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Katsumi Kakinuma - One of the best experts on this subject based on the ideXlab platform.
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Biosynthesis of 2-Deoxystreptamine-containing Antibiotics in Streptoalloteichus hindustanus JCM 3268: Characterization of 2-Deoxy-scyllo-inosose Synthase
The Journal of Antibiotics, 2006Co-Authors: Toshifumi Hirayama, Katsumi Kakinuma, Fumitaka Kudo, Hideyuki Tamegai, Kazumasa Kojima, Tadashi EguchiAbstract:A part of the new biosynthetic gene cluster for 2-Deoxystreptamine-containing antibiotics was identified from Streptoalloteichus hindustanus . The alloH gene in the gene cluster was deduced to encode 2-deoxy- scyllo -inosose synthase and the expressed protein AlloH was confirmed to have this enzyme activity. Furthermore, biochemical properties of AlloH were studied.
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Biosynthesis of 2-Deoxystreptamine by Three Crucial Enzymes in Streptomyces fradiae NBRC 12773
The Journal of Antibiotics, 2005Co-Authors: Fumitaka Kudo, Tadashi Eguchi, Kenichi Yokoyama, Yasuhito Yamamoto, Katsumi KakinumaAbstract:NeoA, B, and C encoded in the neomycin biosynthetic gene cluster have been enzymatically confirmed to be responsible to the formation of 2-Deoxystreptamine (DOS) in Streptomyces fradiae . NeoC was functionally characterized as 2-deoxy- scyllo -inosose synthase, which catalyzes the carbocycle formation from D -glucose-6-phosphate to 2-deoxy- scyllo -inosose. Further, NeoA appeared to catalyze the oxidation of 2-deoxy- scyllo -inosamine (DOIA) with NAD(P)^+ forming 3-amino-2,3-dideoxy- scyllo -inosose (amino-DOI). Consequently, NeoA was characterized as 2-deoxy- scyllo -inosamine dehydrogenase. Finally, amino-DOI produced by NeoA from DOIA was transformed into DOS by NeoB. Since NeoB (Neo6) was also reported to be L -glutamine:2-deoxy- scyllo -inosose aminotransferase, all the enzymes in the DOS biosynthesis were characterized for the first time.
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Crystallization and X-ray analysis of 2-deoxy-scyllo-inosose synthase, the key enzyme in the biosynthesis of 2-Deoxystreptamine-containing aminoglycoside antibiotics.
Acta Crystallographica Section F Structural Biology and Crystallization Communications, 2005Co-Authors: Eriko Nango, Katsumi Kakinuma, Takashi Kumasaka, Takao Sato, Nobuo Tanaka, Tadashi EguchiAbstract:The crystallization of 2-deoxy-scyllo-inosose synthase, the key enzyme in the biosynthesis of 2-Deoxystreptamine-containing aminoglycoside antibiotics, is reported. A recombinant 2-deoxy-scyllo-inosose synthase from Bacillus circulans has been crystallized at 277 K using PEG 4000 as precipitant. The diffraction pattern of the crystal extends to 2.30 A resolution at 100 K using synchrotron radiation at the Photon Factory. The crystals are monoclinic and belong to space group P2{sub 1}, with unit-cell parameters a = 80.5, b = 70.4, c = 83.0 A, β = 117.8°. The presence of two molecules per asymmetric unit gives a crystal volume per protein weight (V{sub M}) of 2.89 A{sup 3} Da{sup −1} and a solvent constant of 57.4% by volume.
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Stereochemical recognition of doubly functional aminotransferase in 2-Deoxystreptamine biosynthesis
Journal of the American Chemical Society, 2005Co-Authors: Kenichi Yokoyama, Fumitaka Kudo, Hideyuki Tamegai, Tadashi Eguchi, Mieko Kuwahara, Kousuke Inomata, Katsumi KakinumaAbstract:The doubly functional aminotransferase BtrS in the 2-Deoxystreptamine (DOS) biosynthesis, in which two transaminations are involved, was characterized by a genetic as well as a chemical approach with the heterologously expressed enzyme. The gene disruption study clearly showed that BtrS is involved, in addition to the previously confirmed first transamination, in the second transamination as well. This dual function of BtrS for the DOS biosynthesis was further confirmed by the structural determination of the reverse reaction product from DOS. Enantiospecific formation of the reverse reaction product from DOS clearly showed that BtrS distinguishes the enantiotopic amino groups of DOS, but in contrast, both enantiomers of 2-deoxy-scyllo-inosose (DOI) were efficiently accepted by BtrS to give a racemic product. This unique stereochemical recognition of DOI chirality and DOS prochirality by BtrS is mechanistically explained by a specific hydrogen-bond donating force in the enzyme active site as a particular f...
