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microbiology (43) 43
index medicus (36) 36
biosynthesis (33) 33
antibiotics (28) 28
chemistry (26) 26
streptomyces (26) 26
streptomyces - genetics (26) 26
metallurgy (22) 22
biotechnology & applied microbiology (20) 20
biochemistry (18) 18
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enzymology (17) 17
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beer (15) 15
mutation or genetic engineering (15) 15
spirits (15) 15
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biochemistry & molecular biology (14) 14
gene expression regulation, bacterial (13) 13
cluster (12) 12
expression (12) 12
molecular sequence data (12) 12
bacterial proteins - genetics (11) 11
genetic aspects (11) 11
human necessities (11) 11
hygiene (11) 11
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gene (10) 10
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nucleosides (10) 10
organic chemistry (10) 10
regulation (10) 10
aminoglycosides - biosynthesis (9) 9
fermentation or enzyme-using processes to synthesise a desiredchemical compound or composition or to separate optical isomersfrom a racemic mixture (9) 9
gene deletion (9) 9
moenomycin (9) 9
multigene family (9) 9
research (9) 9
analysis (8) 8
bacterial proteins - metabolism (8) 8
compositions thereof (8) 8
culture media (8) 8
derivatives thereof (8) 8
escherichia-coli (8) 8
metabolism (8) 8
microorganisms or enzymes (8) 8
nucleic acids (8) 8
nucleotides (8) 8
propagating, preserving or maintaining microorganisms (8) 8
sugars (8) 8
antibiotika (7) 7
applied microbiology (7) 7
coelicolor a3 (7) 7
dna, bacterial - genetics (7) 7
generation (7) 7
genomes (7) 7
genomics (7) 7
metabolites (7) 7
molecular structure (7) 7
oligosaccharides - biosynthesis (7) 7
polyketides (7) 7
resistance (7) 7
anti-bacterial agents - pharmacology (6) 6
bambermycins - biosynthesis (6) 6
biosynthese (6) 6
compositions or test papers therefor (6) 6
condition-responsive control in microbiological orenzymological processes (6) 6
environmental engineering/biotechnology (6) 6
enzymes (6) 6
gen (6) 6
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genes, bacterial (6) 6
glycosylation (6) 6
gram-positive bacteria (6) 6
measuring or testing processes involving enzymes, nucleicacids or microorganisms (6) 6
microbial genetics and genomics (6) 6
natural products (6) 6
processes of preparing such compositions (6) 6
protein (6) 6
proteins (6) 6
streptomyces - enzymology (6) 6
streptomyces ghanaensis (6) 6
transcription (6) 6
actinomycetes (5) 5
base sequence (5) 5
biochemistry, general (5) 5
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61. Full Text A Streamlined Metabolic Pathway for the Biosynthesis of Moenomycin A
by Ostash, Bohdan and Saghatelian, Alan and Walker, Suzanne
Chemistry & Biology, ISSN 1074-5521, 2007, Volume 14, Issue 3, pp. 257 - 267
Moenomycin A (MmA) is a member of the phosphoglycolipid family of antibiotics, which are the only natural products known to directly target the extracellular... 
CHEMBIOL | MICROBIO | LIPID PART | ANTIBIOTICS | PEPTIDOGLYCAN BIOSYNTHESIS | GENOME SEQUENCE | STREPTOMYCES-COELICOLOR A3 | GENE-CLUSTER | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | PHOSPHATE SYNTHASE | GLYCOSYLTRANSFERASES | Carbohydrate Sequence | DNA, Bacterial - isolation & purification | Streptomyces - genetics | Models, Molecular | Molecular Sequence Data | Bacillus cereus - enzymology | Bambermycins - biosynthesis | Bambermycins - chemistry | Glycosyltransferases - metabolism | Bacillus cereus - genetics | DNA, Bacterial - genetics | Mutagenesis | Bacterial Proteins - metabolism | Streptomyces - enzymology | Transcription, Genetic | Kinetics | Microbiology | Physiological aspects | Chemical properties
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62. Full Text Expression of the regulatory protein LndI for landomycin E production in Streptomyces globisporus 1912 is controlled by the availability of tRNA for the rare UUA codon
by Rebets, Yuriy V and Ostash, Bohdan O and Fukuhara, Masahiro and Nakamura, Tatsunosuke and Fedorenko, Victor O
FEMS Microbiology Letters, ISSN 0378-1097, 03/2006, Volume 256, Issue 1, pp. 30 - 37
Abstract The gene lndI encodes the activator of landomycin biosynthesis. The utilization of LndI-EGFP fusions led us to investigate the temporal pattern of... 
