KEGG   PATHWAY: rn01057
Entry
rn01057                     Pathway                                

Name
Biosynthesis of type II polyketide products
Class
Metabolism; Metabolism of terpenoids and polyketides
Pathway map
rn01057  Biosynthesis of type II polyketide products
rn01057

Module
M00779  Dihydrokalafungin biosynthesis, octaketide => dihydrokalafungin [PATH:rn01057]
M00780  Tetracycline/oxytetracycline biosynthesis, pretetramide => tetracycline/oxytetracycline [PATH:rn01057]
M00781  Nogalavinone/aklavinone biosynthesis, deoxynogalonate/deoxyaklanonate => nogalavinone/aklavinone [PATH:rn01057]
M00782  Mithramycin biosynthesis, 4-demethylpremithramycinone => mithramycin [PATH:rn01057]
M00783  Tetracenomycin C/8-demethyltetracenomycin C biosynthesis, tetracenomycin F2 => tetracenomycin C/8-demethyltetracenomycin C [PATH:rn01057]
M00784  Elloramycin biosynthesis, 8-demethyltetracenomycin C => elloramycin A [PATH:rn01057]
M00823  Chlortetracycline biosynthesis, pretetramide => chlortetracycline [PATH:rn01057]
Reaction
R04060  anhydrotetracycline,NADPH:oxygen oxidoreductase (6-hydroxylating)
R05459  tetracycline:coenzyme-F420 oxidoreductase
R05462  4-hydroxy-6-methylpretetramide,NADPH:oxygen oxidoreductase (12a-hydroxylating)
R05463  6-methylpretetramide,NADPH:oxygen oxidoreductase (4-hydroxylating)
R05705  FMNH2:NAD+ oxidoreductase
R06650   
R06651   
R06652   
R06653   
R06654   
R06655   
R06656   
R06659   
R06660  dTDP-D-olivose:compound-100-1 O-beta-D-olivosyltransferase
R06661   
R06662   
R06664   
R06665   
R06666   
R06667   
R06668  dTDP-D-olivose:urdamycin-G D-olivosyltransferase
R06670   
R06671   
R06672   
R06673   
R06674   
R06675  S-adenosyl-L-methionine:nogalonic-acid O-methyltransferase
R06676  auraviketone lyase (decyclizing)
R06677  auramycinone:NADP+ 7-oxidoreductase
R06678   
R06679  12-deoxyaklanonic-acid:oxygen oxidoreductase
R06680  S-adenosyl-L-methionine:aklanonate O-methyltransferase
R06681  aklaviketone lyase (ring-opening)
R06682  aklavinone:NADP+ 7-oxidoreductase
R06683  aklavinone,NADPH:oxygen oxidoreductase (12-hydroxylating)
R06684  dTDP-beta-L-daunosamine:epsilon-rhodomycinone beta-L-daunosaminyltransferase
R06685   
R06686   
R06687  S-adenosyl-L-methionine:13-deoxycarminomycin 4-O-methyltransferase
R06688  13-deoxydaunorubicin,NADPH:oxygen oxidoreductase (13-hydroxylating)
R06689  13-dihydrodaunorubicin,NADPH:oxygen oxidoreductase (13-hydroxylating)
R06690  daunorubicin,NADPH:oxygen oxidoreductase (hydroxylating)
R06691  13-deoxycarminomycin,NADPH:oxygen oxidoreductase (13-hydroxylating)
R06692  13-dihydrocarminomycin,NADPH:oxygen oxidoreductase
R06693  S-adenosyl-L-methionine:carminomycin 4-O-methyltransferase
R06694   
R06695   
R06696   
R06698   
R06699  tetracenomycin-F2 hydro-lyase (tetracenomycin-F1-forming)
R06700  tetracenomycin-F1:oxygen C5-monooxygenase
R06701   
R06702   
R06703  S-adenosyl-L-methionine:tetracenomycin-E O-methyltransferase
R06704  tetracenomycin-A2,NADPH:oxygen oxidoreductase (tetracenomycin-C-forming)
R06706   
R06707   
R06709   
R06710   
R06711   
R06713  S-adenosyl-L-methionine:tetracenomycin-B3 O-methyltransferase
R06714   
R06715  S-adenosyl-L-methionine:4-demethylpremithramycinone O-methyltransferase
R06716  dTDP-D-olivose:premithramycinone D-olivosyltransferase
R06717  dTDP-D-oliose:premithramycin-A1 D-oliosyltransferase
R06718   
R06719  S-adenosyl-L-methionine:premithramycin-A3' C-methyltransferase
R09188   
R09189  S-adenosyl-L-methionine:pretetramid C-methyltransferase
R09190  6-methylpretetramide,NADPH:oxygen oxidoreductase (4,12a-hydroxylating)
R09191  S-adenosyl-L-methionine:4-amino-anhydrotetracycline N-methyltransferase
