Show legend Show as text

Structure type: monomer
Trivial name: DIBOA glucoside
Compound class: glycoside
Contained glycoepitopes: IEDB_142488,IEDB_146664,IEDB_983931,SB_192

• Article ID: 12049
  Cambier V, Hance T, de Hoffmann E "Variation of DIMBOA and related compounds content in relation to the age and plant organ in maize" - Phytochemistry 53(2) (2000) 223-229
  

  We report the variation of all 1,4-benzoxazin-3-one derivatives content detectable in maize with plant age in roots and aerial parts. Our results show that the concentration of hydroxamic acids, 2,4-dihydroxy-7-methoxy-1,4-benzoxazin-3-one glucoside (DIMBOA-Glc) and its 8-methoxylated analogue (DIM2BOA-Glc) is high after seed germination and then decreases with plant age. Nevertheless, these compounds continue to be biosynthesised during 6-10 days after germination. Variation in concentration of N-O-methylated DIMBOA-Glc (HDMBOA-Glc) is similar to the one of hydroxamic acids in aerial parts. On the contrary, in roots, its concentration remains relatively stable with plant age. After 10 days, HDMBOA-Glc becomes the main compound in roots. This compound is also present in higher concentration than hydroxamic acids in the oldest leaf of 20-day-old maize. The presence of four other DIMBOA related compounds in maize plants depends on variety, age and tissue. The role of these compounds in plant resistance to aphids is discussed.

  1, maize, hydroxamic acids, Poaceae, DIMBOA, 4-benzoxazin-3-one, plant resistance

  NCBI PubMed ID: 10680175
  Publication DOI: 10.1016/s0031-9422(99)00498-7
  Journal NLM ID: 0151434
  Publisher: Elsevier
  Correspondence: cambier@cico.ucl.ac.be
  Institutions: Unité d'Ecologie et de Biogéographie, Louvain-la-Neuve, Belgium, Unité de Spectrométrie de masse, Louvain-la-Neuve, Belgium
  Methods: UV, extraction, evaporation, centrifugation, HPLC-APCI-MS
  
   
  
  Zea mays
  CSDB ID 64988 (all data & tools)
• Article ID: 12692
  Sicker D, Frey M, Schulz M, Gierl A "Role of natural benzoxazinones in the survival strategy of plants" - International Review of Cytology 198 (2000) 319-346
  

  Benzoxazinoid acetal glucosides are a unique class of natural products abundant in Gramineae, including the major agricultural crops maize, wheat, and rye. These secondary metabolites are also found in several dicotyledonous species. Benzoxazinoids serve as important factors of host plant resistance against microbial diseases and insects and as allelochemicals and endogenous ligands. Interdisciplinary investigations by biologists, biochemists, and chemists are stimulated by the intention to make agricultural use of the benzoxazinones as natural pesticides. These natural products are not only constituents of a plant defense system but also part of an active allelochemical system used in the competition with other plants. This review covers biological and chemical aspects of benzoxazinone research over the last decade with special emphasis on recent advances in the elucidation of the biosynthetic pathway.

  biosynthesis, allelopathy, benzoxazinones, cyclic hydroxamic acids, acetal glucosides, defence

  NCBI PubMed ID: 10804466
  Publication DOI: 10.1016/s0074-7696(00)98008-2
  Journal NLM ID: 2985180R
  Institutions: Institute of Organic Chemistry, University of Leipzig, Leipzig, Germany, Institut für Genetik, Technische Universität München, Garching, Germany, Institute of Agricultural Botany, University of Bonn, Bonn, Germany
  
   
  
  Secale cereale, Triticum aestivum, Zea mays, Hordeum vulgare, Agropyron repens, Acanthus mollis, Aphelandra tetragona, Consolida orientalis
  CSDB ID 67915 (all data & tools)
• Article ID: 12725
  Sue M, Ishihara A, Iwamura H "Purification and characterization of a β-glucosidase from rye (Secale cereale L.) seedlings" - Plant Science 155(1) (2000) 67-74
  

