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Volumn 13, Issue 2, 2009, Pages 161-170

Progress in aminocyclitol biosynthesis

Author keywords

[No Author keywords available]

Indexed keywords

AMINOCYCLITOL; NATURAL PRODUCT; SUGAR PHOSPHATE;

EID: 65349195723     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpa.2009.02.030     Document Type: Review
Times cited : (33)

References (50)
  • 1
    • 0037321281 scopus 로고    scopus 로고
    • 7N aminocyclitol family of natural products
    • 7N aminocyclitol family of natural products. Nat Prod Rep 20 (2003) 137-166
    • (2003) Nat Prod Rep , vol.20 , pp. 137-166
    • Mahmud, T.1
  • 2
    • 33751228406 scopus 로고    scopus 로고
    • Aminoglycosides: ancient and modern
    • Davies J.E. Aminoglycosides: ancient and modern. J Antibiot (Tokyo) 59 (2006) 529-532
    • (2006) J Antibiot (Tokyo) , vol.59 , pp. 529-532
    • Davies, J.E.1
  • 3
    • 49049119763 scopus 로고    scopus 로고
    • Efficacy and safety of kanamycin, ethionamide, PAS and cycloserine in multidrug-resistant pulmonary tuberculosis patients.
    • Prasad R., Verma S.K., Sahai S., Kumar S., and Jain A. Efficacy and safety of kanamycin, ethionamide, PAS and cycloserine in multidrug-resistant pulmonary tuberculosis patients. Indian J Chest Dis Allied Sci 48 (2006) 183-186
    • (2006) Indian J Chest Dis Allied Sci , vol.48 , pp. 183-186
    • Prasad, R.1    Verma, S.K.2    Sahai, S.3    Kumar, S.4    Jain, A.5
  • 4
    • 38049084300 scopus 로고    scopus 로고
    • Prediction of aminoglycoside response against methicillin-resistant Staphylococcus aureus infection in burn patients by artificial neural network modeling
    • Yamamura S., Kawada K., Takehira R., Nishizawa K., Katayama S., Hirano M., and Momose Y. Prediction of aminoglycoside response against methicillin-resistant Staphylococcus aureus infection in burn patients by artificial neural network modeling. Biomed Pharmacother 62 (2008) 53-58
    • (2008) Biomed Pharmacother , vol.62 , pp. 53-58
    • Yamamura, S.1    Kawada, K.2    Takehira, R.3    Nishizawa, K.4    Katayama, S.5    Hirano, M.6    Momose, Y.7
  • 5
    • 34548610296 scopus 로고    scopus 로고
    • Biosynthesis of unusual aminocyclitol-containing natural products
    • Mahmud T., Flatt P.M., and Wu X. Biosynthesis of unusual aminocyclitol-containing natural products. J Nat Prod 70 (2007) 1384-1391
    • (2007) J Nat Prod , vol.70 , pp. 1384-1391
    • Mahmud, T.1    Flatt, P.M.2    Wu, X.3
  • 6
    • 33846928949 scopus 로고    scopus 로고
    • A comparative analysis of the sugar phosphate cyclase superfamily involved in primary and secondary metabolism
    • Describes a detailed comparative analysis of sugar phosphate cyclases and the identification of a new class of sugar phosphate cyclases that might regulate the biosynthesis of a novel set of secondary metabolites in fungi and cyanobacteria.
    • Wu X., Flatt P.M., Schlorke O., Zeeck A., Dairi T., and Mahmud T. A comparative analysis of the sugar phosphate cyclase superfamily involved in primary and secondary metabolism. Chembiochem 8 (2007) 239-248. Describes a detailed comparative analysis of sugar phosphate cyclases and the identification of a new class of sugar phosphate cyclases that might regulate the biosynthesis of a novel set of secondary metabolites in fungi and cyanobacteria.
