Enzymic synthesis of 1-O-indol-3-ylacetyl-β-<scp>d</scp>-glucose and indol-3-ylacetyl-myo-inositol

Michalczuk, Lech; Bandurski, Robert S.

doi:10.1042/bj2070273

Cited by 71 publications

(37 citation statements)

References 22 publications

(29 reference statements)

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“…As shown by the data of Table I-A, the enzyme is specific for UDPG and will not make an ester from labeled IAA and UDPGal or UDPXylose, the activity with these two latter substrates being zero. A previously published study (14) established that the reaction would only use the uridine nucleotide, and would not use ADP, CDP, or GDP-glucose. Thus, specificity for the nucleotide sugar is stringent.…”

Section: Results Substrate Specificitymentioning

confidence: 99%

“…We conclude that there is an unknown, heat-stable factor which can, in part, restore enzyme activity. DISCUSSION The synthesis of IAA-glucose from free IAA and UDPG is the first step in a series of reactions leading to the characteristic IAAmyo-inositol conjugates in plants such as Zea mays (4,5,7,13,14,18). Thus, this enzyme may represent a control point for the regulation of the relative amounts of free and esterified IAA.…”

Section: Results Substrate Specificitymentioning

confidence: 99%

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Enzymic Synthesis of Indole-3-Acetyl-1-O-β-d-Glucose

Leźnicki

Bandurski²

1988

Plant Physiol.

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ABSTRACIThe synthesis of indole-3-acetyl-1-0-,8->glucose from indole-3-acetic acid (IAA) and uridine diphosphoglucose (UDPG) has been shown to be a reversible reaction with the equilibrium away from ester formation and toward formation of IAA. The enzyme occurs primarily in the liquid endosperm of the corn kernel but some activity occurs in the embryo. It is relatively specific showing no glucose ester formation with oxindole-3-acetic acid or 7-hydroxy-oxindole-3-acetic acid, and low activity with phenylpropene acids, such as p-coumaric acid. The enzyme is also specific for the nucleotide sugar showing no activity with UDPGalactose or UDPXylose. The enzyme is inhibited by inorganic pyrophosphate, by phosphate esters and by phospholipids, particularly phosphatidyl ethanolamine. The enzyme is inhibited by zeatin, by 2,4-dichlorophenoxyacetic acid, by IAA-myo-inositol and IAA-glucan, but not by zeatin riboside, and only weakly by gibberellic acid, abscisic acid, and kinetin. The reaction is slightly stimulated by both calcium and calmodulin and, in some cases, by thiol compounds. The role of this enzyme in the homeostatic control of indole-3-acetic acid levels in Zea mays is discussed.The preceding paper (13) describes a method for the extraction and partial purification of the enzyme catalyzing the formation of indole-3-acetyl-1-0-J-D-glucose from UDPG3 and IAA. In addition, certain physical parameters of the enzyme including its mol wt, pH optimum and stability were provided and an assay method described. In this work, we describe the substrate specificity of the enzyme, its sensitivity to inhibitors, the reversibility of the reaction, how this enzyme could function in the control of levels of free IAA, and our attempt to prepare antibodies to the enzyme. MATERIALS AND METHODSThe enzyme assay, purification procedure, and all analytical techniques were as described previously (13). Briefly, the assay depends upon separating the uncharged reaction product, l-['4C] '

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Section: Results Substrate Specificitymentioning

confidence: 99%

Section: Results Substrate Specificitymentioning

confidence: 99%

Enzymic Synthesis of Indole-3-Acetyl-1-O-β-d-Glucose

Leźnicki

Bandurski²

1988

Plant Physiol.