R09192  oxytetracycline:coenzyme-F420 oxidoreductase
R09196   
R09197   
R09198  5a,11a-dehydrotetracycline,NADPH:oxygen oxidoreductase (5-hydroxylating)
R09305   
R09306   
R09307   
R09308   
R09309   
R09310   
R09311   
R09312   
R09313  dihydrokalafungin-dihydroquinone,FMNH2:oxygen oxidoreductase (hydroxylating)
R09314   
R09325   
R09326   
R09327  deoxynogalonate:oxygen oxidoreductase
R09328  nogalaviketone lyase (ring-opening)
R09329  nogalavinone:NADP+ 7-oxidoreductase
R09330   
R09331  dTDP-beta-L-rhodosamine:aklavinone 7-alpha-L-rhodosaminyltransferase
R09332  dTDP-2-deoxy-beta-L-fucose:aclacinomycin-T 2-deoxy-alpha-L-fucosyltransferase
R09333   
R09334  aclacinomycin N:oxygen oxidoreductase
R09335  aclacinomycin A:oxygen oxidoreductase
R09336   
R09337  epsilon-rhodomycin-T acylhydrolase
R09338   
R09340   
R09341   
R09342   
R09343   
R09344   
R09345  dTDP-D-olivose:UWM6 9-C-beta-D-olivosyltransferase
R09346   
R09347   
R09348   
R09349   
R09350   
R09351  dTDP-D-olivose:premithramycin-A3 D-olivosyltransferase
R09352  dTDP-D-olivose:3A-deolivosylpremithramycin-B D-olivosyltransferase
R09353  premithramycin-B,NADPH:oxygen oxidoreductase
R09354   
R09355   
R09357   
R10545  aclacinomycin T acylhydrolase
R10954  tetracenomycin-B2,NADPH:oxygen oxidoreductase (8-demethyltetracenomycin-C-forming)
R10955  dTDP-beta-L-rhamnose:8-demethyltetracenomycin-C alpha-L-rhamnosyltransferase
R10956  S-adenosyl-L-methionine:8-demethyl-8-alpha-L-rhamnosyltetracenomycin-C 2'-O-methyltransferase
R10957  S-adenosyl-L-methionine:8-demethyl-8-(2-methoxy-alpha-L-rhamnosyl)tetracenomycin-C 3'-O-methyltransferase
R10958  S-adenosyl-L-methionine:8-demethyl-8-(2,3-di-O-methoxy-alpha-L-rhamnosyl)tetracenomycin-C 4'-O-methyltransferase
R10959  S-adenosyl-L-methionine:8-demethyl-8-(2,3,4-tri-O-methyl-alpha-L-rhamnosyl)tetracenomycin-C O-methyltransferase
R11478  tetracycline:FADH2 oxidoreductase (7-halogenating)
Compound
C00061  FMN
C01661  Doxorubicin
C01847  Reduced FMN
C01907  Daunorubicin
C02811  Anhydrotetracycline
C03206  5a,11a-Dehydrotetracycline
C06570  Tetracycline
C06571  Chlortetracycline
C06624  Oxytetracycline
C06627  4-Keto-anhydrotetracycline
C06628  4-Hydroxy-6-methylpretetramide
C06629  6-Methylpretetramide
C06654  4-Amino-anhydrotetracycline
C06691  Actinorhodin
C06799  Granaticin
C06801  Tetracenomycin C
C12366  Tetracenomycin F2
C12367  Tetracenomycin F1
C12368  Tetracenomycin D3
C12369  Tetracenomycin B3
C12370  Tetracenomycin E
C12371  Tetracenomycin A2
C12373  Tetracenomycin F1 methylester
C12374  Decarboxytetracenomycin F1
C12375  Tetracenomycin D3 methylester
C12376  Tetracenomycin D1
C12377  Tetracenomycin B1
C12378  Tetracenomycin B2
C12379  8-Demethyltetracenomycin C
C12380  Tetracenomycin X
C12381  Elloramycin A
C12382  4-Demethylpremithramycinone
C12383  Premithramycinone
C12384  Premithramycin A1
C12385  Premithramycin A2'
C12386  Premithramycin A3'
C12387  Premithramycin A3
C12388  Premithramycin B
C12389  Mithramycin
C12390  Dehydrorabelomycin
C12391  Kinobscurinone
C12392  Stealthin C
C12393  Prekinamycin
C12394  Kinamycin D
C12395  Jadomycin B
C12396  Tetrangomycin
C12397  Tetrangulol
C12398  8-O-Methyltetrangulol
C12399  19-Hydroxytetrangulol
C12400  19-Hydroxy-8-O-methyltetrangulol
C12401  PD116740
C12402  Rabelomycin
C12404  Urdamycinone B
C12405  100-1
C12406  Urdamycin B
C12407  104-2
C12408  100-2
C12409  124-1
C12410  Urdamycinone F
C12411  Urdamycin F
C12412  Aquayamycin
C12413  Urdamycin A
C12414  Urdamycin G
C12415  Methyl nogalonate
C12416  Nogalonate
C12417  Auraviketone
C12418  Dihydro-NAME
C12419  Auramycinone
C12420  12-Deoxyaklanonic acid
C12421  Aklanonate
