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1. Full Text phoD alkaline phosphatase gene diversity in soil
by Ragot, Sabine A and Kertesz, Michael A and Bünemann, Else K
Applied and Environmental Microbiology, ISSN 0099-2240, 2015, Volume 81, Issue 20, pp. 7281 - 7289
Phosphatase enzymes are responsible for much of the recycling of organic phosphorus in soils. The PhoD alkaline phosphatase takes part in this process by... 
BACTERIAL COMMUNITY | LIBRARIES | PHOSPHORUS FERTILIZATION | MANAGEMENT | SEQUENCES | ALIGNMENT | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | NITROGEN | PRIMERS | MICROBIOLOGY | SUCCESSION | RHIZOSPHERE | Xanthomonadaceae - enzymology | Bacillales - enzymology | Alkaline Phosphatase - genetics | Soil Microbiology | Deinococcus - enzymology | Genetic Variation - genetics | Planctomycetales - enzymology | Actinomycetales - enzymology | Usage | Phosphatases | Research | Nucleotide sequencing | Soil microbiology | Biological diversity | DNA sequencing | Enzymes | Soils | Phosphorus | Genomes | Genetic diversity | Recycling | Index Medicus | Environmental Microbiology
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2. Full Text Salix purpurea stimulates the expression of specific bacterial xenobiotic degradation genes in a soil contaminated with hydrocarbons
by Pagé, Antoine P and Yergeau, Étienne and Greer, Charles W
PLoS ONE, ISSN 1932-6203, 07/2015, Volume 10, Issue 7, pp. e0132062 - e0132062
The objectives of this study were to uncover Salix purpurea-microbe xenobiotic degradation systems that could be harnessed in rhizoremediation, and to identify... 
PLANT-ROOT EXTRACTS | PAH DEGRADATION | POLYCYCLIC AROMATIC-HYDROCARBONS | PETROLEUM-HYDROCARBONS | MULTIDISCIPLINARY SCIENCES | PHYTOREMEDIATION SYSTEM | RHIZOSPHERE | CROP PLANTS | POLYCHLORINATED-BIPHENYLS | DEGRADING BACTERIA | CO2 EVOLUTION | Burkholderiaceae - enzymology | Burkholderiaceae - genetics | Cytochrome P-450 Enzyme System - metabolism | Iron-Sulfur Proteins - genetics | Soil Pollutants - analysis | Salix - physiology | Actinomycetales - genetics | Oxygenases - metabolism | Rhodospirillales - genetics | Cytochrome P-450 CYP4A - genetics | Caulobacteraceae - enzymology | Xenobiotics | Rhodospirillales - enzymology | Biodegradation, Environmental | Genes, Bacterial | Cytochrome P-450 CYP4A - metabolism | Bacterial Proteins - genetics | Actinomycetales - enzymology | Laccase - genetics | Laccase - metabolism | Petroleum Pollution - analysis | Alteromonadaceae - genetics | Metabolic Networks and Pathways | Cytochrome P-450 Enzyme System - genetics | Bacterial Proteins - metabolism | Iron-Sulfur Proteins - metabolism | Oxygenases - genetics | Rhizobiaceae - enzymology | Gene Expression Regulation, Bacterial | Alteromonadaceae - enzymology | Caulobacteraceae - genetics | Rhizobiaceae - genetics | Oxidases | Polychlorinated biphenyls | Bacterial genetics | Gene expression | Genes | Cytochrome | Laboratories | Hydrocarbons | Alkanes | Partnerships | Benzo(a)pyrene | Soil pollution | Molecular weight | Consortia | Datasets | Degradation | PCB compounds | Taxa | Microorganisms | Biphenyl | Bacteria | Bioremediation | Laccase | Soil contamination | Biodegradation | Anthracene | Cytochrome P450 | Detoxification | Soil degradation | Plant communities | Sediment pollution | PCB | Oxygenase | Rhizosphere | Pyrene | Soils | Contaminants | Biphenyl 2,3-dioxygenase | Willow | Environmental degradation | Polychlorinated biphenyls--PCB | Genetic engineering | Exudation | Fluoranthene | Index Medicus
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3. Full Text Purification and biochemical characterization of a detergent-stable keratinase from a newly thermophilic actinomycete Actinomadura keratinilytica strain Cpt29 isolated from poultry compost
by Habbeche, Amina and Saoudi, Boudjema and Jaouadi, Bassem and Haberra, Soumaya and Kerouaz, Bilal and Boudelaa, Mokhtar and Badis, Abdelmalek and Ladjama, Ali
Journal of Bioscience and Bioengineering, ISSN 1389-1723, 04/2014, Volume 117, Issue 4, pp. 413 - 421
An extracellular thermostable keratinase (KERAK-29) was purified and biochemically characterized from a thermophilic actinomycete  strain Cpt29 newly isolated... 
