties | Bacterial genetics | Structure | Observations | Transfer RNA | Proteins | Enzymes | Cellular biology | Ribonucleic acid--RNA | Molecular biology | Bacteriology
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16. Full Text Synthesis of a Fucosylated Trisaccharide Via Transglycosylation by α-l-Fucosidase from Thermotoga maritima
by Guzmán-Rodríguez, Francisco and Alatorre-Santamaría, Sergio and Gómez-Ruiz, Lorena and Rodríguez-Serrano, Gabriela and García-Garibay, Mariano and Cruz-Guerrero, Alma
Applied Biochemistry and Biotechnology, ISSN 0273-2289, 11/2018, Volume 186, Issue 3, pp. 681 - 691
Fucosylated oligosaccharides, such as 2′-fucosyllactose in human milk, have important biological functions such as prebiotics and preventing infection. In this... 
Biochemistry, general | Transglycosylation | Biotechnology | Chemistry | Thermotoga maritima | Fucosidase | Fucosyllactose | PROTECTION | DISACCHARIDES | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | LACTOSE | TRANSFERASES | BREAST | ENZYME | BIOTECHNOLOGY & APPLIED MICROBIOLOGY |