  Cyclic hydroxamic acids and a glucosidase that occur in rye seedlings were investigated. The concentration of the glucoside of 2,4-dihydroxy-1,4-benzoxazin-3-one (DIBOA-Glc) in shoots increased soon after germination and decreased to a lower, constant level as the plants started autotrophic growth. Cyclic hydroxamic acid glucoside β-glucosidase activity also occurred transiently, and the timing of the increase and decrease was concurrent with that of cyclic hydroxamic acid glucosides. The glucosidase was isolated from 48-h-old rye shoots and purified to apparent homogeneity by using isoelectric precipitation, anion exchange chromatography, and gel filtration. The isoelectric point and the optimum reaction temperature were 4.9–5.1 and 25–30°C, respectively. The N-terminal amino acid sequence was almost identical to that of the wheat glucosidases, but did not show any similarity to the sequences of other glucosidases of plant origin. SDS– and native–PAGE analyses showed that rye had several isozymes of glucosidase, and each isozyme was an oligomer of 60-kDa monomers with a molecular mass of ~300 kDa. The enzyme was highly active not only for DIMBOA-Glc but also for its 7-demethoxy analogue, DIBOA-Glc, which was different from the specificities of maize and wheat glucosidases.

  cyclic hydroxamic acid; β-glucosidase; rye (Secale)

  NCBI PubMed ID: 10773341
  Publication DOI: 10.1016/s0168-9452(00)00204-1
  Publisher: Elsevier
  Correspondence: sue@kais.kyoto-u.ac.jp
  Institutions: Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Kyoto, Japan
  Methods: SDS-PAGE, electrophoresis, HPLC, enzymatic digestion, extraction, enzymatic assay
  
   
  
  Secale cereale cv. haru-ichiban
  CSDB ID 68049 (all data & tools)
• Article ID: 12726
  Sue M, Ishihara A, Iwamura H "Occurrence and characterization of a UDP-glucose:hydroxamic acid glucosyltransferase isolated from wheat (Triticum aestivum) seedlings" - Zeitschrift für Naturforschung. C, Journal of Biosciences 55(9-10) (2000) 701-707
  

  Cyclic hydroxamic acid glucosides are present at high concentrations immediately after germination in wheat (Triticum aestivum L.). Changes in the activity of UDP-Glucose:cyclic hydroxamic acid glucosyltransferase (EC 2.4.1.-) in wheat were investigated using the cyclic hydroxamic acids 2.4-dihydroxy-1,4-benzoxazin-3-one (DIBOA) and its 7-methoxy derivative (DIMBOA) as sugar acceptors. Glucosyltransferase activity on both substrates was detected in dry seeds, with activity increasing after imbibition, peaking in shoots and roots 36-48 hours after imbibition and decreasing thereafter. The transience of glucosyltransferase activity was concurrent with the transient occurrence of the hydroxamic acid glucosides [Nakagawa E., Amano T., Hirai N., and Iwamura H. (1995) Phytochemistry 38, 1349-1354], suggesting that glucosyltransferases regulate the accumulation of hydroxamic acid glucosides in wheat seedlings. Two peaks in activity of UDP-Glucose:DIMBOA glucosyltransferase were detected using a Mono Q column, indicating the presence of at least two isozymes of this glucosyltransferase. The enzyme in the major peak was purified about 1500-fold and shown to be in a monomeric form with a molecular mass of 47 or 49 kDa. The enzyme reacted strongly with DIMBOA, less so with DIBOA. The enzyme of the minor peak on the Mono Q chromatogram, which was also a monomeric enzyme with a molecular mass of 47 kDa, showed similar substrate specificity to that of the major peak enzyme.

  glucosyltransferase, hydroxamic acid, Triticum aestivum

  NCBI PubMed ID: 11098819
  Publication DOI: 10.1515/znc-2000-9-1006
  Journal NLM ID: 8912155
  Publisher: Verlag der Zeitschrift für Naturforschung
  Correspondence: sue@kais.kyoto-u.ac.jp
  Institutions: Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Kyoto, Japan, CREST, Japan Science and Technology Corporation
  Methods: SDS-PAGE, electrophoresis, HPLC, enzymatic digestion, extraction, enzymatic assay
  
