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Volumn 31, Issue , 2016, Pages 1-7

Unusual chemistries in fungal meroterpenoid biosynthesis

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME P450; DIOXYGENASE; FLAVINE ADENINE NUCLEOTIDE; MEROTERPENOID; MOLECULAR SCAFFOLD; OXYGENASE; POLYKETIDE; QUERCETIN; TERPENOID DERIVATIVE; TERRETONIN; UNCLASSIFIED DRUG; UNSPECIFIC MONOOXYGENASE; TERPENE;

EID: 84947803631     PISSN: 13675931     EISSN: 18790402     Source Type: Journal    
DOI: 10.1016/j.cbpa.2015.11.001     Document Type: Review
Times cited : (54)

References (28)
  • 1
    • 68249113421 scopus 로고    scopus 로고
    • Meroterpenoids produced by fungi
    • Geris R., Simpson T. Meroterpenoids produced by fungi. Nat Prod Rep 2009, 26:1063-1094.
    • (2009) Nat Prod Rep , vol.26 , pp. 1063-1094
    • Geris, R.1    Simpson, T.2
  • 2
    • 84952650492 scopus 로고    scopus 로고
    • Biosynthesis of fungal meroterpenoids
    • In press
    • Matsuda Y., Abe I. Biosynthesis of fungal meroterpenoids. Nat Prod Rep 2015, In press. 10.1039/C5NP00090D.
    • (2015) Nat Prod Rep
    • Matsuda, Y.1    Abe, I.2
  • 3
    • 77957276543 scopus 로고    scopus 로고
    • Reconstitution of a fungal meroterpenoid biosynthesis reveals the involvement of a novel family of terpene cyclases
    • Itoh T., Tokunaga K., Matsuda Y., Fujii I., Abe I., Ebizuka Y., Kushiro T. Reconstitution of a fungal meroterpenoid biosynthesis reveals the involvement of a novel family of terpene cyclases. Nat Chem 2010, 2:858-864.
    • (2010) Nat Chem , vol.2 , pp. 858-864
    • Itoh, T.1    Tokunaga, K.2    Matsuda, Y.3    Fujii, I.4    Abe, I.5    Ebizuka, Y.6    Kushiro, T.7
  • 4
    • 84861435197 scopus 로고    scopus 로고
    • Identification of a key prenyltransferase involved in biosynthesis of the most abundant fungal meroterpenoids derived from 3,5-dimethylorsellinic acid
    • Itoh T., Tokunaga K., Radhakrishnan E.K., Fujii I., Abe I., Ebizuka Y., Kushiro T. Identification of a key prenyltransferase involved in biosynthesis of the most abundant fungal meroterpenoids derived from 3,5-dimethylorsellinic acid. ChemBioChem 2012, 13:1132-1135.
    • (2012) ChemBioChem , vol.13 , pp. 1132-1135
    • Itoh, T.1    Tokunaga, K.2    Radhakrishnan, E.K.3    Fujii, I.4    Abe, I.5    Ebizuka, Y.6    Kushiro, T.7
  • 7
    • 84924662553 scopus 로고    scopus 로고
    • Uncovering the unusual D-ring construction in terretonin biosynthesis by collaboration of a multifunctional cytochrome P450 and a unique isomerase
    • Matsuda Y., Iwabuchi T., Wakimoto T., Awakawa T., Abe I. Uncovering the unusual D-ring construction in terretonin biosynthesis by collaboration of a multifunctional cytochrome P450 and a unique isomerase. J Am Chem Soc 2015, 137:3393-3401.
    • (2015) J Am Chem Soc , vol.137 , pp. 3393-3401
    • Matsuda, Y.1    Iwabuchi, T.2    Wakimoto, T.3    Awakawa, T.4    Abe, I.5
  • 8
    • 84881150453 scopus 로고    scopus 로고
    • Reconstituted biosynthesis of fungal meroterpenoid andrastin A
    • Matsuda Y., Awakawa T., Abe I. Reconstituted biosynthesis of fungal meroterpenoid andrastin A. Tetrahedron 2013, 69:8199-8204.