Streptomyces | regulation | polyketides | antibiotics | SECONDARY METABOLISM | MICROBIOLOGY | GREEN FLUORESCENT PROTEIN | MUTANTS | GENE | CEPHAMYCIN-C | BLDA | COELICOLOR A3 | GENERATION | CLUSTER | Fluorescent Dyes - chemistry | Blotting, Western - methods | Streptomyces - physiology | Aminoglycosides - physiology | Streptomyces - genetics | Aminoglycosides - genetics | Aminoglycosides - chemistry | Mutagenesis, Site-Directed - methods | Green Fluorescent Proteins - genetics | Codon - analysis | Mutation - physiology | Gene Expression Regulation, Bacterial - genetics | RNA, Transfer - physiology | Time Factors | Aminoglycosides - biosynthesis | Transcription, Genetic - genetics | Green Fluorescent Proteins - chemistry | Gene Order | Proteins | Translation | tRNA | Transcription | Streptomyces coelicolor | Biosynthesis | Gene expression | Delay
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63. Identification and characterization of the Streptomyces globisporus 1912 regulatory gene lndYR that affects sporulation and antibiotic production
by Ostash, Bohdan and Rebets, Yuriy and Myronovskyy, Maksym and Tsypik, Olga and Ostash, Iryna and Kulachkovskyy, Oleksandr and Datsyuk, Yuriy and Nakamura, Tatsunosuke and Walker, Suzanne and Fedorenko, Victor
Microbiology, ISSN 1350-0872, 01/2011, Volume 157, pp. 1240 - 1249
Here, we report the identification and functional characterization of the Streptomyces globisporus 1912 gene lndYR, which encodes a GntR-like regulator of the... 
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64. Full Text Cultivable actinomycetes from rhizosphere of birch (Betula pendula) growing on a coal mine dump in Silets, Ukraine
by Ostash, Bohdan and Gren, Tetiana and Hrubskyy, Yaroslav and Tistechok, Stepan and Beshley, Stepan and Baranov, Volodymyr and Fedorenko, Victor
Journal of Basic Microbiology, ISSN 0233-111X, 08/2014, Volume 54, Issue 8, pp. 851 - 857
Five actinomycete strains were isolated from the rhizosphere of birch, one of a few native tree forms capable of thriving on the upper level of a coal mine... 
Rhizosphere | 16S rRNA | Mine tailings | Actinomycetes | ENVIRONMENTS | GROWTH-PROMOTING BACTERIA | MICROBIOLOGY | STREPTOMYCES | SEQUENCE | SOIL | PLANTS | METAL | TAILINGS | PHYTOSTABILIZATION | ACTINOBACTERIA | Metals, Heavy - metabolism | Streptomyces - genetics | Soil Microbiology | Betula - microbiology | Ukraine | Phylogeny | Sequence Analysis, DNA | Siderophores - biosynthesis | Streptomyces - isolation & purification | Streptomyces - classification | Base Sequence | Cell Wall - metabolism | RNA, Ribosomal, 16S - genetics | Anti-Bacterial Agents - biosynthesis | Coal Mining | Mycological Typing Techniques | DNA, Ribosomal - genetics
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65. Full Text Novel teichulosonic acid from cell wall of Streptomyces coelicolor M145
by Shashkov, Alexander S and Ostash, Bohdan E and Fedorenko, Victor A and Streshinskaya, Galina M and Tul’skaya, Elena M and Senchenkova, Sof’ya N and Baryshnikova, Lidiya M and Evtushenko, Ludmila I
Carbohydrate Research, ISSN 0008-6215, 10/2012, Volume 359, pp. 70 - 75
The cell wall of M145, a prototrophic plasmidless (SCP1 SCP2 ) variant of strain A3(2) contains the main glycopolymer represented by Kdn-containing... 