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Reaction Stereochemistry of 2-Deoxy-scyllo-inosose Synthase, the Key Enzyme in the Biosynthesis of 2-Deoxystreptamine
Chemistry Letters, 2003Co-Authors: Eriko Nango, Tadashi Eguchi, Fumitaka Kudo, Katsumi KakinumaAbstract:The reaction stereochemistry of 2-deoxy-scyllo-inosose (DOI) synthase (DOIS) derived from butirosin-producing Bacillus circulans, the key starter enzyme of 2-Deoxystreptamine biosynthesis, was closely analyzed by use of the purified recombinant DOIS. The stereochemical pathway of the DOIS reaction is common in the aminoglycoside-producing Bacillus and Streptomyces, but is distinct from a related dehydroquinate synthase reaction in the shikimate pathway. Evolutionary relationship between these enzymes is also discussed.
Tadashi Eguchi - One of the best experts on this subject based on the ideXlab platform.
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biosynthetic enzymes for the aminoglycosides butirosin and neomycin
Methods in Enzymology, 2009Co-Authors: Fumitaka Kudo, Tadashi EguchiAbstract:Butirosin and neomycin belong to a family of clinically valuable 2-Deoxystreptamine (2DOS)-containing aminoglycoside antibiotics. The biosynthetic gene clusters for butirosin and neomycin were identified in 2000 and in 2005, respectively. In recent years, most of the enzymes encoded in the gene clusters have been characterized, and thus almost all the biosynthetic steps leading to the final antibiotics have been understood. This knowledge could shed light on the complex biosynthetic pathways for other related structurally diverse aminoglycoside antibiotics. In this chapter, the enzymatic reactions in the biosynthesis of butirosin and neomycin are reviewed step by step.
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Biosynthesis of 2-Deoxystreptamine-containing Antibiotics in Streptoalloteichus hindustanus JCM 3268: Characterization of 2-Deoxy-scyllo-inosose Synthase
The Journal of Antibiotics, 2006Co-Authors: Toshifumi Hirayama, Katsumi Kakinuma, Fumitaka Kudo, Hideyuki Tamegai, Kazumasa Kojima, Tadashi EguchiAbstract:A part of the new biosynthetic gene cluster for 2-Deoxystreptamine-containing antibiotics was identified from Streptoalloteichus hindustanus . The alloH gene in the gene cluster was deduced to encode 2-deoxy- scyllo -inosose synthase and the expressed protein AlloH was confirmed to have this enzyme activity. Furthermore, biochemical properties of AlloH were studied.
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Biosynthesis of 2-Deoxystreptamine by Three Crucial Enzymes in Streptomyces fradiae NBRC 12773
The Journal of Antibiotics, 2005Co-Authors: Fumitaka Kudo, Tadashi Eguchi, Kenichi Yokoyama, Yasuhito Yamamoto, Katsumi KakinumaAbstract:NeoA, B, and C encoded in the neomycin biosynthetic gene cluster have been enzymatically confirmed to be responsible to the formation of 2-Deoxystreptamine (DOS) in Streptomyces fradiae . NeoC was functionally characterized as 2-deoxy- scyllo -inosose synthase, which catalyzes the carbocycle formation from D -glucose-6-phosphate to 2-deoxy- scyllo -inosose. Further, NeoA appeared to catalyze the oxidation of 2-deoxy- scyllo -inosamine (DOIA) with NAD(P)^+ forming 3-amino-2,3-dideoxy- scyllo -inosose (amino-DOI). Consequently, NeoA was characterized as 2-deoxy- scyllo -inosamine dehydrogenase. Finally, amino-DOI produced by NeoA from DOIA was transformed into DOS by NeoB. Since NeoB (Neo6) was also reported to be L -glutamine:2-deoxy- scyllo -inosose aminotransferase, all the enzymes in the DOS biosynthesis were characterized for the first time.
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Crystallization and X-ray analysis of 2-deoxy-scyllo-inosose synthase, the key enzyme in the biosynthesis of 2-Deoxystreptamine-containing aminoglycoside antibiotics.