   
  
  Triticum aestivum
  CSDB ID 68051 (all data & tools)

Show legend Show as text

Structure type: monomer
Trivial name: DIMBOA glucoside
Compound class: glycoside
Contained glycoepitopes: IEDB_142488,IEDB_146664,IEDB_983931,SB_192

• Article ID: 12049
  Cambier V, Hance T, de Hoffmann E "Variation of DIMBOA and related compounds content in relation to the age and plant organ in maize" - Phytochemistry 53(2) (2000) 223-229
  

  We report the variation of all 1,4-benzoxazin-3-one derivatives content detectable in maize with plant age in roots and aerial parts. Our results show that the concentration of hydroxamic acids, 2,4-dihydroxy-7-methoxy-1,4-benzoxazin-3-one glucoside (DIMBOA-Glc) and its 8-methoxylated analogue (DIM2BOA-Glc) is high after seed germination and then decreases with plant age. Nevertheless, these compounds continue to be biosynthesised during 6-10 days after germination. Variation in concentration of N-O-methylated DIMBOA-Glc (HDMBOA-Glc) is similar to the one of hydroxamic acids in aerial parts. On the contrary, in roots, its concentration remains relatively stable with plant age. After 10 days, HDMBOA-Glc becomes the main compound in roots. This compound is also present in higher concentration than hydroxamic acids in the oldest leaf of 20-day-old maize. The presence of four other DIMBOA related compounds in maize plants depends on variety, age and tissue. The role of these compounds in plant resistance to aphids is discussed.

  1, maize, hydroxamic acids, Poaceae, DIMBOA, 4-benzoxazin-3-one, plant resistance

  NCBI PubMed ID: 10680175
  Publication DOI: 10.1016/s0031-9422(99)00498-7
  Journal NLM ID: 0151434
  Publisher: Elsevier
  Correspondence: cambier@cico.ucl.ac.be
  Institutions: Unité d'Ecologie et de Biogéographie, Louvain-la-Neuve, Belgium, Unité de Spectrométrie de masse, Louvain-la-Neuve, Belgium
  Methods: UV, extraction, evaporation, centrifugation, HPLC-APCI-MS
  
   
  
  Zea mays
  CSDB ID 64989 (all data & tools)
• Article ID: 12093
  Cicek M, Blanchard D, Bevan DR, Esen A "The aglycone specificity-determining sites are different in 2,4-dihydroxy-7-methoxy-1,4-benzoxazin-3-one (DIMBOA)-glucosidase (maize β-glucosidase) and dhurrinase (sorghum β-glucosidase)" - Journal of Biological Chemistry 275(26) (2000) 20002-20011
  

  The maize β-glucosidase isozyme Glu1 hydrolyzes a broad spectrum of substrates in addition to its natural substrate DIMBOAGlc (2-O-β-D-glucopyranosyl-4-hydroxy-7-methoxy-1,4-benzoxazin-3-one), whereas the sorghum β-glucosidase isozyme Dhr1 hydrolyzes exclusively its natural substrate dhurrin (p-hydroxy-(S)-mandelonitrile-β-D-glucose). To study the mechanism of substrate specificity further, eight chimeric β-glucosidases were constructed by replacing peptide sequences within the C-terminal region of Glu1 with the homologous peptide sequences of Dhr1 or vice versa, where the two enzymes differ by 4 to 22 amino acid substitutions, depending on the length of the swapped regions. Five Glu1/Dhr1 chimeras hydrolyzed substrates that are hydrolyzed by both parental enzymes, including dhurrin, which is not hydrolyzed by Glu1. In contrast, three Dhr1/Glu1 chimeras hydrolyzed only dhurrin but with lower catalytic efficiency than Dhr1. Additional domain-swapping within the C-terminal domain of Glu1 showed that replacing the peptide (466)FAGFTERY(473) of Glu1 with the homologous peptide (462)SSGYTERF(469) of Dhr1 or replacing the peptide (481)NNNCTRYMKE(490) in Glu1 with the homologous peptide (477)ENGCERTMKR(486) of Dhr1 was sufficient to confer to Glu1 the ability to hydrolyze dhurrin. Data from various reciprocal chimeras, sequence comparisons, and homology modeling suggest that the Dhr1-specific Ser-462-Ser-463 and Phe-469 play a key role in dhurrin hydrolysis. Similar data suggest that DIMBOAGlc hydrolysis determinants are not located within the extreme 47-amino acid-long C-terminal domain of Glu1.