Streptomyces | NMR spectroscopy | Teichulosonic acid | Cell wall | Glycosyl 1-phosphate polymer | TEICHOIC-ACID | POLYMERS | KDN | BIOCHEMISTRY & MOLECULAR BIOLOGY | CHEMISTRY, ORGANIC | CHEMISTRY, APPLIED | Carbohydrate Sequence | Uronic Acids - isolation & purification | Magnetic Resonance Spectroscopy | Molecular Sequence Data | Streptomyces coelicolor - chemistry | Cell Wall - chemistry | Uronic Acids - chemistry | Nuclear magnetic resonance spectroscopy
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66. Full Text Identification and characterization of Streptomyces ghanaensis ATCC14672 integration sites for three actinophage-based plasmids
by Ostash, Bohdan and Makitrinskyy, Roman and Walker, Suzanne and Fedorenko, Victor
Plasmid, ISSN 0147-619X, 2009, Volume 61, Issue 3, pp. 171 - 175
produces the antibiotic moenomycin A, which is the only known direct inhibitor of bacterial peptidoglycan glycosyltransferases (transglycosylases). Recent... 
Moenomycin | Integrative and conjugative elements | Streptomyces ghanaensis | Actinophage | SYSTEM | GENE | BIOSYNTHESIS | GENETICS & HEREDITY | MOENOMYCIN-A | Genetic Engineering - methods | Gene Transfer Techniques | Streptomyces - genetics | Molecular Sequence Data | Sequence Analysis, DNA | Genetic Vectors - genetics | RNA, Transfer, Arg - genetics | Bambermycins - chemistry | Bambermycins - metabolism | Escherichia coli - genetics | Base Sequence | Molecular Structure | Gene Components | Physiological aspects | Chemical properties | Molecular genetics | Transferases | Antineoplastic antibiotics | actinophage | integrative and conjugative elements | moenomycin
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67. Full Text Expression of the regulatory protein LndI for landomycin E production in Streptomyces globisporus1912 is controlled by the availability of tRNA for the rare UUA codon
by Rebets, Yuriy V and Ostash, Bohdan O and Fukuhara, Masahiro and Nakamura, Tatsunosuke and Fedorenko, Victor O
FEMS Microbiology Letters, ISSN 0378-1097, 03/2006, Volume 256, Issue 1, pp. 30 - 37
Streptomyces | Polyketides | Regulation | Antibiotics
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68. Full Text Coordination of export and glycosylation of landomycins inStreptomyces cyanogenusS136
by Ostash, Iryna and Ostash, Bohdan and Luzhetskyy, Andriy and Bechthold, Andreas and Walker, Suzanne and Fedorenko, Victor
FEMS Microbiology Letters, ISSN 0378-1097, 08/2008, Volume 285, Issue 2, pp. 195 - 202
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69. Full Text On the acceptor substrate of C-glycosyl-transferase UrdGT2: Three prejadomycin C-glycosides from an engineered mutant of Streptomyces globisporus 1912 ΔlndE(urdGT2)
by Baig, Irfan and Kharel, Madan and Kobylyanskyy, Anton and Zhu, Lili and Rebets, Yuriy and Ostash, Bohdan and Luzhetskyy, Andriy and Bechthold, Andreas and Fedorenko, Victor A and Rohr, Jürgen
Angewandte Chemie - International Edition, ISSN 1433-7851, 11/2006, Volume 45, Issue 46, pp. 7842 - 7846