    • (2013) Tetrahedron , vol.69 , pp. 8199-8204
    • Matsuda, Y.1    Awakawa, T.2    Abe, I.3
  • 9
    • 84863230058 scopus 로고    scopus 로고
    • Two separate gene clusters encode the biosynthetic pathway for the meroterpenoids austinol and dehydroaustinol in Aspergillus nidulans
    • Lo H.-C., Entwistle R., Guo C.-J., Ahuja M., Szewczyk E., Hung J.-H., Chiang Y.-M., Oakley B., Wang C.C. Two separate gene clusters encode the biosynthetic pathway for the meroterpenoids austinol and dehydroaustinol in Aspergillus nidulans. J Am Chem Soc 2012, 134:4709-4720.
    • (2012) J Am Chem Soc , vol.134 , pp. 4709-4720
    • Lo, H.-C.1    Entwistle, R.2    Guo, C.-J.3    Ahuja, M.4    Szewczyk, E.5    Hung, J.-H.6    Chiang, Y.-M.7    Oakley, B.8    Wang, C.C.9
  • 10
    • 84881065394 scopus 로고    scopus 로고
    • Spiro-ring formation is catalyzed by a multifunctional dioxygenase in austinol biosynthesis
    • Matsuda Y., Awakawa T., Wakimoto T., Abe I. Spiro-ring formation is catalyzed by a multifunctional dioxygenase in austinol biosynthesis. J Am Chem Soc 2013, 135:10962-10965.
    • (2013) J Am Chem Soc , vol.135 , pp. 10962-10965
    • Matsuda, Y.1    Awakawa, T.2    Wakimoto, T.3    Abe, I.4
  • 11
    • 84908635350 scopus 로고    scopus 로고
    • Complete biosynthetic pathway of anditomin: nature's sophisticated synthetic route to a complex fungal meroterpenoid
    • Matsuda Y., Wakimoto T., Mori T., Awakawa T., Abe I. Complete biosynthetic pathway of anditomin: nature's sophisticated synthetic route to a complex fungal meroterpenoid. J Am Chem Soc 2014, 136:15326-15336.
    • (2014) J Am Chem Soc , vol.136 , pp. 15326-15336
    • Matsuda, Y.1    Wakimoto, T.2    Mori, T.3    Awakawa, T.4    Abe, I.5
  • 12
    • 72949098828 scopus 로고    scopus 로고
    • Identification of two aflatrem biosynthesis gene loci in Aspergillus flavus and metabolic engineering of Penicillium paxilli to elucidate their function
    • Nicholson M.J., Koulman A., Monahan B.J., Pritchard B.L., Payne G.A., Scott B. Identification of two aflatrem biosynthesis gene loci in Aspergillus flavus and metabolic engineering of Penicillium paxilli to elucidate their function. Appl Environ Microbiol 2009, 75:7469-7481.
    • (2009) Appl Environ Microbiol , vol.75 , pp. 7469-7481
    • Nicholson, M.J.1    Koulman, A.2    Monahan, B.J.3    Pritchard, B.L.4    Payne, G.A.5    Scott, B.6
  • 13
    • 84907145840 scopus 로고    scopus 로고
    • Oxidative rearrangements during fungal biosynthesis
    • Cox R.J. Oxidative rearrangements during fungal biosynthesis. Nat Prod Rep 2014, 31:1405-1424.
    • (2014) Nat Prod Rep , vol.31 , pp. 1405-1424
    • Cox, R.J.1
  • 14
    • 84908093670 scopus 로고    scopus 로고
    • Highly selective but multifunctional oxygenases in secondary metabolism
    • Cochrane R.V., Vederas J.C. Highly selective but multifunctional oxygenases in secondary metabolism. Acc Chem Res 2014, 47:3148-3161.
    • (2014) Acc Chem Res , vol.47 , pp. 3148-3161
    • Cochrane, R.V.1    Vederas, J.C.2
  • 17
    • 84911418489 scopus 로고    scopus 로고
    • Non-heme dioxygenase catalyzes atypical oxidations of 6,7-bicyclic systems to form the 6,6-quinolone core of viridicatin-type fungal alkaloids
    • Ishikawa N., Tanaka H., Koyama F., Noguchi H., Wang C.C., Hotta K., Watanabe K. Non-heme dioxygenase catalyzes atypical oxidations of 6,7-bicyclic systems to form the 6,6-quinolone core of viridicatin-type fungal alkaloids. Angew Chem Int Ed 2014, 17:12880-12884.