    • (2007) Chembiochem , vol.8 , pp. 239-248
    • Wu, X.1    Flatt, P.M.2    Schlorke, O.3    Zeeck, A.4    Dairi, T.5    Mahmud, T.6
  • 7
    • 33751325834 scopus 로고    scopus 로고
    • Biosynthesis of 2-deoxystreptamine-containing aminoglycoside antibiotics
    • Llewellyn N.M., and Spencer J.B. Biosynthesis of 2-deoxystreptamine-containing aminoglycoside antibiotics. Nat Prod Rep 23 (2006) 864-874
    • (2006) Nat Prod Rep , vol.23 , pp. 864-874
    • Llewellyn, N.M.1    Spencer, J.B.2
  • 8
    • 36048999783 scopus 로고    scopus 로고
    • Cloning of the pactamycin biosynthetic gene cluster and characterization of a crucial glycosyltransferase prior to a unique cyclopentane ring formation
    • Kudo F., Kasama Y., Hirayama T., and Eguchi T. Cloning of the pactamycin biosynthetic gene cluster and characterization of a crucial glycosyltransferase prior to a unique cyclopentane ring formation. J Antibiot (Tokyo) 60 (2007) 492-503
    • (2007) J Antibiot (Tokyo) , vol.60 , pp. 492-503
    • Kudo, F.1    Kasama, Y.2    Hirayama, T.3    Eguchi, T.4
  • 9
    • 0035906453 scopus 로고    scopus 로고
    • Biosynthetic studies on the cyclopentane ring formation of allosamizoline, an aminocyclitol component of the chitinase inhibitor allosamidin
    • Sakuda S., Sugiyama Y., Zhou Z.Y., Takao H., Ikeda H., Kakinuma K., Yamada Y., and Nagasawa H. Biosynthetic studies on the cyclopentane ring formation of allosamizoline, an aminocyclitol component of the chitinase inhibitor allosamidin. J Org Chem 66 (2001) 3356-3361
    • (2001) J Org Chem , vol.66 , pp. 3356-3361
    • Sakuda, S.1    Sugiyama, Y.2    Zhou, Z.Y.3    Takao, H.4    Ikeda, H.5    Kakinuma, K.6    Yamada, Y.7    Nagasawa, H.8
  • 11
    • 39049184513 scopus 로고    scopus 로고
    • The structure and mechanism of myo-inositol-1-phosphate synthase
    • Geiger J.H., and Jin X. The structure and mechanism of myo-inositol-1-phosphate synthase. Subcell Biochem 39 (2006) 157-180
    • (2006) Subcell Biochem , vol.39 , pp. 157-180
    • Geiger, J.H.1    Jin, X.2
  • 12
    • 0037321888 scopus 로고    scopus 로고
    • The biosynthesis of shikimate metabolites
    • Knaggs A.R. The biosynthesis of shikimate metabolites. Nat Prod Rep 20 (2003) 119-136
    • (2003) Nat Prod Rep , vol.20 , pp. 119-136
    • Knaggs, A.R.1
  • 13
    • 0031260232 scopus 로고    scopus 로고
    • Natural products derived from unusual variants of the shikimate pathway
    • Floss H.G. Natural products derived from unusual variants of the shikimate pathway. Nat Prod Rep 14 (1997) 433-452
    • (1997) Nat Prod Rep , vol.14 , pp. 433-452
    • Floss, H.G.1
  • 14
    • 33644519643 scopus 로고    scopus 로고
    • DNA sequencing and transcriptional analysis of the kasugamycin biosynthetic gene cluster from Streptomyces kasugaensis M338-M1
    • Ikeno S., Aoki D., Hamada M., Hori M., and Tsuchiya K.S. DNA sequencing and transcriptional analysis of the kasugamycin biosynthetic gene cluster from Streptomyces kasugaensis M338-M1. J Antibiot (Tokyo) 59 (2006) 18-28
    • (2006) J Antibiot (Tokyo) , vol.59 , pp. 18-28
    • Ikeno, S.1    Aoki, D.2    Hamada, M.3    Hori, M.4    Tsuchiya, K.S.5
  • 15
    • 33947634127 scopus 로고    scopus 로고