Acta Crystallographica Section F Structural Biology and Crystallization Communications, 2005Co-Authors: Eriko Nango, Katsumi Kakinuma, Takashi Kumasaka, Takao Sato, Nobuo Tanaka, Tadashi EguchiAbstract:The crystallization of 2-deoxy-scyllo-inosose synthase, the key enzyme in the biosynthesis of 2-Deoxystreptamine-containing aminoglycoside antibiotics, is reported. A recombinant 2-deoxy-scyllo-inosose synthase from Bacillus circulans has been crystallized at 277 K using PEG 4000 as precipitant. The diffraction pattern of the crystal extends to 2.30 A resolution at 100 K using synchrotron radiation at the Photon Factory. The crystals are monoclinic and belong to space group P2{sub 1}, with unit-cell parameters a = 80.5, b = 70.4, c = 83.0 A, β = 117.8°. The presence of two molecules per asymmetric unit gives a crystal volume per protein weight (V{sub M}) of 2.89 A{sup 3} Da{sup −1} and a solvent constant of 57.4% by volume.
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Stereochemical recognition of doubly functional aminotransferase in 2-Deoxystreptamine biosynthesis
Journal of the American Chemical Society, 2005Co-Authors: Kenichi Yokoyama, Fumitaka Kudo, Hideyuki Tamegai, Tadashi Eguchi, Mieko Kuwahara, Kousuke Inomata, Katsumi KakinumaAbstract:The doubly functional aminotransferase BtrS in the 2-Deoxystreptamine (DOS) biosynthesis, in which two transaminations are involved, was characterized by a genetic as well as a chemical approach with the heterologously expressed enzyme. The gene disruption study clearly showed that BtrS is involved, in addition to the previously confirmed first transamination, in the second transamination as well. This dual function of BtrS for the DOS biosynthesis was further confirmed by the structural determination of the reverse reaction product from DOS. Enantiospecific formation of the reverse reaction product from DOS clearly showed that BtrS distinguishes the enantiotopic amino groups of DOS, but in contrast, both enantiomers of 2-deoxy-scyllo-inosose (DOI) were efficiently accepted by BtrS to give a racemic product. This unique stereochemical recognition of DOI chirality and DOS prochirality by BtrS is mechanistically explained by a specific hydrogen-bond donating force in the enzyme active site as a particular f...
Floris L. Van Delft - One of the best experts on this subject based on the ideXlab platform.
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2-Deoxystreptamine Conjugates by Truncation-Derivatization of Neomycin.
Pharmaceuticals (Basel Switzerland), 2010Co-Authors: M. Waqar Aslam, Floris P. J. T. Rutjes, Leandro C. Tabares, Alessio Andreoni, Gerard W. Canters, Floris L. Van DelftAbstract:A small library of truncated neomycin-conjugates is prepared by consecutive removal of 2,6-diaminoglucose rings, oxidation-reductive amination of ribose, oxidation-conjugation of aminopyridine/aminoquinoline and finally dimerization. The dimeric conjugates were evaluated for antibacterial activity with a unique hemocyanin-based biosensor. Based on the outcome of these results, a second-generation set of monomeric conjugates was prepared and found to display significant antibacterial activity, in particular with respect to kanamycin-resistant E. coli.
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Fully orthogonally protected 2-Deoxystreptamine from kanamycin.
The Journal of organic chemistry, 2008Co-Authors: M. Waqar Aslam, Guuske Frederike Busscher, René De Gelder, Floris P. J. T. Rutjes, David P. Weiner, Floris L. Van DelftAbstract:A fully orthogonally protected and enantiopure 2-Deoxystreptamine derivative is prepared in a few straightforward steps from commercially available kanamycin. Resolution of a sterically hindered diacetate was effected by a Verenium esterase and was followed by a chemoselective Staudinger reduction−acylation protocol.
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A short and scalable route to orthogonally O-protected 2-Deoxystreptamine.
The Journal of organic chemistry, 2007Co-Authors: Sebastiaan A. M. W. Van Den Broek, Floris P. J. T. Rutjes, Floris L. Van Delft, Bas W. T. Gruijters, Richard H. BlaauwAbstract:A seven-step synthesis of orthogonally O-protected 2-deoxy-streptamine has been developed from readily available neomycin, with an overall yield of 28%. Key chemical transformations include a chemoselective glycosidic bond hydrolysis and two regioselective protective group manipulations involving acetylation and deacetylation. The synthetic route is amenable to scale-up for the production of multigram quantities of enantiopure and orthogonally O-protected 2-Deoxystreptamine, a versatile scaffold for the generation of libraries of RNA-targeting ligands.