C12422  Methyl aklanonate
C12423  Aklaviketone
C12424  Aklavinone
C12425  epsilon-Rhodomycinone
C12426  Rhodomycin D
C12427  10-Carboxy-13-deoxycarminomycin
C12428  13-Deoxycarminomycin
C12429  13-Deoxydaunorubicin
C12430  13-Dihydrodaunorubicin
C12431  13-Dihydrocarminomycin
C12432  Carminomycin
C12433  (13S)-13-Dihydrodaunorubicin
C12434  (S)-DNPA
C12435  6-Deoxydihydrokalafungin
C12436  Dihydrokalafungin
C12437  Medermycin
C12451  Fridamycin E
C18293  Nonaketamide monocyclic intermediate
C18294  Nonaketamide tricyclic intermediate
C18295  Pretetramid
C18296  5a,11a-Dehydrooxytetracycline
C18329  7,9,12-Octaketide intermediate 3
C18332  7,9,12-Decaketide intermediate 3
C18335  7,9,12-Decaketide intermediate 6
C18336  7,12-Decaketide intermediate 1
C18337  9,14-Decaketide intermediate 1
C18353  Octaketide bicyclic intermediate
C18354  (S)-Chiral alcohol
C18355  (R)-Chiral alcohol
C18356  (S)-Hemiketal
C18357  (R)-Hemiketal
C18358  DHKred-OH
C18359  Dihydrogranaticin
C18360  Dihydrokalafungin dihydroquinone form
C18629  Deoxynogalonate
C18630  Nogalaviketone
C18631  Nogalavinone
C18632  1-OH-Nogalamycinone
C18633  Nogalamycin
C18634  Aclacinomycin T
C18635  Aclacinomycin S
C18637  Aclacinomycin N
C18638  Aclacinomycin A
C18639  Aclacinomycin Y
C18640  epsilon-Rhodomycin T
C18641  15-Demethoxy-epsilon-rhodomycin
C18642  beta-Rhodomycin
C18678  UWM6
C18679  2,3-Dehydro-UWM6
C18680  Jadomycin A
C18681  C1'-C9-Glycosylated UWM6
C18682  11-Deoxylandomycinone
C18683  Landomycin H
C18684  Landomycin D
C18685  Landomycin E
C18709  Decaketide tricyclic intermediate
C18710  3A-Deolivosylpremithramycin B
C18711  Mithramycin DK
C18778  8-D-Olivosyl-landomycin
C18835  (R)-DNPA
C20689  15-Demethylaclacinomycin T
C20974  8-Demethyl-8-alpha-L-rhamnosyltetracenomycin C
C20975  8-Demethyl-8-(2-O-methyl-alpha-L-rhamnosyl)tetracenomycin C
C20976  8-Demethyl-8-(2,3-di-O-methyl-alpha-L-rhamnosyl)tetracenomycin C
C20977  8-Demethyl-8-(2,3,4-tri-O-methyl-alpha-L-rhamnosyl)tetracenomycin C
Reference
  Authors
Taguchi T, Okamoto S, Lezhava A, Li A, Ochi K, Ebizuka Y, Ichinose K
  Title
Possible involvement of ActVI-ORFA in transcriptional regulation of actVI tailoring-step genes for actinorhodin biosynthesis.
  Journal
FEMS Microbiol Lett 269:234-9 (2007)
DOI:10.1111/j.1574-6968.2007.00627.x
Reference
  Authors
Ichinose K, Ozawa M, Itou K, Kunieda K, Ebizuka Y
  Title
Cloning, sequencing and heterologous expression of the medermycin biosynthetic gene cluster of Streptomyces sp. AM-7161: towards comparative analysis of the benzoisochromanequinone gene clusters.
  Journal
Microbiology 149:1633-45 (2003)
DOI:10.1099/mic.0.26310-0
Reference
  Authors
Li A, Itoh T, Taguchi T, Xiang T, Ebizuka Y, Ichinose K
  Title
Functional studies on a ketoreductase gene from Streptomyces sp. AM-7161 to control the stereochemistry in medermycin biosynthesis.
  Journal
Bioorg Med Chem 13:6856-63 (2005)
DOI:10.1016/j.bmc.2005.07.060
Reference
PMID:9831526
  Authors
Ichinose K, Bedford DJ, Tornus D, Bechthold A, Bibb MJ, Revill WP, Floss HG, Hopwood DA
  Title
The granaticin biosynthetic gene cluster of Streptomyces violaceoruber Tu22: sequence analysis and expression in a heterologous host.
  Journal
Chem Biol 5:647-59 (1998)
DOI:10.1016/S1074-5521(98)90292-7
Reference
  Authors
Hopwood DA
  Title
Genetic Contributions to Understanding Polyketide Synthases.
  Journal
Chem Rev 97:2465-2498 (1997)
DOI:10.1021/cr960034i
Reference
PMID:7929165
  Authors
Fernandez-Moreno MA, Martinez E, Caballero JL, Ichinose K, Hopwood DA, Malpartida F
  Title
DNA sequence and functions of the actVI region of the actinorhodin biosynthetic gene cluster of Streptomyces coelicolor A3(2).