    • Biosynthesis of aminocyclitol-aminoglycoside antibiotics and related compounds
    • Flatt P.M., and Mahmud T. Biosynthesis of aminocyclitol-aminoglycoside antibiotics and related compounds. Nat Prod Rep 24 (2007) 358-392
    • (2007) Nat Prod Rep , vol.24 , pp. 358-392
    • Flatt, P.M.1    Mahmud, T.2
  • 16
    • 44849132618 scopus 로고    scopus 로고
    • Biosynthesis of spectinomycin: heterologous production of spectinomycin and spectinamine in an aminoglycoside-deficient host, Streptomyces venezuelae YJ003
    • Thapa L.P., Oh T.J., Liou K., and Sohng J.K. Biosynthesis of spectinomycin: heterologous production of spectinomycin and spectinamine in an aminoglycoside-deficient host, Streptomyces venezuelae YJ003. J Appl Microbiol 105 (2008) 300-308
    • (2008) J Appl Microbiol , vol.105 , pp. 300-308
    • Thapa, L.P.1    Oh, T.J.2    Liou, K.3    Sohng, J.K.4
  • 17
    • 0347359004 scopus 로고    scopus 로고
    • Functional analysis of spectinomycin biosynthesis genes from Streptomyces spectabilis ATCC 27741
    • Jo Y.Y., Kim S.H., Yang Y.Y., Kang C.M., Sohng J.K., and Suh J.W. Functional analysis of spectinomycin biosynthesis genes from Streptomyces spectabilis ATCC 27741. J Microbiol Biotechnol 13 (2003) 906-911
    • (2003) J Microbiol Biotechnol , vol.13 , pp. 906-911
    • Jo, Y.Y.1    Kim, S.H.2    Yang, Y.Y.3    Kang, C.M.4    Sohng, J.K.5    Suh, J.W.6
  • 19
    • 33746218295 scopus 로고    scopus 로고
    • Production of hygromycin A analogs in Streptomyces hygroscopicus NRRL 2388 through identification and manipulation of the biosynthetic gene cluster
    • Palaniappan N., Ayers S., Gupta S., Habib el S., and Reynolds K.A. Production of hygromycin A analogs in Streptomyces hygroscopicus NRRL 2388 through identification and manipulation of the biosynthetic gene cluster. Chem Biol 13 (2006) 753-764
    • (2006) Chem Biol , vol.13 , pp. 753-764
    • Palaniappan, N.1    Ayers, S.2    Gupta, S.3    Habib el, S.4    Reynolds, K.A.5
  • 20
    • 54049104407 scopus 로고    scopus 로고
    • An O-phosphotransferase catalyzes phosphorylation of hygromycin A in the antibiotic-producing organism Streptomyces hygroscopicus
    • Dhote V., Gupta S., and Reynolds K.A. An O-phosphotransferase catalyzes phosphorylation of hygromycin A in the antibiotic-producing organism Streptomyces hygroscopicus. Antimicrob Agents Chemother 52 (2008) 3580-3588
    • (2008) Antimicrob Agents Chemother , vol.52 , pp. 3580-3588
    • Dhote, V.1    Gupta, S.2    Reynolds, K.A.3
  • 21
    • 34247873120 scopus 로고    scopus 로고
    • Characterization of the enzyme BtrD from Bacillus circulans and revision of its functional assignment in the biosynthesis of butirosin
    • Description of the function of BtrD as a deacetylase and not a nucleotidyltransferase as reported previously.
    • Truman A.W., Huang F., Llewellyn N.M., and Spencer J.B. Characterization of the enzyme BtrD from Bacillus circulans and revision of its functional assignment in the biosynthesis of butirosin. Angew Chem Int Ed Engl 46 (2007) 1462-1464. Description of the function of BtrD as a deacetylase and not a nucleotidyltransferase as reported previously.