    • (2014) Angew Chem Int Ed , vol.17 , pp. 12880-12884
    • Ishikawa, N.1    Tanaka, H.2    Koyama, F.3    Noguchi, H.4    Wang, C.C.5    Hotta, K.6    Watanabe, K.7
  • 19
    • 84923089708 scopus 로고    scopus 로고
    • Terpenoid biosynthesis off the beaten track: unconventional cyclases and their impact on biomimetic synthesis
    • Baunach M., Franke J., Hertweck C. Terpenoid biosynthesis off the beaten track: unconventional cyclases and their impact on biomimetic synthesis. Angew Chem Int Ed 2015, 54:2604-2626.
    • (2015) Angew Chem Int Ed , vol.54 , pp. 2604-2626
    • Baunach, M.1    Franke, J.2    Hertweck, C.3
  • 20
    • 84887738317 scopus 로고    scopus 로고
    • A cytochrome P450 serves as an unexpected terpene cyclase during fungal meroterpenoid biosynthesis
    • Chooi Y.-H., Hong Y.J., Cacho R.A., Tantillo D.J., Tang Y. A cytochrome P450 serves as an unexpected terpene cyclase during fungal meroterpenoid biosynthesis. J Am Chem Soc 2013, 135:16805-16808.
    • (2013) J Am Chem Soc , vol.135 , pp. 16805-16808
    • Chooi, Y.-H.1    Hong, Y.J.2    Cacho, R.A.3    Tantillo, D.J.4    Tang, Y.5
  • 24
    • 39449130475 scopus 로고    scopus 로고
    • Versatility of biological non-heme Fe(II) centers in oxygen activation reactions
    • Kovaleva E.G., Lipscomb J.D. Versatility of biological non-heme Fe(II) centers in oxygen activation reactions. Nat. Chem. Biol. 2008, 4:186-193.
    • (2008) Nat. Chem. Biol. , vol.4 , pp. 186-193
    • Kovaleva, E.G.1    Lipscomb, J.D.2
  • 25
    • 0032755401 scopus 로고    scopus 로고
    • Crystal structure of delta(5)-3-ketosteroid isomerase from Pseudomonas testosteroni in complex with equilenin settles the correct hydrogen bonding scheme for transition state stabilization
    • Cho H.-S., Ha N.-C., Choi G., Kim H.-J., Lee D., Oh K.S., Kim K.S., Lee W., Choi K.Y., Oh B.-H. Crystal structure of delta(5)-3-ketosteroid isomerase from Pseudomonas testosteroni in complex with equilenin settles the correct hydrogen bonding scheme for transition state stabilization. J Biol Chem 1999, 274:32863-32868.
    • (1999) J Biol Chem , vol.274 , pp. 32863-32868
    • Cho, H.-S.1    Ha, N.-C.2    Choi, G.3    Kim, H.-J.4    Lee, D.5    Oh, K.S.6    Kim, K.S.7    Lee, W.8    Choi, K.Y.9    Oh, B.-H.10
  • 27
    • 3142559476 scopus 로고    scopus 로고
    • Structure of the polyketide cyclase SnoaL reveals a novel mechanism for enzymatic aldol condensation
    • Sultana A., Kallio P., Jansson A., Wang J.S., Niemi J., Mäntsälä P., Schneider G. Structure of the polyketide cyclase SnoaL reveals a novel mechanism for enzymatic aldol condensation. EMBO J 2004, 23:1911-1921.
    • (2004) EMBO J , vol.23 , pp. 1911-1921
    • Sultana, A.1    Kallio, P.2    Jansson, A.3    Wang, J.S.4    Niemi, J.5    Mäntsälä, P.6    Schneider, G.7
  • 28
    • 84896707811 scopus 로고    scopus 로고
    • Allosteric regulation of epoxide opening cascades by a pair of epoxide hydrolases in monensin biosynthesis
    • Minami A., Ose T., Sato K., Oikawa A., Kuroki K., Maenaka K., Oguri H., Oikawa H. Allosteric regulation of epoxide opening cascades by a pair of epoxide hydrolases in monensin biosynthesis. ACS Chem Biol 2013, 9:562-569.
    • (2013) ACS Chem Biol , vol.9 , pp. 562-569
    • Minami, A.1    Ose, T.2    Sato, K.3    Oikawa, A.4    Kuroki, K.5    Maenaka, K.6    Oguri, H.7    Oikawa, H.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.