  Journal
J Biol Chem 269:24854-63 (1994)
Reference
  Authors
Itoh T, Taguchi T, Kimberley MR, Booker-Milburn KI, Stephenson GR, Ebizuka Y, Ichinose K
  Title
Actinorhodin biosynthesis: structural requirements for post-PKS tailoring intermediates revealed by functional analysis of ActVI-ORF1 reductase.
  Journal
Biochemistry 46:8181-8 (2007)
DOI:10.1021/bi700190p
Reference
  Authors
Ichinose K, Taguchi T, Bedford DJ, Ebizuka Y, Hopwood DA
  Title
Functional complementation of pyran ring formation in actinorhodin biosynthesis in Streptomyces coelicolor A3(2) by ketoreductase genes for granaticin biosynthesis.
  Journal
J Bacteriol 183:3247-50 (2001)
DOI:10.1128/JB.183.10.3247-3250.2001
Reference
  Authors
Taguchi T, Ebizuka Y, Hopwood DA, Ichinose K
  Title
A new mode of stereochemical control revealed by analysis of the biosynthesis of dihydrogranaticin in Streptomyces violaceoruber Tu22.
  Journal
J Am Chem Soc 123:11376-80 (2001)
DOI:10.1021/ja015981+
Reference
  Authors
Taguchi T, Kunieda K, Takeda-Shitaka M, Takaya D, Kawano N, Kimberley MR, Booker-Milburn KI, Stephenson GR, Umeyama H, Ebizuka Y, Ichinose K
  Title
Remarkably different structures and reaction mechanisms of ketoreductases for the opposite stereochemical control in the biosynthesis of BIQ antibiotics.
  Journal
Bioorg Med Chem 12:5917-27 (2004)
DOI:10.1016/j.bmc.2004.08.026
Reference
  Authors
Okamoto S, Taguchi T, Ochi K, Ichinose K
  Title
Biosynthesis of actinorhodin and related antibiotics: discovery of alternative routes for quinone formation encoded in the act gene cluster.
  Journal
Chem Biol 16:226-36 (2009)
DOI:10.1016/j.chembiol.2009.01.015
Reference
  Authors
Valton J, Mathevon C, Fontecave M, Niviere V, Ballou DP
  Title
Mechanism and regulation of the Two-component FMN-dependent monooxygenase ActVA-ActVB from Streptomyces coelicolor.
  Journal
J Biol Chem 283:10287-96 (2008)
DOI:10.1074/jbc.M709730200
Reference
  Authors
Valton J, Fontecave M, Douki T, Kendrew SG, Niviere V
  Title
An aromatic hydroxylation reaction catalyzed by a two-component FMN-dependent Monooxygenase. The ActVA-ActVB system from Streptomyces coelicolor.
  Journal
J Biol Chem 281:27-35 (2006)
DOI:10.1074/jbc.M506146200
Reference
  Authors
Valton J, Filisetti L, Fontecave M, Niviere V
  Title
A two-component flavin-dependent monooxygenase involved in actinorhodin biosynthesis in Streptomyces coelicolor.
  Journal
J Biol Chem 279:44362-9 (2004)
DOI:10.1074/jbc.M407722200
Reference
  Authors
Ellis HR
  Title
The FMN-dependent two-component monooxygenase systems.
  Journal
Arch Biochem Biophys 497:1-12 (2010)
DOI:10.1016/j.abb.2010.02.007
Reference
  Authors
Filisetti L, Fontecave M, Niviere V
  Title
Mechanism and substrate specificity of the flavin reductase ActVB from Streptomyces coelicolor.
  Journal
J Biol Chem 278:296-303 (2003)
DOI:10.1074/jbc.M209689200
Reference
PMID:9209048
  Authors
Kendrew SG, Hopwood DA, Marsh EN
  Title
Identification of a monooxygenase from Streptomyces coelicolor A3(2) involved in biosynthesis of actinorhodin: purification and characterization of the recombinant enzyme.
  Journal
J Bacteriol 179:4305-10 (1997)
DOI:10.1128/JB.179.13.4305-4310.1997
Reference
  Authors
Sciara G, Kendrew SG, Miele AE, Marsh NG, Federici L, Malatesta F, Schimperna G, Savino C, Vallone B
  Title
The structure of ActVA-Orf6, a novel type of monooxygenase involved in actinorhodin biosynthesis.
  Journal
EMBO J 22:205-15 (2003)
DOI:10.1093/emboj/cdg031
Reference
  Authors
Fetzner S, Steiner RA
  Title
Cofactor-independent oxidases and oxygenases.
  Journal
Appl Microbiol Biotechnol 86:791-804 (2010)
DOI:10.1007/s00253-010-2455-0
Reference
  Authors
Krohn K (ed).