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“…Similarly, indole-3-acetic acid (IAA)-Glc synthesized by indole-3-acetic acid glucosyltransferase serves as an activated form of IAA, which is used in a transesterification reaction to form IAA-inositol (Michalczuk and Bandurski, 1982;Jackson et al, 2001Jackson et al, , 2002Ljung et al, 2002). This latter reaction is analogous to sinapoylmalate biosynthesis and preliminary indications suggest that it may be catalyzed by an SCPL enzyme (Kowalczyk et al, 2003).…”

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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“…For example, glucose ester transesterification reactions are found in pathways leading to numerous other plant secondary metabolites, including the synthesis of chlorogenic acid in sweet potato (Villegas and Kojima, 1986) and gallotannins in oak (Gross, 1983). Similarly, indoleacetic acid (IAA)-glucose serves as an activated form of IAA, which is used in a transesterification reaction to form IAA-inositol (Michalczuk and Bandurski, 1982). These reactions are analogous to sinapoylmalate biosynthesis and may be catalyzed by a SCPL enzyme.…”

Section: Sng1 Encodes Smt a Scpl Proteinmentioning

confidence: 99%

Cloning of the SNG1 Gene of Arabidopsis Reveals a Role for a Serine Carboxypeptidase-like Protein as an Acyltransferase in Secondary Metabolism

et al. 2000

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Serine carboxypeptidases contain a conserved catalytic triad of serine, histidine, and aspartic acid active-site residues. These enzymes cleave the peptide bond between the penultimate and C-terminal amino acid residues of their protein or peptide substrates. The Arabidopsis Genome Initiative has revealed that the Arabidopsis genome encodes numerous proteins with homology to serine carboxypeptidases. Although many of these proteins may be involved in protein turnover or processing, the role of virtually all of these serine carboxypeptidase-like (SCPL) proteins in plant metabolism is unknown. We previously identified an Arabidopsis mutant, sng1 (sinapoylglucose accumulator 1), that is defective in synthesis of sinapoylmalate, one of the major phenylpropanoid secondary metabolites accumulated by Arabidopsis and some other members of the Brassicaceae. We have cloned the gene that is defective in sng1 and have found that it encodes a SCPL protein. Expression of SNG1 in Escherichia coli demonstrates that it encodes sinapoylglucose:malate sinapoyltransferase, an enzyme that catalyzes a transesterification instead of functioning like a hydrolase, as do the other carboxypeptidases. This finding suggests that SCPL proteins have acquired novel functions in plant metabolism and provides an insight into the evolution of secondary metabolic pathways in plants. INTRODUCTIONPlants produce thousands of unique molecules that are collectively referred to as secondary metabolites. Even within the angiosperms, many of these compounds are unique to specific taxa, indicating that the pathways that produce them may have evolved within the last 100,000 years. A central question in the study of plant secondary metabolism concerns how the catalytic diversity of plant secondary metabolism has arisen. What classes of genes and proteins have been co-opted, presumably from their ancestral roles in primary metabolism, to serve as catalysts in the synthesis of secondary metabolites?In Arabidopsis, the phenylpropanoid pathway leads to the production of sinapic acid esters, a group of fluorescent UVprotective secondary metabolites derived from phenylalanine (Figure 1). These compounds are dispensable under laboratory conditions and thus provide targets for the genetic dissection of phenylpropanoid metabolism. The analysis of these compounds is facilitated by their blue fluorescence under UV light both in vivo and after thin-layer chromatography (TLC) (Chapple et al., 1992;Ruegger et al., 1999). Arabidopsis and some other members of the Brassicaceae accumulate three major sinapic acid esters. In the biosynthetic pathway leading to these compounds, sinapoylglucose is the immediate precursor of sinapoylcholine and sinapoylmalate, which accumulate in seeds and leaves, respectively. 1-O -Sinapoylglucose is a ␤ -acetal ester with a high free energy of hydrolysis (Mock and Strack, 1993); it provides the necessary free energy for the transacylation reaction catalyzed by sinapoylglucose:malate sinapoyltransferase (SMT; EC 2.3.1.92) (Strack, 1982), which ...

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Enzymic synthesis of 1-O-indol-3-ylacetyl-β-d-glucose and indol-3-ylacetyl-myo-inositol

Cited by 71 publications

References 22 publications

Enzymic Synthesis of Indole-3-Acetyl-1-O-β-d-Glucose

Enzymic Synthesis of Indole-3-Acetyl-1-O-β-d-Glucose

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

Cloning of the SNG1 Gene of Arabidopsis Reveals a Role for a Serine Carboxypeptidase-like Protein as an Acyltransferase in Secondary Metabolism

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