    • (2007) Angew Chem Int Ed Engl , vol.46 , pp. 1462-1464
    • Truman, A.W.1    Huang, F.2    Llewellyn, N.M.3    Spencer, J.B.4
  • 22
    • 33748255080 scopus 로고    scopus 로고
    • Crystal structures of the PLP- and PMP-bound forms of BtrR, a dual functional aminotransferase involved in butirosin biosynthesis
    • Popovic B., Tang X., Chirgadze D.Y., Huang F., Blundell T.L., and Spencer J.B. Crystal structures of the PLP- and PMP-bound forms of BtrR, a dual functional aminotransferase involved in butirosin biosynthesis. Proteins 65 (2006) 220-230
    • (2006) Proteins , vol.65 , pp. 220-230
    • Popovic, B.1    Tang, X.2    Chirgadze, D.Y.3    Huang, F.4    Blundell, T.L.5    Spencer, J.B.6
  • 23
    • 37049024768 scopus 로고    scopus 로고
    • Characterization and mechanistic study of a radical SAM dehydrogenase in the biosynthesis of butirosin
    • Describes the first example of oxidation of a hydroxyl group by a radical SAM enzyme. The mechanism is unique and is most probably absent in the biosynthetic pathways of other DOI-derived aminocyclitols.
    • Yokoyama K., Numakura M., Kudo F., Ohmori D., and Eguchi T. Characterization and mechanistic study of a radical SAM dehydrogenase in the biosynthesis of butirosin. J Am Chem Soc 129 (2007) 15147-15155. Describes the first example of oxidation of a hydroxyl group by a radical SAM enzyme. The mechanism is unique and is most probably absent in the biosynthetic pathways of other DOI-derived aminocyclitols.
    • (2007) J Am Chem Soc , vol.129 , pp. 15147-15155
    • Yokoyama, K.1    Numakura, M.2    Kudo, F.3    Ohmori, D.4    Eguchi, T.5
  • 24
    • 33750935120 scopus 로고    scopus 로고
    • Role of glutamate 243 in the active site of 2-deoxy-scyllo-inosose synthase from Bacillus circulans
    • Hirayama T., Kudo F., Huang Z., and Eguchi T. Role of glutamate 243 in the active site of 2-deoxy-scyllo-inosose synthase from Bacillus circulans. Bioorg Med Chem 15 (2007) 418-423
    • (2007) Bioorg Med Chem , vol.15 , pp. 418-423
    • Hirayama, T.1    Kudo, F.2    Huang, Z.3    Eguchi, T.4
  • 25
    • 34547562892 scopus 로고    scopus 로고
    • Elaboration of neosamine rings in the biosynthesis of neomycin and butirosin
    • Describes the bifunctional roles of the oxidases and the aminotransferases in the neomycin and butirosin pathways.
    • Huang F., Spiteller D., Koorbanally N.A., Li Y., Llewellyn N.M., and Spencer J.B. Elaboration of neosamine rings in the biosynthesis of neomycin and butirosin. Chembiochem 8 (2007) 283-288. Describes the bifunctional roles of the oxidases and the aminotransferases in the neomycin and butirosin pathways.
    • (2007) Chembiochem , vol.8 , pp. 283-288
    • Huang, F.1    Spiteller, D.2    Koorbanally, N.A.3    Li, Y.4    Llewellyn, N.M.5    Spencer, J.B.6
  • 26
    • 44049095529 scopus 로고    scopus 로고
    • Involvement of two distinct N-acetylglucosaminyltransferases and a dual-function deacetylase in neomycin biosynthesis
    • Describes the distinct substrate specificity of the N-acetylglucosaminyltransferases and the bifunctional roles of the deacetylase from the neomycin pathway.
    • Yokoyama K., Yamamoto Y., Kudo F., and Eguchi T. Involvement of two distinct N-acetylglucosaminyltransferases and a dual-function deacetylase in neomycin biosynthesis. Chembiochem 9 (2008) 865-869. Describes the distinct substrate specificity of the N-acetylglucosaminyltransferases and the bifunctional roles of the deacetylase from the neomycin pathway.