  Title
Anthracycline Chemistry and Biology I : Biological Occurence and Biosynthesis, Synthesis and Chemistry
  Journal
Topics in Current Chemistry 282 (2008)
Reference
  Authors
Torkkell S, Kunnari T, Palmu K, Mantsala P, Hakala J, Ylihonko K
  Title
The entire nogalamycin biosynthetic gene cluster of Streptomyces nogalater: characterization of a 20-kb DNA region and generation of hybrid structures.
  Journal
Mol Genet Genomics 266:276-88 (2001)
DOI:10.1007/s004380100554
Reference
  Authors
Grocholski T, Koskiniemi H, Lindqvist Y, Mantsala P, Niemi J, Schneider G
  Title
Crystal structure of the cofactor-independent monooxygenase SnoaB from Streptomyces nogalater: implications for the reaction mechanism.
  Journal
Biochemistry 49:934-44 (2010)
DOI:10.1021/bi901985b
Reference
  Authors
Koskiniemi H, Grocholski T, Schneider G, Niemi J
  Title
Expression, purification and crystallization of the cofactor-independent monooxygenase SnoaB from the nogalamycin biosynthetic pathway.
  Journal
Acta Crystallogr Sect F Struct Biol Cryst Commun 65:256-9 (2009)
DOI:10.1107/S1744309109001389
Reference
  Authors
Chung JY, Fujii I, Harada S, Sankawa U, Ebizuka Y
  Title
Expression, purification, and characterization of AknX anthrone oxygenase, which is involved in aklavinone biosynthesis in Streptomyces galilaeus.
  Journal
J Bacteriol 184:6115-22 (2002)
DOI:10.1128/JB.184.22.6115-6122.2002
Reference
PMID:7836284
  Authors
Dickens ML, Ye J, Strohl WR
  Title
Analysis of clustered genes encoding both early and late steps in daunomycin biosynthesis by Streptomyces sp. strain C5.
  Journal
J Bacteriol 177:536-43 (1995)
DOI:10.1128/JB.177.3.536-543.1995
Reference
  Authors
Torkkell S, Kunnari T, Palmu K, Hakala J, Mantsala P, Ylihonko K
  Title
Identification of a cyclase gene dictating the C-9 stereochemistry of anthracyclines from Streptomyces nogalater.
  Journal
Antimicrob Agents Chemother 44:396-9 (2000)
DOI:10.1128/AAC.44.2.396-399.2000
Reference
  Authors
Sultana A, Kallio P, Jansson A, Wang JS, Niemi J, Mantsala P, Schneider G
  Title
Structure of the polyketide cyclase SnoaL reveals a novel mechanism for enzymatic aldol condensation.
  Journal
EMBO J 23:1911-21 (2004)
DOI:10.1038/sj.emboj.7600201
Reference
  Authors
Kallio P, Sultana A, Niemi J, Mantsala P, Schneider G
  Title
Crystal structure of the polyketide cyclase AknH with bound substrate and product analogue: implications for catalytic mechanism and product stereoselectivity.
  Journal
J Mol Biol 357:210-20 (2006)
DOI:10.1016/j.jmb.2005.12.064
Reference
PMID:8655529
  Authors
Dickens ML, Ye J, Strohl WR
  Title
Cloning, sequencing, and analysis of aklaviketone reductase from Streptomyces sp. strain C5.
  Journal
J Bacteriol 178:3384-8 (1996)
DOI:10.1128/JB.178.11.3384-3388.1996
Reference
  Authors
Leimkuhler C, Fridman M, Lupoli T, Walker S, Walsh CT, Kahne D
  Title
Characterization of rhodosaminyl transfer by the AknS/AknT glycosylation complex and its use in reconstituting the biosynthetic pathway of aclacinomycin A.
  Journal
J Am Chem Soc 129:10546-50 (2007)
DOI:10.1021/ja072909o
Reference
  Authors
Lu W, Leimkuhler C, Gatto GJ Jr, Kruger RG, Oberthur M, Kahne D, Walsh CT
  Title
AknT is an activating protein for the glycosyltransferase AknS in L-aminodeoxysugar transfer to the aglycone of aclacinomycin A.
  Journal
Chem Biol 12:527-34 (2005)
DOI:10.1016/j.chembiol.2005.02.016
Reference
  Authors
Lu W, Leimkuhler C, Oberthur M, Kahne D, Walsh CT
  Title
AknK is an L-2-deoxyfucosyltransferase in the biosynthesis of the anthracycline aclacinomycin A.
  Journal
Biochemistry 43:4548-58 (2004)
DOI:10.1021/bi035945i
Reference
  Authors
Alexeev I, Sultana A, Mantsala P, Niemi J, Schneider G
  Title
Aclacinomycin oxidoreductase (AknOx) from the biosynthetic pathway of the antibiotic aclacinomycin is an unusual flavoenzyme with a dual active site.
  Journal
Proc Natl Acad Sci U S A 104:6170-5 (2007)
DOI:10.1073/pnas.0700579104
Reference
  Authors
Lindqvist Y, Koskiniemi H, Jansson A, Sandalova T, Schnell R, Liu Z, Mantsala P, Niemi J, Schneider G
  Title
Structural basis for substrate recognition and specificity in aklavinone-11-hydroxylase from rhodomycin biosynthesis.
