Occurrence of oxalyl-CoA synthetase in Indian pulses

Adsule, R. N.; Barat, G. K.

doi:10.1007/bf01922184

Cited by 2 publications

(3 citation statements)

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“…Enzyme activity was shown to be highest in legumes such as pea, soybean, and L. sativus but was also observed in pumpkin (Cucurbita pepo) and wheat germ (Giovanelli and Tobin, 1964;Giovanelli, 1966;Malathi et al, 1970;Adsule and Barat, 1977). Our results indicate that Arabidopsis uses this alternative oxalate catabolism pathway and is not able to degrade oxalate to CO 2 in leaf discs without oxalylCoA synthetase activity.…”

Section: Aae3 Is An Oxalyl-coa Synthetase and Is Required For Oxalatementioning

confidence: 62%

“…The high specificity of the His-AAE3 recombinant enzyme for oxalate identifies AAE3 as the first gene cloned from any organism to encode oxalyl-CoA synthetase activity. Earlier studies have described possible oxalyl-CoA synthetase activity from plant protein extracts, but no gene has previously been isolated that encodes this function (Giovanelli andTobin, 1961, 1964;Malathi et al, 1970;Adsule and Barat, 1977).…”

Section: Aae3 Is An Oxalyl-coa Synthetase and Is Required For Oxalatementioning

confidence: 99%

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A Previously Unknown Oxalyl-CoA Synthetase Is Important for Oxalate Catabolism in Arabidopsis

et al. 2012

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Oxalate is produced by several catabolic pathways in plants. The best characterized pathway for subsequent oxalate degradation is via oxalate oxidase, but some species, such as Arabidopsis thaliana, have no oxalate oxidase activity. Previously, an alternative pathway was proposed in which oxalyl-CoA synthetase (EC 6.2.1.8) catalyzes the first step, but no gene encoding this function has been found. Here, we identify ACYL-ACTIVATING ENZYME3 (AAE3; At3g48990) from Arabidopsis as a gene encoding oxalyl-CoA synthetase. Recombinant AAE3 protein has high activity against oxalate, with K m = 149.0 6 12.7 mM and V max = 11.4 6 1.0 mmol/min/mg protein, but no detectable activity against other organic acids tested. Allelic aae3 mutants lacked oxalyl-CoA synthetase activity and were unable to degrade oxalate into CO 2 . Seeds of mutants accumulated oxalate to levels threefold higher than the wild type, resulting in the formation of oxalate crystals. Crystal formation was associated with seed coat defects and substantially reduced germination of mutant seeds. Leaves of mutants were damaged by exogenous oxalate and more susceptible than the wild type to infection by the fungus Sclerotinia sclerotiorum, which produces oxalate as a phytotoxin to aid infection. Our results demonstrate that, in Arabidopsis, oxalylCoA synthetase encoded by AAE3 is required for oxalate degradation, for normal seed development, and for defense against an oxalate-producing fungal pathogen.

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Section: Aae3 Is An Oxalyl-coa Synthetase and Is Required For Oxalatementioning

confidence: 62%

Section: Aae3 Is An Oxalyl-coa Synthetase and Is Required For Oxalatementioning

confidence: 99%

A Previously Unknown Oxalyl-CoA Synthetase Is Important for Oxalate Catabolism in Arabidopsis

et al. 2012

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“…Biochemical activity of oxalyl-CoA synthetase has been reported in grasspea (Malathi et al 1970) as well as in several other legume crops (Adsule and Barat 1977). However, no information of genes encoding oxalyl-CoA synthetase enzyme were available until 2012.…”

Section: Introductionmentioning

confidence: 99%

Identification of oxalyl-CoA synthetase gene (LsAAE3) and its regulatory role in β-ODAP biosynthesis in grasspea (Lathyrus sativusL.)

Kushwah

Shanmugavadivel

Das

et al. 2021

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Grasspea is a popular pulse crop due to its hardiness and low cost of production. Presence of anti-nutritive factor ‘β-ODAP’ in its seeds and other plant parts hinder its widespread cultivation and usage. Oxalyl-CoA synthetase is one of the key enzyme of β-ODAP biosynthesis pathway, catalyses the conversion of oxalate to oxalyl-CoA. ACYL ACTIVATING ENZYME 3 (AAE3) gene has been characterised to encode an oxalyl-CoA synthetase enzyme in many plant species. We report here the isolation of full length AAE3 homolog in grasspea with a combination of PCR based strategy and in silico analysis. We first identified AAE3 homolog by PCR using degenerate primers. The partial LsAAE3 sequence showed 88% amino acids sequence identity with the characterised AAE3 gene of M. truncatula. We then predicted the full length AAE3 sequence using the publically available transcriptome datasets of grasspea. Determination of LsAAE3 gene and protein structure and phylogenetic relationship analysis strongly suggested that LsAAE3 is a true homolog of AAE3 gene. Expression profiling of LsAAE3 in grasspea varieties with contrast in β-ODAP content revealed its inverse relationship with the β-ODAP content, LsAAE3 thus negatively regulates the synthesis of β-ODAP. Involvement of AAE3 encoded oxalyl-CoA synthetase in a CoA-dependent pathway of oxalate degradation is well proven in many plant species. We also identified the CoA-dependent pathway of oxalate degradation in grasspea. Based on these observations, we hypothesized that LsAAE3 may regulate β-ODAP content, possibly, by CoA-dependent pathway of oxalate degradation in grasspea. If this hypothesis is substantiated, genetic manipulation of LsAAE3 presents viable option for reducing β-ODAP content in grass pea.

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Occurrence of oxalyl-CoA synthetase in Indian pulses

Cited by 2 publications

References 5 publications

A Previously Unknown Oxalyl-CoA Synthetase Is Important for Oxalate Catabolism in Arabidopsis

A Previously Unknown Oxalyl-CoA Synthetase Is Important for Oxalate Catabolism in Arabidopsis

Identification of oxalyl-CoA synthetase gene (LsAAE3) and its regulatory role in β-ODAP biosynthesis in grasspea (Lathyrus sativusL.)

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