hydrolase/arabidopsis

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Functional and chemical characterization of XAF: a heat-stable plant polymer that activates xyloglucan endotransglucosylase/hydrolase (XTH).

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Xyloglucan endotransglucosylase/hydrolase (XTH) proteins that possess xyloglucan endotransglucosylase (XET) activity contribute to cell-wall assembly and remodelling, orchestrating plant growth and development. Little is known about in-vivo XET regulation, other than at the XTH

Cloning, expression and characterization of a Nudix hydrolase that catalyzes the hydrolytic breakdown of ADP-glucose linked to starch biosynthesis in Arabidopsis thaliana.

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'Nudix' hydrolases are widely distributed nucleotide pyrophosphatases that possess a conserved GX5EX7REUXEEXGU motif where U is usually isoleucine, leucine or valine. Among them, Escherichia coli ADP-sugar pyrophosphatase (ASPP) has been shown to catalyze the hydrolytic breakdown of ADP-glucose

Fatty Acid Amide Hydrolases: An Expanded Capacity for Chemical Communication?

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Fatty acid amide hydrolase (FAAH) is an enzyme that belongs to the amidase signature (AS) superfamily and is widely distributed in multicellular eukaryotes. FAAH hydrolyzes lipid signaling molecules - namely, N-acylethanolamines (NAEs) - which terminates their actions. Recently, the crystal

Molecular identification of a functional homologue of the mammalian fatty acid amide hydrolase in Arabidopsis thaliana.

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N-Acylethanolamines (NAEs) are endogenous constituents of plant and animal tissues, and in vertebrates their hydrolysis terminates their participation as lipid mediators in the endocannabinoid signaling system. The membrane-bound enzyme responsible for NAE hydrolysis in mammals has been identified

Overexpression of Fatty Acid Amide Hydrolase Induces Early Flowering in Arabidopsis thaliana.

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N-acylethanolamines (NAEs) are bioactive lipids derived from the hydrolysis of the membrane phospholipid N-acylphosphatidylethanolamine (NAPE). In animal systems this reaction is part of the "endocannabinoid" signaling pathway, which regulates a variety of physiological processes. The signaling

The AMI1 gene family: indole-3-acetamide hydrolase functions in auxin biosynthesis in plants.

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Novel genes that function in the conversion of indole-3-acetamide (IAM) into indole-3-acetic acid (IAA), which were previously thought to exist only in the bacterial genome, have been isolated from plants. The finding of the AtAMI1 gene in Arabidopsis thaliana and the NtAMI1 gene in Nicotiana

Cloning and characterization of an S-formylglutathione hydrolase from Arabidopsis thaliana.

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A cDNA from Arabidopsis thaliana resembling S-formylglutathione hydrolase (SFGH), an enzyme with putative roles in formaldehyde detoxification in animals and microorganisms, has been cloned and expressed in Escherichia coli. The purified recombinant Arabidopsis enzyme (AtSFGH) was a dimer composed

AMP and GMP Catabolism in Arabidopsis Converge on Xanthosine, Which Is Degraded by a Nucleoside Hydrolase Heterocomplex.

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Plants can fully catabolize purine nucleotides. A firmly established central intermediate is the purine base xanthine. In the current widely accepted model of plant purine nucleotide catabolism, xanthine can be generated in various ways involving either inosine and hypoxanthine or guanosine and

Investigating the Induced Systemic Resistance Mechanism of 2,4-Diacetylphloroglucinol (DAPG) using DAPG Hydrolase-Transgenic Arabidopsis

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Plant immune responses can be triggered by chemicals, microbes, pathogens, insects, or abiotic stresses. In particular, induced systemic resistance (ISR) refers to the activation of the immune system due to a plant's interaction with beneficial microorganisms. The phenolic compound,

Comprehensive analysis of cytosolic Nudix hydrolases in Arabidopsis thaliana.

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Nudix hydrolases are a family of proteins that catalyze the hydrolysis of a variety of nucleoside diphosphate derivatives. Twenty-four genes of the Nudix hydrolase homologues (AtNUDTs) with predicted localizations in the cytosol, chloroplasts, and mitochondria exist in Arabidopsis thaliana. Here, we

Molecular characterization of organelle-type Nudix hydrolases in Arabidopsis.

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Nudix (for nucleoside diphosphates linked to some moiety X) hydrolases act to hydrolyze ribonucleoside and deoxyribonucleoside triphosphates, nucleotide sugars, coenzymes, or dinucleoside polyphosphates. Arabidopsis (Arabidopsis thaliana) contains 27 genes encoding Nudix hydrolase homologues

The plant Nudix hydrolase family.

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Nudix hydrolases are a family of proteins defined by a conserved amino-acid sequence GX(5)-EX(7)REUXEEXGU, where U is a hydrophobic residue. These enzymes are widely distributed among all classes of organisms and catalyze, with varying degrees of substrate specificity, the hydrolysis of a variety of

Unique regulation of the active site of the serine esterase S-formylglutathione hydrolase.

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S-Formylglutathione hydrolases (SFGHs) are highly conserved thioesterases present in prokaryotes and eukaryotes, and form part of the formaldehyde detoxification pathway, as well as functioning as xenobiotic-hydrolysing carboxyesterases. As defined by their sensitivity to covalent modification,

Brassica napus soluble epoxide hydrolase (BNSEH1).

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Epoxide hydrolase (EC 3.3.2.3) in plants is involved in the metabolism of epoxy fatty acids and in mediating defence responses. We report the cloning of a full-length epoxide hydrolase cDNA (BNSEH1) from oilseed rape (Brassica napus) obtained by screening of a cDNA library prepared from methyl

Effects of progressive drought stress on the expression of patatin-like lipid acyl hydrolase genes in Arabidopsis leaves.

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Patatin-like genes have recently been cloned from several plant species and found to be involved in stress responses and development. In previous work, we have shown that a patatin-like gene encoding a galactolipid acyl hydrolase (EC 3.1.1.26) was stimulated by drought in the leaves of the tropical

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