  Journal
J Mol Biol 393:966-77 (2009)
DOI:10.1016/j.jmb.2009.09.003
Reference
  Authors
Malla S, Niraula NP, Singh B, Liou K, Sohng JK
  Title
Limitations in doxorubicin production from Streptomyces peucetius.
  Journal
Microbiol Res 165:427-35 (2010)
DOI:10.1016/j.micres.2009.11.006
Reference
PMID:7592454
  Authors
Otten SL, Liu X, Ferguson J, Hutchinson CR
  Title
Cloning and characterization of the Streptomyces peucetius dnrQS genes encoding a daunosamine biosynthesis enzyme and a glycosyl transferase involved in daunorubicin biosynthesis.
  Journal
J Bacteriol 177:6688-92 (1995)
DOI:10.1128/JB.177.22.6688-6692.1995
Reference
  Authors
Malla S, Niraula NP, Liou K, Sohng JK
  Title
Enhancement of doxorubicin production by expression of structural sugar biosynthesis and glycosyltransferase genes in Streptomyces peucetius.
  Journal
J Biosci Bioeng 108:92-8 (2009)
DOI:10.1016/j.jbiosc.2009.03.002
Reference
PMID:9098063
  Authors
Dickens ML, Priestley ND, Strohl WR
  Title
In vivo and in vitro bioconversion of epsilon-rhodomycinone glycoside to doxorubicin: functions of DauP, DauK, and DoxA.
  Journal
J Bacteriol 179:2641-50 (1997)
DOI:10.1128/JB.179.8.2641-2650.1997
Reference
PMID:9864344
  Authors
Lomovskaya N, Otten SL, Doi-Katayama Y, Fonstein L, Liu XC, Takatsu T, Inventi-Solari A, Filippini S, Torti F, Colombo AL, Hutchinson CR
  Title
Doxorubicin overproduction in Streptomyces peucetius: cloning and characterization of the dnrU ketoreductase and dnrV genes and the doxA cytochrome P-450 hydroxylase gene.
  Journal
J Bacteriol 181:305-18 (1999)
DOI:10.1128/JB.181.1.305-318.1999
Reference
  Authors
Jansson A, Koskiniemi H, Erola A, Wang J, Mantsala P, Schneider G, Niemi J
  Title
Aclacinomycin 10-hydroxylase is a novel substrate-assisted hydroxylase requiring S-adenosyl-L-methionine as cofactor.
  Journal
J Biol Chem 280:3636-44 (2005)
DOI:10.1074/jbc.M412095200
Reference
  Authors
Wohlert SE, Wendt-Pienkowski E, Bao W, Hutchinson CR
  Title
Production of aromatic minimal polyketides by the daunorubicin polyketide synthase genes reveals the incompatibility of the heterologous DpsY and JadI cyclases.
  Journal
J Nat Prod 64:1077-80 (2001)
DOI:10.1021/np010067f
Reference
  Authors
Zhou H, Li Y, Tang Y
  Title
Cyclization of aromatic polyketides from bacteria and fungi.
  Journal
Nat Prod Rep 27:839-68 (2010)
DOI:10.1039/b911518h
Reference
  Authors
Hertweck C, Luzhetskyy A, Rebets Y, Bechthold A
  Title
Type II polyketide synthases: gaining a deeper insight into enzymatic teamwork.
  Journal
Nat Prod Rep 24:162-90 (2007)
DOI:10.1039/b507395m
Reference
  Authors
Chen Y, Fan K, He Y, Xu X, Peng Y, Yu T, Jia C, Yang K
  Title
Characterization of JadH as an FAD- and NAD(P)H-dependent bifunctional hydroxylase/dehydrase in jadomycin biosynthesis.
  Journal
Chembiochem 11:1055-60 (2010)
DOI:10.1002/cbic.201000178
Reference
  Authors
Rix U, Wang C, Chen Y, Lipata FM, Remsing Rix LL, Greenwell LM, Vining LC, Yang K, Rohr J
  Title
The oxidative ring cleavage in jadomycin biosynthesis: a multistep oxygenation cascade in a biosynthetic black box.
  Journal
Chembiochem 6:838-45 (2005)
DOI:10.1002/cbic.200400395
Reference
  Authors
Chen YH, Wang CC, Greenwell L, Rix U, Hoffmeister D, Vining LC, Rohr J, Yang KQ
  Title
Functional analyses of oxygenases in jadomycin biosynthesis and identification of JadH as a bifunctional oxygenase/dehydrase.
  Journal
J Biol Chem 280:22508-14 (2005)
DOI:10.1074/jbc.M414229200
Reference
  Authors
Borissow CN, Graham CL, Syvitski RT, Reid TR, Blay J, Jakeman DL
  Title
Stereochemical integrity of oxazolone ring-containing jadomycins.