Combinatorial biosynthesis | Glycosides | Polyketides | Biosynthesis | Landomycins | ANGUCYCLINE ANTIBIOTICS | GENE-CLUSTER | SPECIFICITY | LANDOMYCIN-A | CYANOGENUS S136 | URDAMYCIN-A | JADOMYCIN BIOSYNTHESIS | GENERATION | FRADIAE | GLYCOSYLTRANSFERASES | CHEMISTRY, MULTIDISCIPLINARY
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70. Full Text Minimum Information about a Biosynthetic Gene cluster: commentary
by Medema, Marnix H and Kottmann, Renzo and Yilmaz, Pelin and Cummings, Matthew and Biggins, John B and Blin, Kai and de Bruijn, Irene and Chooi, Yit Heng and Claesen, Jan and Coates, R Cameron and Cruz-Morales, Pablo and Duddela, Srikanth and Dusterhus, Stephanie and Edwards, Daniel J and Fewer, David P and Garg, Neha and Geiger, Christoph and Gomez-Escribano, Juan Pablo and Greule, Anja and Hadjithomas, Michalis and Haines, Anthony S and Helfrich, Eric J N and Hillwig, Matthew L and Ishida, Keishi and Jones, Adam C and Jones, Carla S and Jungmann, Katrin and Kegler, Carsten and Kim, Hyun Uk and Kotter, Peter and Krug, Daniel and Masschelein, Joleen and Melnik, Alexey V and Mantovani, Simone M and Monroe, Emily A and Moore, Marcus and Moss, Nathan and Nutzmann, Hans-Wilhelm and Pan, Guohui and Pati, Amrita and Petras, Daniel and Reen, F Jerry and Rosconi, Federico and Rui, Zhe and Tian, Zhenhua and Tobias, Nicholas J and Tsunematsu, Yuta and Wiemann, Philipp and Wyckoff, Elizabeth and Yan, Xiaohui and Yim, Grace and Yu, Fengan and Xie, Yunchang and Aigle, Bertrand and Apel, Alexander K and Balibar, Carl J and Balskus, Emily P and Barona-Gomez, Francisco and Bechthold, Aneas and Bode, Helge B and Borriss, Rainer and Brady, Sean F and Brakhage, Axel A and Caffrey, Patrick and Cheng, Yi-Qiang and Clardy, Jon and Cox, Russell J and De Mot, Rene and Donadio, Stefano and Donia, Mohamed S and van der Donk, Wilfred A and Dorrestein, Pieter C and Doyle, Sean and essen, Arnold J M and Ehling-Schulz, Monika and Entian, Karl-Dieter and Fischbach, Michael A and Gerwick, Lena and Gerwick, William H and Gross, Harald and Gust, Bertolt and Hertweck, Christian and Hofte, Monica and Jensen, Susan E and Ju, Jianhua and Katz, Leonard and Kaysser, Leonard and Klassen, Jonathan L and Keller, Nancy P and Kormanec, Jan and Kuipers, Oscar P and Kuzuyama, Tomohisa and Kyrpides, Nikos C and Kwon, Hyung-Jin and Lautru, Sylvie and Lavigne, Rob and Lee, Chia Y and Linquan, Bai and Liu, Xinyu and Liu, Wen and ...
Nature Chemical Biology, ISSN 1552-4450, 09/2015, Volume 11, Issue 9, pp. 625 - 631
A wide variety of enzymatic pathways that produce specialized metabolites in bacteria, fungi and plants are known to be encoded in biosynthetic gene clusters.... 
international
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71. Full Text A putative proteinase gene is involved in regulation of landomycin E biosynthesis in Streptomyces globisporus 1912
by Dutko, Lilia and Rebets, Yuriy and Ostash, Bohdan and Luzhetskyy, Andriy and Bechthold, Andreas and Nakamura, Tatsunosuke and Fedorenko, Victor
FEMS Microbiology Letters, ISSN 0378-1097, 02/2006, Volume 255, Issue 2, pp. 280 - 285
abstract The prx gene, which is highly homologous to putative proteinases, has been identified by sequencing in the vicinity of the biosynthetic gene cluster... 