    • (2008) Chembiochem , vol.9 , pp. 865-869
    • Yokoyama, K.1    Yamamoto, Y.2    Kudo, F.3    Eguchi, T.4
  • 27
    • 34648813081 scopus 로고    scopus 로고
    • Heterologous expression of the kanamycin biosynthetic gene cluster (pSKC2) in Streptomyces venezuelae YJ003
    • Thapa L.P., Oh T.J., Lee H.C., Liou K., Park J.W., Yoon Y.J., and Sohng J.K. Heterologous expression of the kanamycin biosynthetic gene cluster (pSKC2) in Streptomyces venezuelae YJ003. Appl Microbiol Biotechnol 76 (2007) 1357-1364
    • (2007) Appl Microbiol Biotechnol , vol.76 , pp. 1357-1364
    • Thapa, L.P.1    Oh, T.J.2    Lee, H.C.3    Liou, K.4    Park, J.W.5    Yoon, Y.J.6    Sohng, J.K.7
  • 28
    • 46149125940 scopus 로고    scopus 로고
    • Genetic dissection of the biosynthetic route to gentamicin A2 by heterologous expression of its minimal gene set
    • Using heterologous expression of different combinations of putative 2-deoxystreptamine biosynthetic genes the authors discovered a subset of genes that is responsible for the biosynthesis of the core aminocyclitol of gentamicin. This in vivo study provided direct evidence for the biosynthetic pathway to gentamicin, allowing the unequivocal assignment of the biochemical role of each gene products.
    • Park J.W., Hong J.S., Parajuli N., Jung W.S., Park S.R., Lim S.K., Sohng J.K., and Yoon Y.J. Genetic dissection of the biosynthetic route to gentamicin A2 by heterologous expression of its minimal gene set. Proc Natl Acad Sci U S A 105 (2008) 8399-8404. Using heterologous expression of different combinations of putative 2-deoxystreptamine biosynthetic genes the authors discovered a subset of genes that is responsible for the biosynthesis of the core aminocyclitol of gentamicin. This in vivo study provided direct evidence for the biosynthetic pathway to gentamicin, allowing the unequivocal assignment of the biochemical role of each gene products.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 8399-8404
    • Park, J.W.1    Hong, J.S.2    Parajuli, N.3    Jung, W.S.4    Park, S.R.5    Lim, S.K.6    Sohng, J.K.7    Yoon, Y.J.8
  • 29
    • 45449088302 scopus 로고    scopus 로고
    • Gene inactivation study of gntE reveals its role in the first step of pseudotrisaccharide modifications in gentamicin biosynthesis
    • Kim J.Y., Suh J.W., Kang S.H., Phan T.H., Park S.H., and Kwon H.J. Gene inactivation study of gntE reveals its role in the first step of pseudotrisaccharide modifications in gentamicin biosynthesis. Biochem Biophys Res Commun 372 (2008) 730-734
    • (2008) Biochem Biophys Res Commun , vol.372 , pp. 730-734
    • Kim, J.Y.1    Suh, J.W.2    Kang, S.H.3    Phan, T.H.4    Park, S.H.5    Kwon, H.J.6
  • 30
    • 37849043342 scopus 로고    scopus 로고
    • +
    • Describes the first crystal structures of 2-deoxy-scyllo-inosose synthase and a comparative study between the 2-deoxy-scyllo-inosose synthases and the dehydroquinate synthases.
    • +. Proteins 70 (2008) 517-527. Describes the first crystal structures of 2-deoxy-scyllo-inosose synthase and a comparative study between the 2-deoxy-scyllo-inosose synthases and the dehydroquinate synthases.