  Journal
Chembiochem 8:1198-203 (2007)
DOI:10.1002/cbic.200700204
Reference
  Authors
Mittler M, Bechthold A, Schulz GE
  Title
Structure and action of the C-C bond-forming glycosyltransferase UrdGT2 involved in the biosynthesis of the antibiotic urdamycin.
  Journal
J Mol Biol 372:67-76 (2007)
DOI:10.1016/j.jmb.2007.06.005
Reference
  Authors
Trefzer A, Hoffmeister D, Kunzel E, Stockert S, Weitnauer G, Westrich L, Rix U, Fuchser J, Bindseil KU, Rohr J, Bechthold A
  Title
Function of glycosyltransferase genes involved in urdamycin A biosynthesis.
  Journal
Chem Biol 7:133-42 (2000)
DOI:10.1016/S1074-5521(00)00079-X
Reference
  Authors
Hoffmeister D, Ichinose K, Bechthold A
  Title
Two sequence elements of glycosyltransferases involved in urdamycin biosynthesis are responsible for substrate specificity and enzymatic activity.
  Journal
Chem Biol 8:557-67 (2001)
DOI:10.1016/S1074-5521(01)00039-4
Reference
  Authors
Rohr J, Schonewolf M, Udvarnoki G, Eckardt K, Schumann G, Wagner C, Beale JM, Sorey SD.
  Title
Investigations on the biosynthesis of the angucycline group antibiotics aquayamycin and the urdamycins A and B. Results from the structural analysis of novel blocked mutant products.
  Journal
J Org Chem 58:2547-51 (1993)
DOI:10.1021/jo00061a032
Reference
  Authors
Zhu L, Ostash B, Rix U, Nur-E-Alam M, Mayers A, Luzhetskyy A, Mendez C, Salas JA, Bechthold A, Fedorenko V, Rohr J
  Title
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.
  Journal
J Org Chem 70:631-8 (2005)
DOI:10.1021/jo0483623
Reference
  Authors
Baig I, Kharel M, Kobylyanskyy A, Zhu L, Rebets Y, Ostash B, Luzhetskyy A, Bechthold A, Fedorenko VA, Rohr J
  Title
On the acceptor substrate of C-glycosyltransferase UrdGT2: three prejadomycin C-Glycosides from an engineered mutant of Streptomyces globisporus 1912 DeltalndE(urdGT2).
  Journal
Angew Chem Int Ed Engl 45:7842-6 (2006)
DOI:10.1002/anie.200603176
Reference
  Authors
Ostash B, Rix U, Rix LL, Liu T, Lombo F, Luzhetskyy A, Gromyko O, Wang C, Brana AF, Mendez C, Salas JA, Fedorenko V, Rohr J
  Title
Generation of new landomycins by combinatorial biosynthetic manipulation of the LndGT4 gene of the landomycin E cluster in S. globisporus.
  Journal
Chem Biol 11:547-55 (2004)
DOI:10.1016/j.chembiol.2004.03.011
Reference
  Authors
Lombo F, Menendez N, Salas JA, Mendez C
  Title
The aureolic acid family of antitumor compounds: structure, mode of action, biosynthesis, and novel derivatives.
  Journal
Appl Microbiol Biotechnol 73:1-14 (2006)
DOI:10.1007/s00253-006-0511-6
Reference
  Authors
Trefzer A, Blanco G, Remsing L, Kunzel E, Rix U, Lipata F, Brana AF, Mendez C, Rohr J, Bechthold A, Salas JA
  Title
Rationally designed glycosylated premithramycins: hybrid aromatic polyketides using genes from three different biosynthetic pathways.
  Journal
J Am Chem Soc 124:6056-62 (2002)
DOI:10.1021/ja017385l
Reference
  Authors
Lozano MJ, Remsing LL, Quiros LM, Brana AF, Fernandez E, Sanchez C, Mendez C, Rohr J, Salas JA
  Title
Characterization of two polyketide methyltransferases involved in the biosynthesis of the antitumor drug mithramycin by Streptomyces argillaceus.
  Journal
J Biol Chem 275:3065-74 (2000)
DOI:10.1074/jbc.275.5.3065
Reference
  Authors
Blanco G, Fernandez E, Fernandez MJ, Brana AF, Weissbach U, Kunzel E, Rohr J, Mendez C, Salas JA
  Title
Characterization of two glycosyltransferases involved in early glycosylation steps during biosynthesis of the antitumor polyketide mithramycin by Streptomyces argillaceus.
  Journal
Mol Gen Genet 262:991-1000 (2000)
DOI:10.1007/PL00008667
Reference
  Authors
Nur-e-Alam M, Mendez C, Salas JA, Rohr J
  Title
Elucidation of the glycosylation sequence of mithramycin biosynthesis: isolation of 3A-deolivosylpremithramycin B and its conversion to premithramycin B by glycosyltransferase MtmGII.
  Journal
Chembiochem 6:632-6 (2005)
DOI:10.1002/cbic.200400309
Reference
PMID:9733697
  Authors
Fernandez E, Weissbach U, Sanchez Reillo C, Brana AF, Mendez C, Rohr J, Salas JA
  Title
Identification of two genes from Streptomyces argillaceus encoding glycosyltransferases involved in transfer of a disaccharide during biosynthesis of the antitumor drug mithramycin.