Streptomyces | regulation | proteinase | polyketides | post‐translational modification | Post-translational modification | Polyketides | Regulation | Proteinase | CONJUGAL TRANSFER | ESCHERICHIA-COLI | MICROBIOLOGY | post-translational modification | COMPLETE GENOME SEQUENCE | CLONING | DNA | COELICOLOR A3 | GENERATION | CLUSTER | Streptomyces - metabolism | Multigene Family | Streptomyces - genetics | Peptide Hydrolases - genetics | Gene Deletion | Bacterial Proteins - genetics | Aminoglycosides - biosynthesis | Bacterial Proteins - metabolism | Protein Processing, Post-Translational | Gene Expression Regulation, Bacterial | Peptide Hydrolases - metabolism | Genetic research | Physiological aspects | Homology | Protein kinase C | Biosynthesis | Gene expression | Gene sequencing
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72. Full Text Minimum Information about a Biosynthetic Gene cluster
by Medema, M.H and Kottmann, Renzo and Yilmaz, Pelin and Cummings, Matthew and Biggins, J.B and Blin, Kai and Bruijn, De, Irene and Chooi, Yit Heng and Claesen, Jan and Coates, R.C and Cruz-Morales, Pablo and Duddela, Srikanth and Düsterhus, Stephanie and Edwards, Daniel J and Fewer, David P and Garg, Neha and Geiger, Christoph and Gomez-Escribano, Juan Pablo and Greule, Anja and Hadjithomas, Michalis and Haines, Anthony S and Helfrich, Eric J.N and Hillwig, Matthew L and Ishida, Keishi and Jones, Adam C and Jones, Carla S and Jungmann, Katrin and Kegler, Carsten and Kim, Hyun Uk and Kötter, Peter and Krug, Daniel and Masschelein, Joleen and Melnik, Alexey V and Mantovani, Simone M and Monroe, Emily A and Moore, Marcus and Moss, Nathan and Nützmann, Hans Wilhelm and Pan, Guohui and Pati, Amrita and Petras, Daniel and Reen, F.J and Rosconi, Federico and Rui, Zhe and Tian, Zhenhua and Tobias, Nicholas J and Tsunematsu, Yuta and Wiemann, Philipp and Wyckoff, Elizabeth and Yan, Xiaohui and Yim, Grace and Yu, Fengan and Xie, Yunchang and Aigle, Bertrand and Apel, Alexander K and Balibar, Carl J and Balskus, Emily P and Barona-Gómez, Francisco and Bechthold, Aneas and Bode, Helge B and Borriss, Rainer and Brady, Sean F and Brakhage, Axel A and Caffrey, Patrick and Cheng, Yi Qiang and Clardy, Jon and Cox, Russell J and Mot, De, René and Donadio, Stefano and Donia, Mohamed S and Donk, Van Der, Wilfred A and Dorrestein, Pieter C and Doyle, Sean and essen, Arnold J.M and Ehling-Schulz, Monika and Entian, Karl Dieter and Fischbach, Michael A and Gerwick, Lena and Gerwick, William H and Gross, Harald and Gust, Bertolt and Hertweck, Christian and Höfte, Monica and Jensen, Susan E and Ju, Jianhua and Katz, Leonard and Kaysser, Leonard and Klassen, Jonathan L and Keller, Nancy P and Kormanec, Jan and Kuipers, Oscar P and Kuzuyama, Tomohisa and Kyrpides, Nikos C and Kwon, Hyung Jin and Lautru, Sylvie and Lavigne, Rob and Lee, Chia Y and Linquan, Bai and Liu, Xinyu and Liu, Wen and ...
Nature Chemical Biology, ISSN 1552-4450, 2015, Volume 11, Issue 9, pp. 625 - 631
A wide variety of enzymatic pathways that produce specialized metabolites in bacteria, fungi and plants are known to be encoded in biosynthetic gene clusters.... 
Laboratory of Phytopathology | EPS | Laboratorium voor Phytopathologie | Bioinformatica | Laboratorium voor Fytopathologie | Bioinformatics
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73. Full Text Identification of the function of gene lndM2 encoding a bifunctional oxygenase-reductase involved in the biosynthesis of the antitumor antibiotic landomycin E by Streptomyces globisporus 1912 supports the originally assigned structure for landomycinone
by Zhu, Lili and Ostash, Bohdan and Rix, Uwe and Nur-E-Alam, Mohammad and Mayers, Almuth and Luzhetskyy, Andriy and Mendez, Carmen and Salas, Jose A and Bechthold, Andreas and Fedorenko, Victor and Rohr, Jürgen
Journal of Organic Chemistry, ISSN 0022-3263, 01/2005, Volume 70, Issue 2, pp. 631 - 638
The angucycline antibiotic family of the landomycins displays potent antitumor activity. To elucidate early post polyketide synthase (PKS) tailoring steps of... 