  glucoside, β-glucosidases, sorghum, maize, DIMBOA

  NCBI PubMed ID: 10748038
  Publication DOI: 10.1074/jbc.M001609200
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: Esen A
  Institutions: Department of Biology, Virginia Polytechnic Institute and State University, Blacksburg, USA, Department of Biochemistry, Virginia Polytechnic Institute and State University, Blacksburg, USA
  Methods: PCR, SDS-PAGE, DNA techniques, inhibition studies, TLC, extraction, CC, enzymatic assay, precipitation, centrifugation, DNA expression
  
   
  
  Zea mays, Sorghum bicolor
  CSDB ID 65162 (all data & tools)
• Article ID: 12336
  Larsen E, Christensen LP "Simple method for large scale isolation of the cyclic arylhydroxamic acid DIMBOA from maize (Zea mays L.)" - Journal of Agricultural and Food Chemistry 48(6) (2000) 2556-2558
  

  The 2-β-O-D-glucoside of the cyclic arylhydroxamic acid 2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one (DIMBOA) that occurs in large amounts in young maize shoots (Zea mays L.) is converted enzymatically to its aglycone upon tissue damage. The aglycone DIMBOA possesses strong biologically activity toward various organisms whereas the glucoside is almost biologically inactive. A simple procedure yielding DIMBOA in gram quantities, from 7-day-old maize seedlings, was developed by using solid-phase extraction.

  isolation, Zea mays, Gramineae, maize, DIMBOA, solid-phase extraction, Amberlite XAD-7

  NCBI PubMed ID: 10888583
  Publication DOI: 10.1021/jf0000934
  Journal NLM ID: 0374755
  Publisher: American Chemical Society
  Correspondence: larsp.christensen@agrsci.dk
  Institutions: Department of Fruit, Vegetable and Food Science, Danish Institute of Agricultural Sciences, Aarslev, Denmark
  
   
  
  Zea mays
  CSDB ID 66209 (all data & tools)
• Article ID: 12692
  Sicker D, Frey M, Schulz M, Gierl A "Role of natural benzoxazinones in the survival strategy of plants" - International Review of Cytology 198 (2000) 319-346
  

  Benzoxazinoid acetal glucosides are a unique class of natural products abundant in Gramineae, including the major agricultural crops maize, wheat, and rye. These secondary metabolites are also found in several dicotyledonous species. Benzoxazinoids serve as important factors of host plant resistance against microbial diseases and insects and as allelochemicals and endogenous ligands. Interdisciplinary investigations by biologists, biochemists, and chemists are stimulated by the intention to make agricultural use of the benzoxazinones as natural pesticides. These natural products are not only constituents of a plant defense system but also part of an active allelochemical system used in the competition with other plants. This review covers biological and chemical aspects of benzoxazinone research over the last decade with special emphasis on recent advances in the elucidation of the biosynthetic pathway.

  biosynthesis, allelopathy, benzoxazinones, cyclic hydroxamic acids, acetal glucosides, defence

  NCBI PubMed ID: 10804466
  Publication DOI: 10.1016/s0074-7696(00)98008-2
  Journal NLM ID: 2985180R
  Institutions: Institute of Organic Chemistry, University of Leipzig, Leipzig, Germany, Institut für Genetik, Technische Universität München, Garching, Germany, Institute of Agricultural Botany, University of Bonn, Bonn, Germany
  