Keratinase | KERAK-29 | Streptomyces | Keratin hydrolysis | Actinomadura | Protease | FOOD SCIENCE & TECHNOLOGY | PROTEOLYTIC-ENZYMES | ALKALINE PROTEASE | IDENTIFICATION | STREPTOMYCES SP | AMINO-ACID-SEQUENCE | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | KERATINOLYTIC SERINE PROTEINASE | BACTERIUM | OPTIMIZATION | EXTRACELLULAR KERATINASE | EXPRESSION | Temperature | Molecular Weight | Poultry - microbiology | Molecular Sequence Data | Substrate Specificity | Enzyme Stability - drug effects | Phylogeny | Feathers - metabolism | Keratins - metabolism | Serine Proteases - chemistry | Manganese - pharmacology | Serine Proteinase Inhibitors - pharmacology | Peptide Hydrolases - metabolism | Serine Proteases - metabolism | Amino Acid Sequence | Detergents - pharmacology | Soil Microbiology | Peptide Hydrolases - chemistry | Actinomycetales - enzymology | Hydrolysis | Animals | Peptide Hydrolases - isolation & purification | Streptomyces - enzymology | Kinetics | Hydrogen-Ion Concentration | Biodegradation | Keratin | Poultry industry | Detergents, Synthetic | Ionization | Proteases | Analysis | Chemical properties | Mass spectrometry | Index Medicus
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4. Full Text Comparison of genetic structures and biochemical properties of tandem cutinase-type polyesterases from Thermobifida alba AHK119
by Thumarat, Uschara and Kawabata, Takeshi and Nakajima, Hajime and Nakajima, Maho and Sugiyama, Akifumi and Yazaki, Kazufumi and Tada, Tomoko and Waku, Tomonori and Tanaka, Naoki and Kawai, Fusako
Journal of Bioscience and Bioengineering, ISSN 1389-1723, 11/2015, Volume 120, Issue 5, pp. 491 - 497
This study described the genetic map of tandem genes ( and ) encoding cutinase-type polyesterases in AHK119 and comparison of wild type and mutant enzymes of... 
Thermostable cutinase | Thermobifida alba AHK119 | PET surface hydrolysis | Ca-activated cutinase | Cutinase-type polyesterase | Tandem genes regulation | FUSCA | ALIPHATIC-AROMATIC COPOLYESTERS | STABILITY | FOOD SCIENCE & TECHNOLOGY | PROTEIN THERMOSTABILITY | HYDROLASE | AMINO-ACID | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | DEGRADATION | LIPASE | PROLINE | RESIDUES | Amino Acid Sequence | Butyrates - metabolism | Temperature | Calcium - pharmacology | Carboxylic Ester Hydrolases - chemistry | Genes, Bacterial - genetics | Molecular Sequence Data | Substrate Specificity | Enzyme Stability - drug effects | Actinomycetales - enzymology | Hydrolysis | Polyesters - chemistry | Polyesters - metabolism | Actinomycetales - genetics | Conserved Sequence | Carboxylic Ester Hydrolases - genetics | Carboxylic Ester Hydrolases - metabolism | Enzymes | Ethylene glycol | Plant genetics | Terephthalic acid | Proline | Genetic research | Esters | Comparative analysis | Index Medicus
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5. Full Text Cloning of a thermostable xylanase from Actinomadura sp. S14 and its expression in Escherichia coli and Pichia pastoris
by Sriyapai, Thayat and Somyoonsap, Peechapack and Matsui, Kenji and Kawai, Fusako and Chansiri, Kosum
Journal of Bioscience and Bioengineering, ISSN 1389-1723, 2011, Volume 111, Issue 5, pp. 528 - 536
A thermophilic xylan-degrading sp. S14 was isolated from compost in Thailand. Hemicellulase activities such as endo-1,4-β-xylanase, β-xylosidase and... 