FRADIAE TU2717 | ANGUCYCLINE ANTIBIOTICS | TETRANGOMYCIN | CLONING | CYANOGENUS S136 | URDAMYCIN-A | CHEMISTRY, ORGANIC | GLYCOSYLTRANSFERASE | HETEROLOGOUS EXPRESSION | CLUSTER | POLYKETIDE SYNTHASE GENE | Multigene Family | Genes, Bacterial - genetics | Streptomyces - genetics | Oxidoreductases - genetics | Antibiotics, Antineoplastic - biosynthesis | Aminoglycosides - chemistry | Gene Expression Regulation, Bacterial - genetics | DNA, Bacterial - genetics | Antibiotics, Antineoplastic - chemistry | Gene Expression Regulation, Enzymologic - genetics | Oligosaccharides - chemistry | Aminoglycosides - biosynthesis | Naphthoquinones - chemistry | Streptomyces - enzymology | Molecular Structure | Mutation | Research | Nucleotide sequence | Antibiotics | Gene expression
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74. Full Text Generation of Novel Landomycins M and O through Targeted Gene Disruption
by Luzhetskyy, Andriy and Zhu, Lili and Gibson, Miranda and Fedoryshyn, Marta and Dürr, Clemens and Hofmann, Carsten and Hoffmeister, Dirk and Ostash, Bohdan and Mattingly, Cynthia and Adams, Val and Fedorenko, Victor and Rohr, Jürgen and Bechthold, Andreas
ChemBioChem, ISSN 1439-4227, 04/2005, Volume 6, Issue 4, pp. 675 - 678
Two genes from Streptomyces cyanogenous S136 that encode the reductase LanZ4 and the hydroxylase LanZ5, which are involved in landomycin A biosynthesis, were... 
glycosylation | landomycin | hydroxylation | biosynthesis | antitumor agents | Biosynthesis | Glycosylation | Antitumor agents | Hydroxylation | Landomycin | ANTIBIOTICS | CHEMISTRY, MEDICINAL | BIOCHEMISTRY & MOLECULAR BIOLOGY | CLUSTER | EXPRESSION | Gene Targeting | Antibiotics, Antineoplastic - pharmacology | Magnetic Resonance Spectroscopy | Streptomyces - genetics | Humans | Antibiotics, Antineoplastic - biosynthesis | Naphthoquinones - pharmacology | Oligosaccharides - biosynthesis | Oligosaccharides - pharmacology | Streptomyces - metabolism | Disaccharides - pharmacology | Disaccharides - biosynthesis | Oligosaccharides - chemistry | Aminoglycosides - biosynthesis | Cell Line, Tumor | Inhibitory Concentration 50 | Naphthoquinones - chemistry | Cell Proliferation - drug effects | Molecular Structure | Oxygenases - genetics | Aminoglycosides - pharmacology
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75. Full Text Generation of Streptomyces globisporus SMY622 Strain with Increased Landomycin E Production and It's Initial Characterization
by GROMYKO, OLEKSANDR and REBETS, YURIY and OSTASH, BOHDAN and LUZHETSKYY, ANDRIY and FUKUHARA, MASAHIRO and BECHTHOLD, ANDREAS and NAKAMURA, TATSUNOSUKE and FEDORENKO, VICTOR
The Journal of Antibiotics, ISSN 0021-8820, 2004, Volume 57, Issue 6, pp. 383 - 389
Landomycin E (LaE) overproducing strain Streptomyces globisporus SMY6222 has been developed using UV induced mutagenesis and selection for streptomycin... 