   
  
  Triticum aestivum, Zea mays, Agropyron repens, Aphelandra tetragona, Aphelandra squarrosa
  CSDB ID 67916 (all data & tools)
• Article ID: 12724
  Sue M, Ishihara A, Iwamura H "Purification and characterization of a hydroxamic acid glucoside β-glucosidase from wheat (Triticum aestivum L.) seedlings" - Planta 210(3) (2000) 432-438
  

  A β-glucosidase (EC 3.2.1.21) with a high affinity for cyclic hydroxamic acid β-D-glucosides was purified from 48-h-old wheat (Triticum aestivum L.) seedlings. The activity occurred transiently at a high level during the non-autotrophic stage of growth, and the nature of the transient occurrence was correlated with that of 2,4-dihydroxy-7-methoxy-1,4-benzoxazin-3-one glucoside (DIMBOA-Glc). The glucosidase had maximum activity at an acidic pH (pH 5.5) and the purified enzyme showed a high affinity for DIMBOA-Glc, V max and K m being 4100 nkat/mg protein and 0.27 mM, respectively. It also hydrolyzed p-nitrophenol β-glycosides, as well as flavone and isoflavone glucosides, but to a lesser extent. The results indicated that the primary natural substrate for the glucosidase is DIMBOA-Glc and that the enzyme is involved in defense against pathogens and herbivores in non-autotrophic wheat. The glucosidase was found to be present as oligomeric forms with a molecular mass of 260–300 kDa comprising 60- and 58-kDa monomers. The N-terminal 12-amino-acid sequences of the two monomers were identical (Gly-Thr-Pro-(Ser?)-Lys-Pro-Ala-Glu-Pro-Ile-Gly-Pro), and showed no similarity to those of other plant glucosidases. Polyacrylamide gel electrophoresis under nondenaturing condition indicated the existence of at least eight isozymes. Three cultivars of Triticum aestivum had the same zone of glucosidase activity on zymograms, but the activity zones of the Triticum species, T. aestivum L., T. spelta L. and T. turgidum L., had different mobilities.

  β-glucosidase, cyclic hydroxamic acid, isozymes, Triticum (β-glucosidase)

  NCBI PubMed ID: 10750901
  Publication DOI: 10.1007/s004250050029
  Journal NLM ID: 1250576
  Publisher: Berlin, New York, Springer
  Correspondence: sue@kais.kyoto-u.ac.jp
  Institutions: Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Kyoto, Japan, CREST, Japan Science and Technology Corporation
  Methods: SDS-PAGE, electrophoresis, HPLC, enzymatic digestion, extraction, enzymatic assay
  
   
  
  Triticum aestivum
  CSDB ID 68048 (all data & tools)
• Article ID: 12725
  Sue M, Ishihara A, Iwamura H "Purification and characterization of a β-glucosidase from rye (Secale cereale L.) seedlings" - Plant Science 155(1) (2000) 67-74
  

  Cyclic hydroxamic acids and a glucosidase that occur in rye seedlings were investigated. The concentration of the glucoside of 2,4-dihydroxy-1,4-benzoxazin-3-one (DIBOA-Glc) in shoots increased soon after germination and decreased to a lower, constant level as the plants started autotrophic growth. Cyclic hydroxamic acid glucoside β-glucosidase activity also occurred transiently, and the timing of the increase and decrease was concurrent with that of cyclic hydroxamic acid glucosides. The glucosidase was isolated from 48-h-old rye shoots and purified to apparent homogeneity by using isoelectric precipitation, anion exchange chromatography, and gel filtration. The isoelectric point and the optimum reaction temperature were 4.9–5.1 and 25–30°C, respectively. The N-terminal amino acid sequence was almost identical to that of the wheat glucosidases, but did not show any similarity to the sequences of other glucosidases of plant origin. SDS– and native–PAGE analyses showed that rye had several isozymes of glucosidase, and each isozyme was an oligomer of 60-kDa monomers with a molecular mass of ~300 kDa. The enzyme was highly active not only for DIMBOA-Glc but also for its 7-demethoxy analogue, DIBOA-Glc, which was different from the specificities of maize and wheat glucosidases.