Family 11 glycoside hydrolase | Pichia pastoris-expression | Hemicellulases | Thermostable xylanase | Actinomadura sp. S14 | TRICHODERMA-REESEI | FOOD SCIENCE & TECHNOLOGY | FLEXUOSA | Actinomadura sp S14 | STREPTOMYCES SP | GENE | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | FAMILIES | PURIFICATION | SEQUENCE | PROTEINS | ALKALINE XYLANASE | Amino Acid Sequence | Endo-1,4-beta Xylanases - metabolism | Temperature | Xylans - metabolism | Glycoside Hydrolases - genetics | Endo-1,4-beta Xylanases - genetics | Molecular Sequence Data | Substrate Specificity | Recombinant Proteins - genetics | Fungal Proteins - genetics | Recombinant Proteins - biosynthesis | Thailand | Actinomycetales - enzymology | Pichia - metabolism | Actinomycetales - genetics | Escherichia coli - genetics | Base Sequence | Cloning, Molecular | Escherichia coli - metabolism | Pichia - genetics | Glycoside Hydrolases - metabolism | Trisaccharides - metabolism | Fungal Proteins - metabolism | Hydrogen-Ion Concentration | Index Medicus
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6. Full Text Diversity and cold-active hydrolytic enzymes of culturable bacteria associated with Arctic sea ice, Spitzbergen
by Groudieva, Tatiana and Kambourova, Margarita and Yusef, Hoda and Royter, Maryna and Grote, Ralf and Trinks, Hauke and Antranikian, Garabed
Extremophiles, ISSN 1431-0651, 12/2004, Volume 8, Issue 6, pp. 475 - 488
The diversity of culturable bacteria associated with sea ice from four permanently cold fjords of Spitzbergen, Arctic Ocean, was investigated. A total of 116... 
Psychrotolerant bacteria | LifeSciences | Arctic | Cold-active hydrolytic enzymes | Sea ice | ANTARCTICA | cold-active hydrolytic enzymes | SP. NOV | BIOCHEMISTRY & MOLECULAR BIOLOGY | arctic | MICROBIOLOGY | IDENTIFICATION | LOW-TEMPERATURE | GENETIC DIVERSITY | MARINE-SEDIMENTS | MICROBIAL COMMUNITIES | sea ice | PSYCHROPHILIC BACTERIA | psychrotolerant bacteria | SULFATE-REDUCING BACTERIA | ALPHA-AMYLASE | Actinomycetales - classification | Gammaproteobacteria - classification | Phylogeny | Bacteroidetes - enzymology | Gram-Positive Endospore-Forming Rods - genetics | Alphaproteobacteria - enzymology | Actinomycetales - genetics | Bacteria - classification | Gammaproteobacteria - genetics | Gram-Positive Endospore-Forming Rods - enzymology | Actinomycetales - isolation & purification | DNA, Ribosomal - genetics | Alphaproteobacteria - isolation & purification | Bacteroidetes - isolation & purification | Genes, Bacterial | Gammaproteobacteria - enzymology | Seawater - microbiology | Ice | Bacteroidetes - classification | Bacteria - genetics | Actinomycetales - enzymology | Gammaproteobacteria - isolation & purification | Hydrolysis | Alphaproteobacteria - classification | Gram-Positive Endospore-Forming Rods - isolation & purification | Bacteria - isolation & purification | Alphaproteobacteria - genetics | DNA, Bacterial - genetics | Arctic Regions | Norway | Gram-Positive Endospore-Forming Rods - classification | Bacteria - enzymology | Bacteroidetes - genetics | Microbiology | Enzymes | Analysis | Bacteria | Cold | Index Medicus | Space life sciences
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7. Full Text Compartmentalization and regulation of arylsulfatase activities in Streptomyces sp., Microbacterium sp. and Rhodococcus sp. soil isolates in response to inorganic sulfate limitation
by Cregut, Mickael and Piutti, Severine and Slezack-Deschaumes, Sophie and Benizri, Emile
Microbiological Research, ISSN 0944-5013, 01/2013, Volume 168, Issue 1, pp. 12 - 21
Arylsulfatases allow microorganisms to satisfy their sulfur (S) requirements as inorganic sulfate after sulfate ester hydrolysis. Our objectives were to... 
