Benzoic acid glucosinolate esters and other glucosinolates from Arabidopsis thaliana

Reichelt, Michael; Brown, P. D.; Schneider, Bernd; Oldham, Neil J.; Stauber, Einar J.; Tokuhisa, James G.; Kliebenstein, Daniel J.; Mitchell-Olds, Thomas; Gershenzon, Jonathan

doi:10.1016/s0031-9422(02)00014-6

Cited by 215 publications

(186 citation statements)

References 24 publications

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“…The majority of the metabolites selected for the analysis of the Arabidopsis samples in this study were glucosinolates because they give unique ion masses, i.e. they are easy to extract from the raw data and are known to be present in many different genotypes (Kliebenstein et al 2001;Reichelt et al 2002). The same criteria were applied to the selection of the metabolites from the potato series.…”

Section: Metabolite Selectionmentioning

confidence: 99%

Accurate mass error correction in liquid chromatography time-of-flight mass spectrometry based metabolomics

Mihaleva¹,

Vorst²,

Maliepaard

et al. 2008

Metabolomics

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Compound identification and annotation in (untargeted) metabolomics experiments based on accurate mass require the highest possible accuracy of the mass determination. Experimental LC/TOF-MS platforms equipped with a time-to-digital converter (TDC) give the best mass estimate for those mass signals with an intensity similar to that of the lock-mass used for internal calibration. However, they systematically underestimate the mass obtained at higher signal intensity and overestimate it at low signal intensities compared to that of the lock-mass. To compensate for these effects, specific tools are required for correction and automation of accurate mass calculations from LC/MS signals. Here, we present a computational procedure for the derivation of an intensity-dependent mass correction function. The chromatographic mass signals for a set of known compounds present in a large number of samples were reconstructed over consecutive scans for each sample. It was found that the mass error is a linear function of the logarithm of the signal intensity adjusted to the associated lock-mass intensity. When applied to all mass data points, the correction function reduced the mass error for the majority of the tested compounds to B1 ppm over a wide range of signal intensities. The mass correction function has been implemented in a Python 2.4 script, which accepts raw data in NetCDF format as input, corrects the detected masses and returns the corrected NetCDF files for subsequent (automated) processing, such as mass signal alignment and database searching.

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Section: Metabolite Selectionmentioning

confidence: 99%

Accurate mass error correction in liquid chromatography time-of-flight mass spectrometry based metabolomics

Mihaleva¹,

Vorst²,

Maliepaard

et al. 2008

Metabolomics

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“…The desulfoglucosinolates were identified and quantified by HPLC analyses on a C18 reversed-phase column (LiChrospher RP-18, 250 3 4.6 mm i.d., 5-mm particle size; Chrompack) by comparison of retention times and UV spectra to those of purified standards and by measuring the A 229 relative to an internal standard (Reichelt et al, 2002;Brown et al, 2003).…”

Section: Glucosinolate Analysesmentioning

confidence: 99%

Two Arabidopsis Genes (IPMS1 and IPMS2) Encode Isopropylmalate Synthase, the Branchpoint Step in the Biosynthesis of Leucine

et al. 2006

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Heterologous expression of the Arabidopsis (Arabidopsis thaliana) IPMS1 (At1g18500) and IPMS2 (At1g74040) cDNAs in Escherichia coli yields isopropylmalate synthases (IPMSs; EC 2.3.3.13). These enzymes catalyze the first dedicated step in leucine (Leu) biosynthesis, an aldol-type condensation of acetyl-coenzyme A (CoA) and 2-oxoisovalerate yielding isopropylmalate. Most biochemical properties of IPMS1 and IPMS2 are similar: broad pH optimum around pH 8.5, Mg 21 as cofactor, feedback inhibition by Leu, K m for 2-oxoisovalerate of approximately 300 mM, and a V max of approximately 2 3 10 3 mmol min 21 g 21 . However, IPMS1 and IPMS2 differ in their K m for acetyl-CoA (45 mM and 16 mM, respectively) and apparent quaternary structure (dimer and tetramer, respectively). A knockout insertion mutant for IPMS1 showed an increase in valine content but no changes in Leu content; two insertion mutants for IPMS2 did not show any changes in soluble amino acid content. Apparently, in planta each gene can adequately compensate for the absence of the other, consistent with available microarray and reverse transcription-polymerase chain reaction data that show that both genes are expressed in all organs at all developmental stages. Both encoded proteins accept 2-oxo acid substrates in vitro ranging in length from glyoxylate to 2-oxohexanoate, and catalyze at a low rate the condensation of acetyl-CoA and 4-methylthio-2-oxobutyrate, i.e. a reaction involved in glucosinolate chain elongation normally catalyzed by methylthioalkylmalate synthases. The evolutionary relationship between IPMS and methylthioalkylmalate synthase enzymes is discussed in view of their amino acid sequence identity (60%) and overlap in substrate specificity.