    • (2008) Proteins , vol.70 , pp. 517-527
    • Nango, E.1    Kumasaka, T.2    Hirayama, T.3    Tanaka, N.4    Eguchi, T.5
  • 31
    • 0032537722 scopus 로고    scopus 로고
    • Structure of dehydroquinate synthase reveals an active site capable of multistep catalysis
    • Carpenter E.P., Hawkins A.R., Frost J.W., and Brown K.A. Structure of dehydroquinate synthase reveals an active site capable of multistep catalysis. Nature 394 (1998) 299-302
    • (1998) Nature , vol.394 , pp. 299-302
    • Carpenter, E.P.1    Hawkins, A.R.2    Frost, J.W.3    Brown, K.A.4
  • 32
    • 17744378979 scopus 로고    scopus 로고
    • Stereochemical recognition of doubly functional aminotransferase in 2-deoxystreptamine biosynthesis
    • Yokoyama K., Kudo F., Kuwahara M., Inomata K., Tamegai H., Eguchi T., and Kakinuma K. Stereochemical recognition of doubly functional aminotransferase in 2-deoxystreptamine biosynthesis. J Am Chem Soc 127 (2005) 5869-5874
    • (2005) J Am Chem Soc , vol.127 , pp. 5869-5874
    • Yokoyama, K.1    Kudo, F.2    Kuwahara, M.3    Inomata, K.4    Tamegai, H.5    Eguchi, T.6    Kakinuma, K.7
  • 33
    • 0028936482 scopus 로고
    • Enzymatic synthesis of aminocyclitol moieties of aminoglycoside antibiotics from inositol by Streptomyces spp.: detection of glutamine-aminocyclitol aminotransferase and diaminocyclitol aminotransferase activities in a spectinomycin producer
    • Walker J.B. Enzymatic synthesis of aminocyclitol moieties of aminoglycoside antibiotics from inositol by Streptomyces spp.: detection of glutamine-aminocyclitol aminotransferase and diaminocyclitol aminotransferase activities in a spectinomycin producer. J Bacteriol 177 (1995) 818-822
    • (1995) J Bacteriol , vol.177 , pp. 818-822
    • Walker, J.B.1
  • 34
    • 13644269270 scopus 로고    scopus 로고
    • A new family of glucose-1-phosphate/glucosamine-1-phosphate nucleotidylyltransferase in the biosynthetic pathways for antibiotics
    • Kudo F., Kawabe K., Kuriki H., Eguchi T., and Kakinuma K. A new family of glucose-1-phosphate/glucosamine-1-phosphate nucleotidylyltransferase in the biosynthetic pathways for antibiotics. J Am Chem Soc 127 (2005) 1711-1718
    • (2005) J Am Chem Soc , vol.127 , pp. 1711-1718
    • Kudo, F.1    Kawabe, K.2    Kuriki, H.3    Eguchi, T.4    Kakinuma, K.5
  • 35
    • 31444455929 scopus 로고    scopus 로고
    • Biosynthesis of 2-deoxystreptamine by three crucial enzymes in Streptomyces fradiae NBRC 12773
    • Kudo F., Yamamoto Y., Yokoyama K., Eguchi T., and Kakinuma K. Biosynthesis of 2-deoxystreptamine by three crucial enzymes in Streptomyces fradiae NBRC 12773. J Antibiot (Tokyo) 58 (2005) 766-774
    • (2005) J Antibiot (Tokyo) , vol.58 , pp. 766-774
    • Kudo, F.1    Yamamoto, Y.2    Yokoyama, K.3    Eguchi, T.4    Kakinuma, K.5
  • 36
    • 50149113479 scopus 로고    scopus 로고
    • Mechanistic study on the reaction of a radical SAM dehydrogenase BtrN by electron paramagnetic resonance spectroscopy
    • Yokoyama K., Ohmori D., Kudo F., and Eguchi T. Mechanistic study on the reaction of a radical SAM dehydrogenase BtrN by electron paramagnetic resonance spectroscopy. Biochemistry 47 (2008) 8950-8960
    • (2008) Biochemistry , vol.47 , pp. 8950-8960
    • Yokoyama, K.1    Ohmori, D.2    Kudo, F.3    Eguchi, T.4
  • 37
    • 34248652943 scopus 로고    scopus 로고
    • Unique O-ribosylation in the biosynthesis of butirosin
    • Kudo F., Fujii T., Kinoshita S., and Eguchi T. Unique O-ribosylation in the biosynthesis of butirosin. Bioorg Med Chem 15 (2007) 4360-4368
    • (2007) Bioorg Med Chem , vol.15 , pp. 4360-4368
    • Kudo, F.1    Fujii, T.2    Kinoshita, S.3    Eguchi, T.4
  • 38
    • 34247198471 scopus 로고    scopus 로고
    • Biosynthesis of butirosin: transfer and deprotection of the unique amino acid side chain
    • Describes a complete elucidation of ACP-mediated formation and transfer of (S)-4-amino-2-hydroxybutyrate side chain in butirosin biosynthesis. The pathway involves unusual protective biochemistry via γ-L-glutamylation of an ACP-bound substrate.