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Carbohydrate mimic of 2-Deoxystreptamine for the preparation of conformationally constrained aminoglycosides
Tetrahedron, 2007Co-Authors: Guuske Frederike Busscher, Floris P. J. T. Rutjes, Sebastiaan A. M. W. Van Den Broek, Floris L. Van DelftAbstract:Abstract The synthesis of a carbohydrate mimic of 2-Deoxystreptamine (2-DOS) is described starting from d -ribose. Crucial steps of the synthesis involve a stereoselective nitroaldol condensation and deoxygenation via elimination–in situ reduction. Moreover, glycosylation of the carbohydrate 2-DOS derivative with a phenyl thioglycoside donor in the presence of TTBP and AgOTf followed by ring-closing metathesis yielded a conformationally restricted aminoglycoside analogue.
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Efficient preparation of a 1,3-diazidocyclitol as a versatile 2-Deoxystreptamine precursor
The Journal of organic chemistry, 2004Co-Authors: Guuske Frederike Busscher, Stan Groothuys, René De Gelder, Floris P. J. T. Rutjes, Floris L. Van DelftAbstract:A synthesis route toward 2-Deoxystreptamine, a common structure in many of the clinically important aminoglycosides, is presented. Starting from p-benzoquinone and cyclopentadiene, 2-Deoxystreptamine is synthesized with key steps involving Pd(0)-catalyzed rearrangement, a retro-Diels-Alder by flash vacuum thermolysis, and Yb(III)-directed regioselective epoxide opening. The obtained diazidocyclitol 17 is a suitable 2-Deoxystreptamine precursor, conveniently protected for incorporation in new aminoglycoside entities.
Jae Kyung Sohng - One of the best experts on this subject based on the ideXlab platform.
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Re-engineering of genetic circuit for 2-Deoxystreptamine (2-DOS) biosynthesis in Escherichia coli BL21 (DE3)
Biotechnology Letters, 2013Co-Authors: Amit Kumar Chaudhary, Je Won Park, Yeo Joon Yoon, Byung-gee Kim, Jae Kyung SohngAbstract:Various approaches for monocistronic constructions of genetic circuits have been designed for metabolite production but there has been no attempt to apply such methodology for aminoglycosides biosynthesis. Here, a simple and commercially available bio-part, despite the current trend focusing on the standardized BioBricks bio-parts available in the registry, is used. A 181-bp nucleotide fragment was designed for the efficient construction of an expression vector for monocistronic assembly of genes. Furthermore, a single vector with multi-monocistronic assembled genes for 2-Deoxystreptamine (2-DOS) synthesis was constructed for production in engineered Escherichia coli. The working efficiency of model vector was concluded by reporter assay whereas the expressions of biosynthesis genes were confirmed by RT-PCR and SDS-PAGE. Production of 2-DOS was confirmed by TLC, LC-ELSD, and ESI–MS/MS.
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2-Deoxystreptamine-containing aminoglycoside antibiotics: Recent advances in the characterization and manipulation of their biosynthetic pathways
Natural product reports, 2013Co-Authors: Sung Ryeol Park, Jae Kyung Sohng, Je Won Park, Yeon Hee Ban, Yeo Joon YoonAbstract:Covering: 2007 to September 2012The 2-Deoxystreptamine-containing aminoglycosides, such as neomycin, kanamycin and gentamicin, are an important class of antibiotics. A detailed understanding of the complete biosynthetic pathway of aminoglycosides and their biosynthetic enzymes will allow us to not only generate more robust antibiotic agents or drugs with other altered biological activities, but also to produce clinically important semi-synthetic antibiotics by direct fermentation. This Highlight focuses on recent advances in the characterization of their biosynthetic enzymes and pathway as well as some chemo-enzymatic and metabolic engineering approaches for the biological production of natural, semi-synthetic, and novel aminoglycosides.