Sulfate limitation | Actinobacteria | Sulfate esters | Arylsulfatase regulation | Arylsulfatase activity | KLEBSIELLA-AEROGENES | ESCHERICHIA-COLI | CYSTEINE | MICROBIOLOGY | FIELD-GROWN RAPE | SULFUR ASSIMILATION | STARVATION RESPONSE | GENE | PSEUDOMONAS-AERUGINOSA | PURIFICATION | PROTEINS | Cytoplasm - enzymology | Sulfates - metabolism | Soil Microbiology | Models, Molecular | Molecular Sequence Data | DNA, Bacterial - chemistry | Phylogeny | Sequence Analysis, DNA | Actinomycetales - enzymology | Arylsulfatases - metabolism | Rhodococcus - isolation & purification | Actinomycetales - metabolism | Sequence Homology | Streptomyces - metabolism | Cell Membrane - enzymology | Streptomyces - isolation & purification | DNA, Bacterial - genetics | Rhodococcus - metabolism | Arylsulfatases - genetics | Streptomyces - enzymology | Rhodococcus - enzymology | Actinomycetales - isolation & purification | Cluster Analysis | Index Medicus | Life Sciences | Agricultural sciences | Agronomy
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8. Full Text Restructuring the crystalline cellulose hydrogen bond network enhances its depolymerization rate
by Chundawat, Shishir P. S and Bellesia, Giovanni and Uppugundla, Nirmal and Da Costa Sousa, Leonardo and Gao, Dahai and Cheh, Albert M and Agarwal, Umesh P and Bianchetti, Christopher M and Phillips Jr, George N and Langan, Paul and Balan, Venkatesh and Gnanakaran, S and Dale, Bruce E and Great Lakes Bioenergy Research Center (GLBRC)
Journal of the American Chemical Society, ISSN 0002-7863, 07/2011, Volume 133, Issue 29, pp. 11163 - 11174
Conversion of lignocellulose to biofuels is partly inefficient due to the deleterious impact of cellulose crystallinity on enzymatic saccharification. We... 
LIGNOCELLULOSIC BIOMASS | MOLECULAR-DYNAMICS | CARBOHYDRATE-BINDING MODULE | NEUTRON FIBER DIFFRACTION | ENZYMATIC-HYDROLYSIS | LIQUID WATER | RECALCITRANT POLYSACCHARIDES | CHEMISTRY, MULTIDISCIPLINARY | I-BETA | SYNCHROTRON X-RAY | MICROCRYSTALLINE CELLULOSE | Cellulase - chemistry | Gossypium - metabolism | Crystallography, X-Ray | Trichoderma - enzymology | Molecular Dynamics Simulation | Actinomycetales - enzymology | Hydrolysis | Actinomycetales - chemistry | Cellulose - chemistry | Cellulase - metabolism | Hydrogen Bonding | Gossypium - chemistry | Protein Binding | Kinetics | Trichoderma - chemistry | Cellulose - metabolism | Usage | Analysis | Cellulose | Crystals | Molecular dynamics | Enzyme binding | Chemical properties | Structure | Hydrogen bonding | Index Medicus
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9. Full Text Intrinsic bioremediability of an aromatic hydrocarbon-polluted groundwater: diversity of bacterial population and toluene monoxygenase genes
by Cavalca, L and Dell’Amico, E and Andreoni, V
Applied Microbiology and Biotechnology, ISSN 0175-7598, 5/2004, Volume 64, Issue 4, pp. 576 - 587
The functional and phylogenetic biodiversity of bacterial communities in a benzene, toluene, ethylbenzene and xylene (BTEX)-polluted groundwater was analysed.... 
LifeSciences | PATHWAYS | BIODEGRADATION | CATABOLISM | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | PSEUDOMONAS-PUTIDA | CONTAMINATED AQUIFER | PLASMID | P-CRESOL | DEGRADATION | MONOOXYGENASE | DEGRADING BACTERIA | Benzene - metabolism | Xylenes - metabolism | DNA Fingerprinting | Actinomycetales - classification | Molecular Sequence Data | DNA, Bacterial - chemistry | Phylogeny | Biodiversity | DNA, Ribosomal - chemistry | Azoarcus - isolation & purification | Mycobacterium - isolation & purification | Oxygenases - analysis | Pseudomonas - enzymology | Actinomycetales - genetics | Bacteria - classification | Mycobacterium - classification | DNA, Bacterial - analysis | Mycobacterium - enzymology | Catechol 2,3-Dioxygenase | Pseudomonas - genetics | Actinomycetales - isolation & purification | Catechols - metabolism | Pseudomonas - classification | Biodegradation, Environmental | DNA, Bacterial - isolation & purification | Benzene Derivatives - metabolism | DNA, Ribosomal - isolation & purification | Toluene - metabolism | Azoarcus - genetics | Bradyrhizobium - classification | Gene Transfer, Horizontal | Dioxygenases | Bacteria - genetics | Actinomycetales - enzymology | Azoarcus - enzymology | Bradyrhizobium - isolation & purification | Mycobacterium - genetics | Bradyrhizobium - enzymology | Pseudomonas - isolation & purification | Bradyrhizobium - genetics | Catechol 1,2-Dioxygenase | Water Pollutants, Chemical - metabolism | Bacteria - isolation & purification | Hydrocarbons, Aromatic - metabolism | Bacteria - enzymology | Oxygenases - genetics | Water Microbiology | Azoarcus - classification | Studies | Biological diversity | Index Medicus
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10. Full Text Comparison of Family 9 Cellulases from Mesophilic and Thermophilic Bacteria
by Florence Mingardon and John D. Bagert and Cyprien Maisonnier and Devin L. Trudeau and Frances H. Arnold
Applied and Environmental Microbiology, ISSN 0099-2240, 02/2011, Volume 77, Issue 4, pp. 1436 - 1442
Classifications Services AEM Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit... 