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“…These compounds are substrates for myrosinases, which convert the various glucosinolates into an array of toxic and volatile substances that are important in plant-insect interactions (Rask et al, 2000). The enzymes that catalyze the core reactions of glucosinolate biosynthesis have been identified (Wittstock and Halkier, 2002); however, a number of glucosinolates are further modified by additions of other substituents that include sinapoyl and benzoyl groups (Linscheid et al, 1980;Reichelt et al, 2002;Brown et al, 2003). This acylation may have an impact on glucosinolate turnover and plant-herbivore interactions because they are not readily degradable targets for myrosinases (Taipalensuu et al, 1997).…”

Section: Candidate Reactions For Scpl Acyltransferases Can Be Found Tmentioning

confidence: 99%

“…This acylation may have an impact on glucosinolate turnover and plant-herbivore interactions because they are not readily degradable targets for myrosinases (Taipalensuu et al, 1997). The presence of benzoylated glucosinolates in Arabidopsis has already been demonstrated, and sinapoylated glucosinolates have been detected in Arabidopsis seed extracts (Graser et al, 2001;Reichelt et al, 2002). Sinapoyl-Glc and benzoyl-Glc are potential donor molecules in the acylation reaction, making Clade IA SCPL enzymes good candidates for the catalysts involved.…”

Section: Candidate Reactions For Scpl Acyltransferases Can Be Found Tmentioning

confidence: 99%

An Expression and Bioinformatics Analysis of the Arabidopsis Serine Carboxypeptidase-Like Gene Family

2005

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The Arabidopsis (Arabidopsis thaliana) genome encodes a family of 51 proteins that are homologous to known serine carboxypeptidases. Based on their sequences, these serine carboxypeptidase-like (SCPL) proteins can be divided into several major clades. The first group consists of 21 proteins which, despite the function implied by their annotation, includes two that have been shown to function as acyltransferases in plant secondary metabolism: sinapoylglucose:malate sinapoyltransferase and sinapoylglucose:choline sinapoyltransferase. A second group comprises 25 SCPL proteins whose biochemical functions have not been clearly defined. Genes encoding representatives from both of these clades can be found in many plants, but have not yet been identified in other phyla. In contrast, the remaining SCPL proteins include five members that are similar to serine carboxypeptidases from a variety of organisms, including fungi and animals. Reverse transcription PCR results suggest that some SCPL genes are expressed in a highly tissue-specific fashion, whereas others are transcribed in a wide range of tissue types. Taken together, these data suggest that the Arabidopsis SCPL gene family encodes a diverse group of enzymes whose functions are likely to extend beyond protein degradation and processing to include activities such as the production of secondary metabolites.Serine carboxypeptidases (SCPs) are members of the a/b hydrolase family of proteins, which make use of a Ser-Asp-His catalytic triad to cleave the carboxyterminal peptide bonds of their protein or peptide substrates (Hayashi et al., 1973(Hayashi et al., , 1975Bech and Breddam, 1989;Liao and Remington, 1990;Liao et al., 1992;Ollis et al., 1992). Proteins that contain this catalytic triad and are otherwise homologous to SCPs have been found in a variety of organisms (Doi et al., 1980;Kim and Hayashi, 1983;Breddam, 1986;Baulcombe et al., 1987;Galjart et al., 1988;Bradley, 1992;Degan et al., 1994;Endrizzi et al., 1994;Wajant et al., 1994;Jones et al., 1996;Li and Steffens, 2000). Many of these serine carboxypeptidase-like (SCPL) proteins have been annotated as peptidases based only on this shared sequence similarity; however, studies have shown that some of them function not as peptidases, but as acyltransferases and lyases (Wajant et al., 1994;Lehfeldt et al., 2000;Li and Steffens, 2000;Shirley et al., 2001). For example, several SCPL proteins have been shown to catalyze the production of plant secondary metabolites involved in herbivory defense and UV protection (Wajant et al., 1994;Lehfeldt et al., 2000;Li and Steffens, 2000), including the hydroxynitrile lyase from Sorghum bicolor (SbHNL) necessary for cyanogenesis, and the acyltransferases in wild tomato (Lycopersicon pennellii) that catalyze the formation 2,3,4-isobutyryl-Glc (Wajant et al., 1994;Lehfeldt et al., 2000). Two enzymes in Arabidopsis (Arabidopsis thaliana) responsible for sinapate ester biosynthesis are also SCPL proteins. Sinapoylglucose:malate sinapoyltransferase (SMT) catalyzes the formation of s...

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Benzoic acid glucosinolate esters and other glucosinolates from Arabidopsis thaliana

Cited by 215 publications

References 24 publications

Accurate mass error correction in liquid chromatography time-of-flight mass spectrometry based metabolomics

Accurate mass error correction in liquid chromatography time-of-flight mass spectrometry based metabolomics

Two Arabidopsis Genes (IPMS1 and IPMS2) Encode Isopropylmalate Synthase, the Branchpoint Step in the Biosynthesis of Leucine

An Expression and Bioinformatics Analysis of the Arabidopsis Serine Carboxypeptidase-Like Gene Family

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