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Heterologous production of paromamine in Streptomyces lividans TK24 using kanamycin biosynthetic genes from Streptomyces kanamyceticus ATCC12853
Molecules and Cells, 2009Co-Authors: Keshav Kumar Nepal, Jae Kyung SohngAbstract:The 2-Deoxystreptamine and paromamine are two key intermediates in kanamycin biosynthesis. In the present study, pSK-2 and pSK-7 recombinant plasmids were constructed with two combinations of genes: kan ABK and kan ABKF and kac A respectively from kanamycin producer Streptomyces kanamyceticus ATCC12853. These plasmids were heterologously expressed into Streptomyces lividans TK24 independently and generated two recombinant strains named S. lividans Sk-2/SL and S. lividans SK-7/SL, respectively. ESI/ MS and ESI-LC/MS analysis of the metabolite from S. lividans SK-2/SL showed that the compound had a molecular mass of 163 [M + H]^+, which corresponds to that of 2-Deoxystreptamine. ESI/MS and MS/MS analysis of metabolites from S. lividans SK-7/SL demonstrated the production of paromamine with a molecular mass of 324 [M + H]^+. In this study, we report the production of paromamine in a heterologous host for the first time. This study will evoke to explore complete biosynthetic pathways of kanamycin and related aminoglycoside antibiotics.
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Heterologous production and detection of recombinant directing 2-Deoxystreptamine (DOS) in the non-aminoglycoside-producing host Streptomyces venezuelae YJ003.
Journal of microbiology and biotechnology, 2008Co-Authors: Nagendra Prasad Kurumbang, Kwangkyoung Liou, Jae Kyung SohngAbstract:2-Deoxystreptamine is a core aglycon that is vital to backbone formation in various aminoglycosides. This core structure can be modified to develop hybrid types of aminoglycoside antibiotics. We obtained three genes responsible for 2-Deoxystreptamine production, neo7, neo6, and neo5, which encode 2-deoxy-scyllo -inosose synthase, L-glutamine: 2-deoxy-scyllo -inosose aminotransferase, and dehydrogenase, respectively, from the neomycin gene cluster These genes were cloned into pIBR25, a Streptomyces expression vector, resulting in pNDOS. The recombinant pNDOS was transformed into a non-aminoglycoside-producing host, Streptomyces venezuelae YJ003, for heterologous expression. Based on comparisons of the retention time on LC-ESI/MS and ESI-MS data with those of the 2-Deoxystreptamine standard, a compound produced by S. venezuelae YJ003/pNDOS was found to be 2-Deoxystreptamine.
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Molecular cloning and characterization of a 2-Deoxystreptamine biosynthetic gene cluster in gentamicin-producing Micromonospora echinospora ATCC15835.
Molecules and cells, 2004Co-Authors: Madan K. Kharel, Kwangkyoung Liou, Hei Chan Lee, Jin Suk Woo, Devi B. Basnet, Young Ho Moon, Jae-jong Kim, Jae Kyung SohngAbstract:The organization of the 2-Deoxystreptamine (DOS) biosynthetic gene cluster of Micromonospora echinospora has been determined. Sequencing of a 14.04 kb-region revealed twelve open reading frames (ORFs): four putative DOS biosynthetic genes (gtmA, B, C, and D), five amino sugars biosynthetic genes (gtmE, G, H, I, and gacB), two aminoglycoside resistance genes (gtmF and J) as well as a hypothetical ORF (gacA). One of the putative DOS biosynthetic genes, gtmA, was expressed in Escherichia coli, and the purified protein was shown to convert glucose-6-phosphate (G-6-P) to 2-deoxy-scyllo-inosose (DOI), a key step in DOS biosynthesis. In addition gtmJ was expressed in Streptomyces lividans and shown to confer gentamicin resistance. Thus gtmA and gtmJ are implicated in the biosynthesis of gentamicin and in resistance to it, respectively.
Fumitaka Kudo - One of the best experts on this subject based on the ideXlab platform.
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biosynthetic enzymes for the aminoglycosides butirosin and neomycin
Methods in Enzymology, 2009Co-Authors: Fumitaka Kudo, Tadashi EguchiAbstract:Butirosin and neomycin belong to a family of clinically valuable 2-Deoxystreptamine (2DOS)-containing aminoglycoside antibiotics. The biosynthetic gene clusters for butirosin and neomycin were identified in 2000 and in 2005, respectively. In recent years, most of the enzymes encoded in the gene clusters have been characterized, and thus almost all the biosynthetic steps leading to the final antibiotics have been understood. This knowledge could shed light on the complex biosynthetic pathways for other related structurally diverse aminoglycoside antibiotics. In this chapter, the enzymatic reactions in the biosynthesis of butirosin and neomycin are reviewed step by step.