ENDOGLUCANASE | THERMOCELLUM | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | ENZYMES | CHIMERAS | HYDROLYSIS | MICROBIOLOGY | FUNGAL CELLULASES | BINDING | THERMOMONOSPORA-FUSCA | CLOSTRIDIUM-CELLULOLYTICUM | CRYSTALLINE CELLULOSE | Cellulase - chemistry | Cellulase - genetics | Bacterial Proteins - chemistry | Bacterial Proteins - genetics | Clostridium cellulolyticum - enzymology | Hot Temperature | Recombinant Fusion Proteins - chemistry | Recombinant Fusion Proteins - metabolism | Actinomycetales - enzymology | Cellulase - metabolism | Glycoside Hydrolases - chemistry | Bacterial Proteins - metabolism | Glycoside Hydrolases - metabolism | Clostridium thermocellum - enzymology | Cellulose - metabolism | Microbial enzymes | Research | Structure | Comparative analysis | Bacteria, Thermophilic | Enzymes | Temperature | Microbiology | Crystals | Gram-positive bacteria | Catalysis | Cells | Index Medicus | Cellulase | Enzymology and Protein Engineering
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11. Full Text Deamination of 6-aminodeoxyfutalosine in menaquinone biosynthesis by distantly related enzymes
by Goble, Alissa M and Toro, Rafael and Li, Xu and Ornelas, Argentina and Fan, Hao and Eswaramoorthy, Subramaniam and Patskovsky, Yury and Hillerich, Brandan and Seidel, Ron and Sali, Andrej and Shoichet, Brian K and Almo, Steven C and Swaminathan, Subramanyam and Tanner, Martin E and Raushel, Frank M and Brookhaven National Laboratory (BNL)
Biochemistry, ISSN 0006-2960, 09/2013, Volume 52, Issue 37, pp. 6525 - 6536
Proteins of unknown function belonging to cog1816 and cog0402 were characterized. Sav2595 from Steptomyces avermitilis MA-4680, Ace10264 from Acidothermus... 
REFINEMENT | ACTIVATION | ADENOSINE-DEAMINASE | CONFORMATIONAL-CHANGE | UNKNOWN FUNCTION | STREPTOMYCES-COELICOLOR A3 | DOCKING | BIOCHEMISTRY & MOLECULAR BIOLOGY | INHIBITORS | MULTIPLE SEQUENCE ALIGNMENT | PREDICTION | Catalytic Domain | Epsilonproteobacteria - genetics | Streptomyces - genetics | Models, Molecular | Substrate Specificity | Crystallography, X-Ray | Vitamin K 2 - metabolism | Actinomycetales - enzymology | Nucleoside Deaminases - metabolism | Nucleoside Deaminases - genetics | Deamination | Epsilonproteobacteria - enzymology | Streptomyces - enzymology | Deinococcus - enzymology | Molecular Docking Simulation | Kinetics | Purine Nucleosides - metabolism | Measurement | Analysis | Crystals | Research | Enzyme kinetics | Structure | Activation energy | Vitamin K | Index Medicus
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12. Full Text Snapshots of Enzymatic Baeyer-Villiger Catalysis OXYGEN ACTIVATION AND INTERMEDIATE STABILIZATION
by Orru, Roberto and Dudek, Hanna M and Martinoli, Christian and Pazmino, Daniel E. Torres and Royant, Antoine and Weik, Martin and Fraaije, Marco W and Mattevi, Anea
The Journal of Biological Chemistry, ISSN 0021-9258, 08/2011, Volume 286, Issue 33, pp. 29284 - 29291
Baeyer-Villiger monooxygenases catalyze the oxidation of carbonylic substrates to ester or lactone products using NADPH as electron donor and molecular oxygen... 