  Journal
J Bacteriol 180:4929-37 (1998)
DOI:10.1128/JB.180.18.4929-4937.1998
Reference
  Authors
Beam MP, Bosserman MA, Noinaj N, Wehenkel M, Rohr J
  Title
Crystal structure of Baeyer-Villiger monooxygenase MtmOIV, the key enzyme of the mithramycin biosynthetic pathway .
  Journal
Biochemistry 48:4476-87 (2009)
DOI:10.1021/bi8023509
Reference
  Authors
Wang C, Gibson M, Rohr J, Oliveira MA
  Title
Crystallization and X-ray diffraction properties of Baeyer-Villiger monooxygenase MtmOIV from the mithramycin biosynthetic pathway in Streptomyces argillaceus.
  Journal
Acta Crystallogr Sect F Struct Biol Cryst Commun 61:1023-6 (2005)
DOI:10.1107/S1744309105033221
Reference
  Authors
Rodriguez D, Quiros LM, Brana AF, Salas JA
  Title
Purification and characterization of a monooxygenase involved in the biosynthetic pathway of the antitumor drug mithramycin.
  Journal
J Bacteriol 185:3962-5 (2003)
DOI:10.1128/JB.185.13.3962-3965.2003
Reference
  Authors
Hutchinson CR
  Title
Biosynthetic Studies of Daunorubicin and Tetracenomycin C.
  Journal
Chem Rev 97:2525-2536 (1997)
DOI:10.1021/cr960022x
Reference
PMID:8244926
  Authors
Summers RG, Wendt-Pienkowski E, Motamedi H, Hutchinson CR
  Title
The tcmVI region of the tetracenomycin C biosynthetic gene cluster of Streptomyces glaucescens encodes the tetracenomycin F1 monooxygenase, tetracenomycin F2 cyclase, and, most likely, a second cyclase.
  Journal
J Bacteriol 175:7571-80 (1993)
DOI:10.1128/JB.175.23.7571-7580.1993
Reference
PMID:8218177
  Authors
Shen B, Hutchinson CR
  Title
Tetracenomycin F2 cyclase: intramolecular aldol condensation in the biosynthesis of tetracenomycin C in Streptomyces glaucescens.
  Journal
Biochemistry 32:11149-54 (1993)
DOI:10.1021/bi00092a026
Reference
PMID:8329392
  Authors
Shen B, Hutchinson CR
  Title
Tetracenomycin F1 monooxygenase: oxidation of a naphthacenone to a naphthacenequinone in the biosynthesis of tetracenomycin C in Streptomyces glaucescens.
  Journal
Biochemistry 32:6656-63 (1993)
DOI:10.1021/bi00077a019
Reference
PMID:1548230
  Authors
Summers RG, Wendt-Pienkowski E, Motamedi H, Hutchinson CR
  Title
Nucleotide sequence of the tcmII-tcmIV region of the tetracenomycin C biosynthetic gene cluster of Streptomyces glaucescens and evidence that the tcmN gene encodes a multifunctional cyclase-dehydratase-O-methyl transferase.
  Journal
J Bacteriol 174:1810-20 (1992)
DOI:10.1128/JB.174.6.1810-1820.1992
Reference
  Authors
Ames BD, Korman TP, Zhang W, Smith P, Vu T, Tang Y, Tsai SC
  Title
Crystal structure and functional analysis of tetracenomycin ARO/CYC: implications for cyclization specificity of aromatic polyketides.
  Journal
Proc Natl Acad Sci U S A 105:5349-54 (2008)
DOI:10.1073/pnas.0709223105
Reference
  Authors
Rafanan ER Jr, Hutchinson CR, Shen B
  Title
Triple hydroxylation of tetracenomycin A2 to tetracenomycin C involving two molecules of O(2) and one molecule of H(2)O.
  Journal
Org Lett 2:3225-7 (2000)
DOI:10.1021/ol0002267
Reference
  Authors
Ramos A, Lombo F, Brana AF, Rohr J, Mendez C, Salas JA
  Title
Biosynthesis of elloramycin in Streptomyces olivaceus requires glycosylation by enzymes encoded outside the aglycon cluster.
  Journal
Microbiology 154:781-8 (2008)
DOI:10.1099/mic.0.2007/014035-0
Reference
  Authors
Patallo EP, Blanco G, Fischer C, Brana AF, Rohr J, Mendez C, Salas JA
  Title
Deoxysugar methylation during biosynthesis of the antitumor polyketide elloramycin by Streptomyces olivaceus. Characterization of three methyltransferase genes.
  Journal
J Biol Chem 276:18765-74 (2001)
DOI:10.1074/jbc.M101225200
Related
pathway
rn00253  Tetracycline biosynthesis
rn01056  Biosynthesis of type II polyketide backbone
KO pathway
ko01057   

DBGET integrated database retrieval system