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Biosynthesis of 2-Deoxystreptamine-containing Antibiotics in Streptoalloteichus hindustanus JCM 3268: Characterization of 2-Deoxy-scyllo-inosose Synthase
The Journal of Antibiotics, 2006Co-Authors: Toshifumi Hirayama, Katsumi Kakinuma, Fumitaka Kudo, Hideyuki Tamegai, Kazumasa Kojima, Tadashi EguchiAbstract:A part of the new biosynthetic gene cluster for 2-Deoxystreptamine-containing antibiotics was identified from Streptoalloteichus hindustanus . The alloH gene in the gene cluster was deduced to encode 2-deoxy- scyllo -inosose synthase and the expressed protein AlloH was confirmed to have this enzyme activity. Furthermore, biochemical properties of AlloH were studied.
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Biosynthesis of 2-Deoxystreptamine by Three Crucial Enzymes in Streptomyces fradiae NBRC 12773
The Journal of Antibiotics, 2005Co-Authors: Fumitaka Kudo, Tadashi Eguchi, Kenichi Yokoyama, Yasuhito Yamamoto, Katsumi KakinumaAbstract:NeoA, B, and C encoded in the neomycin biosynthetic gene cluster have been enzymatically confirmed to be responsible to the formation of 2-Deoxystreptamine (DOS) in Streptomyces fradiae . NeoC was functionally characterized as 2-deoxy- scyllo -inosose synthase, which catalyzes the carbocycle formation from D -glucose-6-phosphate to 2-deoxy- scyllo -inosose. Further, NeoA appeared to catalyze the oxidation of 2-deoxy- scyllo -inosamine (DOIA) with NAD(P)^+ forming 3-amino-2,3-dideoxy- scyllo -inosose (amino-DOI). Consequently, NeoA was characterized as 2-deoxy- scyllo -inosamine dehydrogenase. Finally, amino-DOI produced by NeoA from DOIA was transformed into DOS by NeoB. Since NeoB (Neo6) was also reported to be L -glutamine:2-deoxy- scyllo -inosose aminotransferase, all the enzymes in the DOS biosynthesis were characterized for the first time.
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Stereochemical recognition of doubly functional aminotransferase in 2-Deoxystreptamine biosynthesis
Journal of the American Chemical Society, 2005Co-Authors: Kenichi Yokoyama, Fumitaka Kudo, Hideyuki Tamegai, Tadashi Eguchi, Mieko Kuwahara, Kousuke Inomata, Katsumi KakinumaAbstract:The doubly functional aminotransferase BtrS in the 2-Deoxystreptamine (DOS) biosynthesis, in which two transaminations are involved, was characterized by a genetic as well as a chemical approach with the heterologously expressed enzyme. The gene disruption study clearly showed that BtrS is involved, in addition to the previously confirmed first transamination, in the second transamination as well. This dual function of BtrS for the DOS biosynthesis was further confirmed by the structural determination of the reverse reaction product from DOS. Enantiospecific formation of the reverse reaction product from DOS clearly showed that BtrS distinguishes the enantiotopic amino groups of DOS, but in contrast, both enantiomers of 2-deoxy-scyllo-inosose (DOI) were efficiently accepted by BtrS to give a racemic product. This unique stereochemical recognition of DOI chirality and DOS prochirality by BtrS is mechanistically explained by a specific hydrogen-bond donating force in the enzyme active site as a particular f...
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Reaction Stereochemistry of 2-Deoxy-scyllo-inosose Synthase, the Key Enzyme in the Biosynthesis of 2-Deoxystreptamine
Chemistry Letters, 2003Co-Authors: Eriko Nango, Tadashi Eguchi, Fumitaka Kudo, Katsumi KakinumaAbstract:The reaction stereochemistry of 2-deoxy-scyllo-inosose (DOI) synthase (DOIS) derived from butirosin-producing Bacillus circulans, the key starter enzyme of 2-Deoxystreptamine biosynthesis, was closely analyzed by use of the purified recombinant DOIS. The stereochemical pathway of the DOIS reaction is common in the aminoglycoside-producing Bacillus and Streptomyces, but is distinct from a related dehydroquinate synthase reaction in the shikimate pathway. Evolutionary relationship between these enzymes is also discussed.