THERMOBIFIDA-FUSCA | BIOCATALYSTS | SPECIFICITY | MECHANISM | BIOCHEMISTRY & MOLECULAR BIOLOGY | OXIDATIONS | CRYSTALS | CRYSTALLOGRAPHY | CYCLOHEXANONE MONOOXYGENASE | FLAVIN-CONTAINING MONOOXYGENASE | PHENYLACETONE-MONOOXYGENASE | Acetone - chemistry | Acetone - analogs & derivatives | Models, Chemical | Bacterial Proteins - chemistry | Oxygen - chemistry | Mixed Function Oxygenases - chemistry | Catalysis | NADP - chemistry | Actinomycetales - enzymology | Index Medicus | Enzyme Mechanisms | Enzyme Structure | Baeyer-Villiger | Flavin | Biocatalysis | Oxidation-Reduction | Enzyme Catalysis | Enzymology | Monooxygenase
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13. Full Text Temperature adaptations in psychrophilic, mesophilic and thermophilic chloride-dependent alpha-amylases
by Cipolla, Alexandre and Delbrassine, François and Da Lage, Jean-Luc and Feller, Georges
Biochimie, ISSN 0300-9084, 09/2012, Volume 94, Issue 9, pp. 1943 - 1950
The functional and structural adaptations to temperature have been addressed in homologous chloride-dependent α-amylases from a psychrophilic Antarctic... 
Alpha-amylase | Differential scanning calorimetry | Protein stability | Antarctic | Extremophiles | COLD ADAPTATION | EVOLUTIONARY RELATIONSHIPS | ACTIVATION | BACTERIA | STABILITY | BIOCHEMISTRY & MOLECULAR BIOLOGY | CONFORMATIONAL FLEXIBILITY | STEPWISE ADAPTATIONS | SIMILARITIES | ENZYMES | PROTEINS | Adaptation, Physiological | Temperature | Drosophila melanogaster - physiology | Protein Unfolding - drug effects | Guanidine - pharmacology | Enzyme Stability | alpha-Amylases - metabolism | Actinomycetales - physiology | Actinomycetales - enzymology | Thermodynamics | Animals | alpha-Amylases - chemistry | Chlorides - metabolism | Drosophila melanogaster - enzymology | Protein Conformation | Enzyme Activation | Pseudoalteromonas - physiology | Pseudoalteromonas - enzymology | Fluorescence | Physiological aspects | Enzymes | Index Medicus
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14. Full Text Manipulation of prenylation reactions by structure-based engineering of bacterial indolactam prenyltransferases
by Mori, Takahiro and Zhang, Lihan and Awakawa, Takayoshi and Hoshino, Shotaro and Okada, Masahiro and Morita, Hiroyuki and Abe, Ikuro
Nature Communications, ISSN 2041-1723, 03/2016, Volume 7, Issue 1, pp. 10849 - 10849
Prenylation reactions play crucial roles in controlling the activities of biomolecules. Bacterial prenyltransferases, TleC from Streptomyces blastmyceticus and... 
TRYPTOPHAN | INDOLE PRENYLTRANSFERASES | PROTEIN | GENE-CLUSTER | AROMATIC PRENYLTRANSFERASE | STRUCTURE REFINEMENT | MULTIDISCIPLINARY SCIENCES | BIOSYNTHETIC-PATHWAY | PHENIX | CATALYTIC MECHANISM | IDENTIFICATION | Prenylation | Streptomyces - genetics | Streptomyces - chemistry | Bacterial Proteins - chemistry | Bacterial Proteins - genetics | Substrate Specificity | Lactams - metabolism | Actinomycetales - enzymology | Actinomycetales - metabolism | Actinomycetales - chemistry | Indoles - metabolism | Dimethylallyltranstransferase - genetics | Protein Engineering | Dimethylallyltranstransferase - metabolism | Bacterial Proteins - metabolism | Streptomyces - enzymology | Molecular Structure | Indoles - chemistry | Dimethylallyltranstransferase - chemistry | Lactams - chemistry | Index Medicus
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