    • Llewellyn N.M., Li Y., and Spencer J.B. Biosynthesis of butirosin: transfer and deprotection of the unique amino acid side chain. Chem Biol 14 (2007) 379-386. Describes a complete elucidation of ACP-mediated formation and transfer of (S)-4-amino-2-hydroxybutyrate side chain in butirosin biosynthesis. The pathway involves unusual protective biochemistry via γ-L-glutamylation of an ACP-bound substrate.
    • (2007) Chem Biol , vol.14 , pp. 379-386
    • Llewellyn, N.M.1    Li, Y.2    Spencer, J.B.3
  • 39
    • 49249130589 scopus 로고    scopus 로고
    • Chemoenzymatic acylation of aminoglycoside antibiotics
    • Llewellyn N.M., and Spencer J.B. Chemoenzymatic acylation of aminoglycoside antibiotics. Chem Commun (Camb) (2008) 3786-3788
    • (2008) Chem Commun (Camb) , pp. 3786-3788
    • Llewellyn, N.M.1    Spencer, J.B.2
  • 40
    • 38349036020 scopus 로고    scopus 로고
    • Isotope tracer investigations of natural products biosynthesis: the discovery of novel metabolic pathways
    • Mahmud T. Isotope tracer investigations of natural products biosynthesis: the discovery of novel metabolic pathways. J Labelled Comp Radiophar 50 (2007) 1039-1051
    • (2007) J Labelled Comp Radiophar , vol.50 , pp. 1039-1051
    • Mahmud, T.1
  • 41
    • 0033574676 scopus 로고    scopus 로고
    • 7-cyclitol synthase related to 3-dehydroquinate synthases and is involved in the biosynthesis of the alpha-glucosidase inhibitor acarbose
    • 7-cyclitol synthase related to 3-dehydroquinate synthases and is involved in the biosynthesis of the alpha-glucosidase inhibitor acarbose. J Biol Chem 274 (1999) 10889-10896
    • (1999) J Biol Chem , vol.274 , pp. 10889-10896
    • Stratmann, A.1    Mahmud, T.2    Lee, S.3    Distler, J.4    Floss, H.G.5    Piepersberg, W.6
  • 43
    • 0345270037 scopus 로고    scopus 로고
    • The acarbose-biosynthetic enzyme AcbO from Actinoplanes sp. SE 50/110 is a 2-epi-5-epi-valiolone-7-phosphate 2-epimerase
    • Zhang C.S., Podeschwa M., Altenbach H.J., Piepersberg W., and Wehmeier U.F. The acarbose-biosynthetic enzyme AcbO from Actinoplanes sp. SE 50/110 is a 2-epi-5-epi-valiolone-7-phosphate 2-epimerase. FEBS Lett 540 (2003) 47-52
    • (2003) FEBS Lett , vol.540 , pp. 47-52
    • Zhang, C.S.1    Podeschwa, M.2    Altenbach, H.J.3    Piepersberg, W.4    Wehmeier, U.F.5
  • 44
    • 25144443003 scopus 로고    scopus 로고
    • Gene cluster responsible for validamycin biosynthesis in Streptomyces hygroscopicus subsp. jinggangensis 5008
    • Yu Y., Bai L., Minagawa K., Jian X., Li L., Li J., Chen S., Cao E., Mahmud T., Floss H.G., et al. Gene cluster responsible for validamycin biosynthesis in Streptomyces hygroscopicus subsp. jinggangensis 5008. Appl Environ Microbiol 71 (2005) 5066-5076
    • (2005) Appl Environ Microbiol , vol.71 , pp. 5066-5076
    • Yu, Y.1    Bai, L.2    Minagawa, K.3    Jian, X.4    Li, L.5    Li, J.6    Chen, S.7    Cao, E.8    Mahmud, T.9    Floss, H.G.10
  • 45
    • 33646054552 scopus 로고    scopus 로고
    • Functional analysis of the validamycin biosynthetic gene cluster and engineered production of validoxylamine A