  cyclic hydroxamic acid; β-glucosidase; rye (Secale)

  NCBI PubMed ID: 10773341
  Publication DOI: 10.1016/s0168-9452(00)00204-1
  Publisher: Elsevier
  Correspondence: sue@kais.kyoto-u.ac.jp
  Institutions: Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Kyoto, Japan
  Methods: SDS-PAGE, electrophoresis, HPLC, enzymatic digestion, extraction, enzymatic assay
  
   
  
  Secale cereale cv. haru-ichiban
  CSDB ID 68050 (all data & tools)
• Article ID: 12726
  Sue M, Ishihara A, Iwamura H "Occurrence and characterization of a UDP-glucose:hydroxamic acid glucosyltransferase isolated from wheat (Triticum aestivum) seedlings" - Zeitschrift für Naturforschung. C, Journal of Biosciences 55(9-10) (2000) 701-707
  

  Cyclic hydroxamic acid glucosides are present at high concentrations immediately after germination in wheat (Triticum aestivum L.). Changes in the activity of UDP-Glucose:cyclic hydroxamic acid glucosyltransferase (EC 2.4.1.-) in wheat were investigated using the cyclic hydroxamic acids 2.4-dihydroxy-1,4-benzoxazin-3-one (DIBOA) and its 7-methoxy derivative (DIMBOA) as sugar acceptors. Glucosyltransferase activity on both substrates was detected in dry seeds, with activity increasing after imbibition, peaking in shoots and roots 36-48 hours after imbibition and decreasing thereafter. The transience of glucosyltransferase activity was concurrent with the transient occurrence of the hydroxamic acid glucosides [Nakagawa E., Amano T., Hirai N., and Iwamura H. (1995) Phytochemistry 38, 1349-1354], suggesting that glucosyltransferases regulate the accumulation of hydroxamic acid glucosides in wheat seedlings. Two peaks in activity of UDP-Glucose:DIMBOA glucosyltransferase were detected using a Mono Q column, indicating the presence of at least two isozymes of this glucosyltransferase. The enzyme in the major peak was purified about 1500-fold and shown to be in a monomeric form with a molecular mass of 47 or 49 kDa. The enzyme reacted strongly with DIMBOA, less so with DIBOA. The enzyme of the minor peak on the Mono Q chromatogram, which was also a monomeric enzyme with a molecular mass of 47 kDa, showed similar substrate specificity to that of the major peak enzyme.

  glucosyltransferase, hydroxamic acid, Triticum aestivum

  NCBI PubMed ID: 11098819
  Publication DOI: 10.1515/znc-2000-9-1006
  Journal NLM ID: 8912155
  Publisher: Verlag der Zeitschrift für Naturforschung
  Correspondence: sue@kais.kyoto-u.ac.jp
  Institutions: Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Kyoto, Japan, CREST, Japan Science and Technology Corporation
  Methods: SDS-PAGE, electrophoresis, HPLC, enzymatic digestion, extraction, enzymatic assay
  
   
  
  Triticum aestivum
  CSDB ID 68052 (all data & tools)
• Article ID: 12799
  Vogt T "Glycosyltransferases involved in plant secondary metabolism" - Book: Evolution of Metabolic Pathways (2000) 317-347
  

  glycosyltransferases, glycosides, plant secondary metabolism

  WWW link: https://books.google.ru/books/about/Evolution_of_Metabolic_Pathways.html?id=tSwKpXKVmOkC&redir_esc=y
  Publisher: Elsevier
  Editors: Romeo JT, Ibrahim R, Varin L, De Luca V
  Institutions: Leibniz-Institut for Ptlanzenbiochemie, Halle/Saale, Germany
  
   
  
  (plant)
  CSDB ID 68398 (all data & tools)