UDP-glucosyltransferase activity toward exogenous substrates in Drosophila melanogaster

Real, M. Dolores; Ferré, Juan; Chapa, F.J.

doi:10.1016/0003-2697(91)90239-p

Cited by 25 publications

(13 citation statements)

References 11 publications

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“…UGTs active against several plant phenolics and tyrosine have been described in M. sexta [7,33]. UGT activity against p ‐nitrophenol, 1‐naphthol, 2‐naphthol and xanthurenic acid has been reported in D. melanogaster [13,34], and activity against p ‐nitrophenol has also been reported in the housefly, Musca domestica [35]. As discussed already, the insect baculovirus EGT enzymes are UGTs specific for various ecdysteroids [36].…”

Section: Discussionmentioning

confidence: 99%

Characterization of a novel silkworm (Bombyx mori) phenol UDP‐glucosyltransferase

Luque

Okano²,

O’Reilly

2002

European Journal of Biochemistry

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Sugar conjugation is a major pathway for the inactivation and excretion of both endogenous and exogenous compounds. We report here the molecular cloning and functional characterization of a phenol UDP-glucosyltransferase (UGT) from the silkworm, Bombyx mori, which was named BmUGT1. The complete cDNA clone is 1.6 kb, and the gene is expressed in several tissues of fifth-instar larvae, including fat body, midgut, integument, testis, silk gland and haemocytes. The predicted protein comprises 520 amino acids and has 30% overall amino-acid identity with other members of the UGT family. The most conserved region of the protein is the C-terminal half, which has been implicated in binding the UDP-sugar. BmUGT1 was expressed in insect cells using the baculovirus expression system, and a range of compounds belonging to diverse chemical groups were assessed as potential substrates for the enzyme. The expressed enzyme had a wide substrate specificity, showing activity with flavonoids, coumarins, terpenoids and simple phenols. These results support a role for the enzyme in detoxication processes, such as minimizing the harmful effects of ingested plant allelochemicals. This work represents the first instance where an insect ugt gene has been associated with a specific enzyme activity.

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Section: Discussionmentioning

confidence: 99%

Characterization of a novel silkworm (Bombyx mori) phenol UDP‐glucosyltransferase

Luque

Okano²,

O’Reilly

2002

European Journal of Biochemistry

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“…Further work is needed to solve this problem. GTases that has an activity against naphthol was reported from several insects [31,32] but not from plants. Other researchers may not have investigated this point because naphthols are rarely found in plants.…”

Section: Discussionmentioning

confidence: 99%

Molecular cloning and heterologous expression of novel glucosyltransferases from tobacco cultured cells that have broad substrate specificity and are induced by salicylic acid and auxin

Taguchi

Yazawa

Hayashida

et al. 2001

European Journal of Biochemistry

113

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Scopoletin is one of the phytoalexins in tobacco. Cells of the T-13 cell line (Nicotiana tabacum L. Bright Yellow) accumulate a large amount of scopoletin, also known as 7-hydroxy-6-methoxycoumarin, as a glucoconjugate, scopolin, in vacuoles. We report here the molecular cloning of glucosyltransferases that can catalyze the glucosylation of many kinds of secondary metabolites including scopoletin. Two cDNAs encoding glucosyltransferase (NtGT1a and NtGT1b) were isolated from a cDNA library derived from the tobacco T-13 cell line by screening with heterologous cDNAs as a probe. The deduced amino-acid sequences of NtGT1a and NtGT1b exhibited 92% identity with each other, < 20±50% identities with other reported glucosyltransferases. Heterologous expression of these genes in Escherichia coli showed that the recombinant enzymes had glucosylation activity against both flavonoids and coumarins.They also strongly reacted with 2-naphthol as a substrate. These recombinant enzymes can utilize UDP-glucose as the sugar donor, but they can also utilize UDP-xylose as a weak donor. RNA blot analysis showed that these genes are induced by salicylic acid and auxin, but the time course of the expression was different. This result is similar to the changes in scopoletin glucosylation activity in these tobacco cells after addition of these plant growth regulators. These results might suggest that one of the roles of the products of these genes is scopoletin glucosylation, in response to salicylic acid and/or auxin, together with the other glucosyltransferases in tobacco cells.

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“…To demonstrate the occurrence of GT isoenzymes, we analyzed one endogenous and two xenobiotic compounds previously reported as substrates for the GT activity (Real and Ferré, 1990;Real et al, 1991) in three developmental stages of Drosophila melanogaster. For all three studied substrates, maxi- mum GT activity was found in the larval and adult stages, whose high metabolic rates correlate with the capability for increased detoxification levels.…”

Section: Discussionmentioning

confidence: 99%

“…Assays of xanthurenic acid:UDP-GT activity and of 1-naphthol: and 2naphthol:UDP-GT activities were carried out according to Real and Ferré (1990) and Real et al (1991), respectively.…”

Section: Enzyme Assaysmentioning

confidence: 99%

“…In Drosophila, UDP-GT activity toward the endogenous substrate xanthurenic acid and the xenobiotics 4-nitrophenol, 1-naphthol, and 2-naphthol has been demonstrated (Real and Ferré, 1990;Real et al, 1991). The distribution and substrate specificity of GT activity in Drosophila (Real and Ferré, 1990) and in the larval tissues of Manduca sexta (Ahmad and Hopkins, 1993) suggested the presence of multiple enzyme forms.…”

Section: Introductionmentioning

confidence: 99%

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Separation by FPLC chromatofocusing of UDP-glucosyltransferases from three developmental stages ofDrosophila melanogaster

Rausell

Llorca

Real

1997

Arch. Insect Biochem. Physiol.

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Variation of UDP‐glucosyltransferase activity, during Drosophila melanogaster development, was analyzed. The endogenous metabolite xanthurenic acid and the xenobiotic compounds 1‐naphthol and 2‐naphthol were used as substrates. Developmentally regulated differences were observed for the three substrates, suggesting the presence of UDP‐glucosyltransferase isoenzymes. This was further confirmed by FPLC chromatofocusing on a Mono P column: seven peaks of UDP‐glucosyltransferase activity (pHs: ≥6.3, 5.8, 5.5, 4.9, 4.5, 4.2, ≤4.0) with either single or overlapping substrate specificity were detected. A single xanthurenic acid:UDP‐glucosyltransferase activity (pl 5.8) was found throughout development. In contrast, a gradual increase in the number of 2‐napthol:UDP‐glucosyltransferase isoenzymes (pl from 6.3 to 4.0) was observed during development, whereas no isoenzymes specific for 1‐naphthol were resolved. Based on the distribution and substrate specificity of the eluted peaks in the three developmental stages analyzed, the presence of seven or possibly eight UDP‐glucosyltransferase isoenzymes is proposed. Arch. Insect Biochem. Physiol. 34:347–358, 1997. © 1997 Wiley‐Liss, Inc.

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UDP-glucosyltransferase activity toward exogenous substrates in Drosophila melanogaster

Cited by 25 publications

References 11 publications

Characterization of a novel silkworm (Bombyx mori) phenol UDP‐glucosyltransferase

Characterization of a novel silkworm (Bombyx mori) phenol UDP‐glucosyltransferase

Molecular cloning and heterologous expression of novel glucosyltransferases from tobacco cultured cells that have broad substrate specificity and are induced by salicylic acid and auxin

Separation by FPLC chromatofocusing of UDP-glucosyltransferases from three developmental stages ofDrosophila melanogaster

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