phaseolus leptostachyus/phosphatase

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Intracellular localization of CA1P and CA1P phosphatase activity in leaves of Phaseolus vulgaris L.

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CA1P and CA1P phosphatase occur in the chloroplasts of leaf mesophyll cells of many species. However, whether either may occur exclusively in the chloroplast has not yet been established. To examine their intracellular distribution, mature, dark-or light-treated leaves of Phaseolus vulgaris were

Altered lipid A structures and polymyxin hypersensitivity of Rhizobium etli mutants lacking the LpxE and LpxF phosphatases.

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The lipid A of Rhizobium etli, a nitrogen-fixing plant endosymbiont, displays significant structural differences when compared to that of Escherichia coli. An especially striking feature of R. etli lipid A is that it lacks both the 1- and 4'-phosphate groups. The 4'-phosphate moiety of the distal

Characteristics of a photorespiratory mutant of barley (Hordeum vulgare L.) deficient in phosphogly collate phosphatase.

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A barley mutant RPr84/90 has been isolated by selecting for plants which grow poorly in natural air, but normally in air enriched to 0.8% CO2. After 5 minutes of photosynthesis in air containing(14)CO2 this mutant incorporated 26% of the(14)C carbon into phosphoglycollate, a compound not normally

The oligosaccharides of the Fe(III)-Zn(II) purple acid phosphatase of the red kidney bean. Determination of the structure by a combination of matrix-assisted laser desorption/ionization mass spectrometry and selective enzymic degradation.

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Purple acid phosphatase of the common bean Phaseolus vulgaris (KBPase), a dimeric 110-kDa glycoprotein related to the mammalian purple acid phosphatases with a two-metal cluster at the active site contains five oligosaccharide side chains/monomer. The N-linked glycan structures were characterized by

Molecular cloning of the cDNA encoding a stress-inducible protein phosphatase 1 (PP1) catalytic subunit from French bean (Phaseolus vulgaris L.).

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A cDNA showing high sequence similarity (> 70%) to plant protein phosphatase 1 catalytic subunit variants from other species has been isolated from a cDNA library derived from mRNAs expressed in elicitor-treated suspension-cultured cells. The clone appears to be a near full-length 1431 bp with a 172

A single amino acid substitution in soybean VSPalpha increases its acid phosphatase activity nearly 20-fold.

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Soybean [Glycine max (L.) Merr.] contains two proteins called vegetative storage proteins (VSPs) that function as temporary storage reserves, but are also closely related to plant acid phosphatases of the haloacid dehalogenase (HAD) superfamily. This study examined the biochemical basis for the

Unique structural features of red kidney bean purple acid phosphatase.

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Purple acid phosphatase from red kidney beans (Phaseolus vulgaris) has been purified to homogeneity and characterized. The enzyme is a homodimer of 60 kDa subunits each containing one atom of zinc and iron in the active site. Circular dichroism spectral studies on the purified enzyme reveals that a

Characterization of two putative protein phosphatase genes and their involvement in phosphorus efficiency in Phaseolus vulgaris.

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Protein dephosphorylation mediated by protein phosphatases plays a major role in signal transduction of plant responses to environmental stresses. In this study, two putative protein phosphatases, PvPS2:1 and PvPS2:2 were identified and characterized in bean (Phaseolus vulgaris). The two PvPS2

Characterization of a novel acid phosphatase from embryonic axes of kidney bean exhibiting vanadate-dependent chloroperoxidase activity.

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A novel colorless acid phosphatase (KeACP), which was distinct from the kidney bean purple acid phosphatase, was purified to apparent homogeneity and cloned from embryonic axes of kidney bean (Phaseolus vulgaris L. Ohfuku) during germination. When orthovanadate (VO(4)(-3)) is added to the apo form

The major Kurloff cell glycoproteins: lectin affinities, glycosidase susceptibilities and relationship with the sialylated acid phosphatases of the Kurloff body.

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Urea-soluble fractions from purified Kurloff cells (KC) were analysed by affinoblotting. Lectin reactivities were quasi-exclusively confined to the 30-35 kDa major glycoproteins (mGPs) (responsible for the PAS positivity of the Kurloff body) with strong affinities for Canavalia ensiformis lectin,

Specific expression and activity of acid phosphatases in common bean nodules.

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Under phosphorus (P) deficiency, sensitivity of the N 2-fixing legumes increases since the large amount of P-dependent carbon and energy turnover required during N 2 fixation are not satisfied. However, despites the fact that these crops have been widely characterized under P-deficiency and a number

The amino acid sequence of the red kidney bean Fe(III)-Zn(II) purple acid phosphatase. Determination of the amino acid sequence by a combination of matrix-assisted laser desorption/ionization mass spectrometry and automated Edman sequencing.

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Purple acid phosphatase of the common bean Phaseolus vulgaris is a homodimeric 110-kDa glycoprotein with a Fe(III)-Zn(II) center in the active site of each monomer. After exchange of Zn(II) for Fe(II), the enzyme spectroscopically and kinetically resembles the mammalian purple acid phosphatases with

Induction of a major leaf acid phosphatase does not confer adaptation to low phosphorus availability in common bean.

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Acid phosphatase is believed to be important for phosphorus scavenging and remobilization in plants, but its role in plant adaptation to low phosphorus availability has not been critically evaluated. To address this issue, we compared acid phosphatase activity (APA) in leaves of common bean

Effect of vanadate on bean leaf movement, stomatal conductance, barley leaf unrolling, respiration, and phosphatase activity.

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Vanadate (Na(3) VO(4)) inhibits leaf movement and stomatal conductance of Phaseolus vulgaris L. cv. Carlos Favorit in light-dark cycles as well as photomorphogenetic leaf unrolling of Hordeum vulgare L. cv. Rupal. Inhibition was 50% by 10 to 100 micromolar vanadate and 100% by millimolar vanadate.

Regulation of 2-carboxy-D-arabinitol 1-phosphate phosphatase: activation by glutathione and interaction with thiol reagents.

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2-Carboxy-D-arabinitol 1-phosphate (CA1P) phosphatase de- grades CA1P, an inhibitor associated with the regulation of ribulose bisphosphate carboxylase/oxygenase in numerous plant species. CA1P phosphatase purified from Phaseolus vulgaris was partially inactivated by oxidizing conditions during

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