    • Bai L., Li L., Xu H., Minagawa K., Yu Y., Zhang Y., Zhou X., Floss H.G., Mahmud T., and Deng Z. Functional analysis of the validamycin biosynthetic gene cluster and engineered production of validoxylamine A. Chem Biol 13 (2006) 387-397
    • (2006) Chem Biol , vol.13 , pp. 387-397
    • Bai, L.1    Li, L.2    Xu, H.3    Minagawa, K.4    Yu, Y.5    Zhang, Y.6    Zhou, X.7    Floss, H.G.8    Mahmud, T.9    Deng, Z.10
  • 46
    • 50849144645 scopus 로고    scopus 로고
    • Genetic organization of the putative salbostatin biosynthetic gene cluster including the 2-epi-5-epi-valiolone synthase gene in Streptomyces albus ATCC 21838
    • Choi W.S., Wu X., Choeng Y.H., Mahmud T., Jeong B.C., Lee S.H., Chang Y.K., Kim C.J., and Hong S.K. Genetic organization of the putative salbostatin biosynthetic gene cluster including the 2-epi-5-epi-valiolone synthase gene in Streptomyces albus ATCC 21838. Appl Microbiol Biotechnol 80 (2008) 637-645
    • (2008) Appl Microbiol Biotechnol , vol.80 , pp. 637-645
    • Choi, W.S.1    Wu, X.2    Choeng, Y.H.3    Mahmud, T.4    Jeong, B.C.5    Lee, S.H.6    Chang, Y.K.7    Kim, C.J.8    Hong, S.K.9
  • 47
    • 60449083176 scopus 로고    scopus 로고
    • Biosynthetic gene cluster of cetoniacytone A, an unusual aminocyclitol from the endosymbiotic Bacterium Actinomyces sp. Lu 9419
    • Description of the first 2-epi-5-epi-valiolone epimerases that belong to the Vicinal Oxygen Chelate (VOC) superfamily.
    • Wu X., Flatt P.M., Xu H., and Mahmud T. Biosynthetic gene cluster of cetoniacytone A, an unusual aminocyclitol from the endosymbiotic Bacterium Actinomyces sp. Lu 9419. Chembiochem 10 (2009) 304-314. Description of the first 2-epi-5-epi-valiolone epimerases that belong to the Vicinal Oxygen Chelate (VOC) superfamily.
    • (2009) Chembiochem , vol.10 , pp. 304-314
    • Wu, X.1    Flatt, P.M.2    Xu, H.3    Mahmud, T.4
  • 49
    • 49049110489 scopus 로고    scopus 로고
    • Catalytic analysis of the validamycin glycosyltransferase (ValG) and enzymatic production of 4″-epi-validamycin A
    • Xu H., Minagawa K., Bai L., Deng Z., and Mahmud T. Catalytic analysis of the validamycin glycosyltransferase (ValG) and enzymatic production of 4″-epi-validamycin A. J Nat Prod 71 (2008) 1233-1236
    • (2008) J Nat Prod , vol.71 , pp. 1233-1236
    • Xu, H.1    Minagawa, K.2    Bai, L.3    Deng, Z.4    Mahmud, T.5
  • 50
    • 58149148222 scopus 로고    scopus 로고
    • Genetically engineered production of 1,1′-bis-valienamine and validienamycin in Streptomyces hygroscopicus and their conversion to valienamine
    • Xu H., Yang J., Bai L., Deng Z., and Mahmud T. Genetically engineered production of 1,1′-bis-valienamine and validienamycin in Streptomyces hygroscopicus and their conversion to valienamine. Appl Microbiol Biotechnol 81 (2009) 895-902
    • (2009) Appl Microbiol Biotechnol , vol.81 , pp. 895-902
    • Xu, H.1    Yang, J.2    Bai, L.3    Deng, Z.4    Mahmud, T.5


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