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l alanine/arabidopsis
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The Arabidopsis thaliana isogene NIT4 and its orthologs in tobacco encode beta-cyano-L-alanine hydratase/nitrilase.
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Nitrilases (nitrile aminohydrolases, EC ) are enzymes that catalyze the hydrolysis of nitriles to the corresponding carbon acids. Among the four known nitrilases of Arabidopsis thaliana, the isoform NIT4 is the most divergent one, and homologs of NIT4 are also known from species not belonging to the
Molecular cloning of Brassica rapa nitrilases and their expression during clubroot development.
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SUMMARY Three isoforms of nitrilase were cloned from turnip, Brassica rapa L., and their expression during clubroot development caused by Plasmodiophora brassicae was investigated. The isoforms were designated BrNIT-T1, BrNIT-T2 and BrNIT-T4 based on homology to known nitrilases. BrNIT-T1 and
Identification and Biochemical Characterization of the Serine Biosynthetic Enzyme 3-Phosphoglycerate Dehydrogenase in Marchantia polymorpha.
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L-serine is an important molecule in all living organisms, and thus its biosynthesis is considered to be regulated according to demand. 3-Phosphoglycerate dehydrogenase (PGDH), the first committed enzyme of the phosphorylated pathway of L-serine biosynthesis, is regulated by negative feedback from
Microarray analysis of Arabidopsis plants in response to allelochemical L-DOPA.
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Velvetbean (Mucuna pruriens) plants impede the growth of neighboring plants. One compound, 3-(3',4'-dihydroxyphenyl)-L-alanine (L-DOPA), is responsible for the allelopathic capacity of velvetbean. This compound is an active allelochemical that decreases root growth of several plant species. In
Triazolyl phenyl disulfides: 8-Amino-7-oxononanoate synthase inhibitors as potential herbicides.
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The chemical validation of a potential herbicide target was investigated with 8-amino-7-oxononanoate synthase (AONS, also known as 7-keto-8-aminopelargonate synthase, KAPAS) and triazolyl phenyl disulfide derivatives in vitro and in vivo. AONS activity was completely inhibited by these synthesized
The Arabidopsis thaliana gene annotated by the locus tag At3g08860 encodes alanine aminotransferase.
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The aminotransferase gene family in the model plant Arabidopsis thaliana consists of 44 genes, eight of which are suggested to be alanine aminotransferases. One of the putative alanine aminotransferases genes, At3g08860, was attributed the function of alanine:glyoxylate
Molecular and biochemical characterization of a serine racemase from Arabidopsis thaliana.
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A cDNA encoding a homolog of mammalian serine racemase, a unique enzyme in eukaryotes, was isolated from Arabidopsis thaliana and expressed in Escherichia coli cells. The gene product, of which the amino acid residues for binding pyridoxal 5'-phosphate (PLP) are conserved in this as well as
The mutagenicity of azido derivatives of monosaccharides and alcohols and of N-(3-azido-2-hydroxypropyl) derivatives of purines and pyrimidines in Arabidopsis thaliana and in Salmonella typhimurium.
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The azido derivatives of alcohols (3-azido-1,2-propandiol and 1,3-diazido-2-propanol) and monosaccharides (6-azido-6-deoxy-beta-D-glucose and 6-azido-6-deoxy-beta-D-galactose), as well as the proximal mutagenic product of sodium azide metabolism beta-azido-L-alanine, exhibited a high mutagenic
A role for nitrilase 3 in the regulation of root morphology in sulphur-starving Arabidopsis thaliana.
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Arabidopsis thaliana expresses four nitrilases, three of which (NIT1, NIT2 and NIT3) are able to convert indole-3-acetonitrile to indole-3-acetic acid (IAA), the plant growth hormone, while the isozyme NIT4 is a beta-cyano-l-alanine hydratase/nitrilase. NIT3 promoter activity is marginal in leaves
Properties of serine:glyoxylate aminotransferase purified from Arabidopsis thaliana leaves.
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The photorespiratory enzyme L-serine:glyoxylate aminotransferase (SGAT; EC 2.6.1.45) was purified from Arabidopsis thaliana leaves. The final enzyme was approximately 80% pure as revealed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis with silver staining. The identity of the enzyme
Arabidopsis sulfurtransferases: investigation of their function during senescence and in cyanide detoxification.
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Sulfurtransferases (STs) and beta-cyano- l-alanine synthase (CAS) are suggested to be involved in cyanide detoxification. Therefore, the accumulation of ST1 and CAS RNAs, and the ST and CAS protein levels and enzyme activities were determined in Arabidopsis thaliana Heynh. plants grown under
Crystal Structure Of Photorespiratory Alanine:Glyoxylate Aminotransferase 1 (AGT1) From Arabidopsis thaliana.
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Photorespiration is an energetically costly metabolic pathway for the recycling of phosphoglycolate produced by the oxygenase activity of ribulose-1,5-bisphosphate carboxylase/oxygenase (RUBISCO) to phosphoglycerate. Arabidopsis alanine:glyoxylate aminotransferase 1 (AGT1) is a peroxisomal
Characterization of the NifS-like domain of ABA3 from Arabidopsis thaliana provides insight into the mechanism of molybdenum cofactor sulfuration.
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The molybdenum cofactor sulfurase ABA3 from Arabidopsis thaliana specifically regulates the activity of the molybdenum enzymes aldehyde oxidase and xanthine dehydrogenase by converting their molybdenum cofactor from the desulfo-form into the sulfo-form. ABA3 is a two-domain protein with an
An integrated RNAseq-1H NMR metabolomics approach to understand soybean primary metabolism regulation in response to Rhizoctonia foliar blight disease.
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Rhizoctonia solani AG1-IA is a devastating phytopathogen causing Rhizoctonia foliar blight (RFB) of soybean worldwide with yield losses reaching 60%. Plant defense mechanisms are complex and information from different metabolic pathways is required to thoroughly understand plant defense regulation
Cyanide metabolism in higher plants: cyanoalanine hydratase is a NIT4 homolog.
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Cyanoalanine hydratase (E.C. 4.2.1.65) is an enzyme involved in the cyanide detoxification pathway of higher plants and catalyzes the hydrolysis of beta-cyano-L-alanine to asparagine. We have isolated the enzyme from seedlings of blue lupine (Lupinus angustifolius) to obtain protein sequence
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