PROTEIN | GENE | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | CYANOGENUS S136 | BIOSYNTHESIS | RESISTANCE | COELICOLOR A3 | MICROBIOLOGY | PHARMACOLOGY & PHARMACY | MUTATIONS | IMMUNOLOGY | CLUSTER | Ribosomal Proteins - chemistry | Streptomyces - genetics | Aminoglycosides - genetics | Ribosomal Proteins - genetics | Selection, Genetic | DNA, Bacterial - chemistry | Streptomyces - metabolism | Point Mutation | Transcription, Genetic - physiology | DNA, Bacterial - genetics | Mutagenesis | Cloning, Molecular | Polymerase Chain Reaction | Aminoglycosides - biosynthesis | Oxygenases - genetics
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76. Full Text Expression of the regulatory protein LndI for landomycin E production inStreptomyces globisporus1912 is controlled by the availability of tRNA for the rare UUA codon
by Rebets, Yuriy V and Ostash, Bohdan O and Fukuhara, Masahiro and Nakamura, Tatsunosuke and Fedorenko, Victor O
FEMS Microbiology Letters, ISSN 0378-1097, 03/2006, Volume 256, Issue 1, pp. 30 - 37
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77. Full Text Function of lanGT3, a Glycosyltransferase Gene Involved in Landomycin A Biosynthesis
by Luzhetskyy, Andriy and Liu, Tao and Fedoryshyn, Marta and Ostash, Bohdan and Fedorenko, Viktor and Rohr, Jürgen and Bechthold, Andreas
ChemBioChem, ISSN 1439-4227, 11/2004, Volume 5, Issue 11, pp. 1567 - 1570
The glycosyltransferase gene lanGT3, involved in the biosynthesis of the angucyclic antibiotic landomycin A, has been characterised by targeted gene deletion.... 
glycosyltransferases | glycosylation | olivose | landomycin | biosynthesis | Olivose | Biosynthesis | Glycosylation | Landomycin | Glycosyltransferases | ANTIBIOTICS | CHEMISTRY, MEDICINAL | BIOCHEMISTRY & MOLECULAR BIOLOGY | GENERATION | CLUSTER | STEPS | Carbohydrate Sequence | Glycosyltransferases - metabolism | Escherichia coli - enzymology | Escherichia coli - metabolism | Aminoglycosides - biosynthesis | Molecular Sequence Data | Anti-Bacterial Agents - biosynthesis | Glycosyltransferases - genetics | Mutation | Gene Expression Regulation, Bacterial
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78. Full Text A putative proteinase gene is involved in regulation of landomycin E biosynthesis inStreptomyces globisporus1912
by Dutko, Lilia and Rebets, Yuriy and Ostash, Bohdan and Luzhetskyy, Andriy and Bechthold, Andreas and Nakamura, Tatsunosuke and Fedorenko, Victor
FEMS Microbiology Letters, ISSN 0378-1097, 02/2006, Volume 255, Issue 2, pp. 280 - 285
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79. Full Text On the Acceptor Substrate of C‐Glycosyltransferase UrdGT2: Three Prejadomycin C‐Glycosides from an Engineered Mutant of Streptomyces globisporus 1912 ΔlndE(urdGT2)
by Baig, Irfan and Kharel, Madan and Kobylyanskyy, Anton and Zhu, Lili and Rebets, Yuriy and Ostash, Bohdan and Luzhetskyy, Andriy and Bechthold, Andreas and Fedorenko, Victor A and Rohr, Jürgen
Angewandte Chemie International Edition, ISSN 1433-7851, 11/2006, Volume 45, Issue 46, pp. 7842 - 7846
The transfer of the gene urdGT2, which encodes a C‐glycosyltransferase in the urdamycin pathway, into the lnd‐minus mutant of the landomycin (lnd) biosynthetic... 
combinatorial biosynthesis | landomycins | polyketides | glycosides | biosynthesis
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80. Full Text On the Acceptor Substrate of C-Glycosyltransferase UrdGT2: Three Prejadomycin C-Glycosides from an Engineered Mutant ofStreptomyces globisporus 1912 ΔlndE(urdGT2)
by Baig, Irfan and Kharel, Madan and Kobylyanskyy, Anton and Zhu, Lili and Rebets, Yuriy and Ostash, Bohdan and Luzhetskyy, Andriy and Bechthold, Andreas and Fedorenko, Victor A and Rohr, Jürgen
Angewandte Chemie International Edition, ISSN 1433-7851, 11/2006, Volume 45, Issue 46, pp. 7842 - 7846
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