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sweet potato/phosphatase
Odkaz sa uloží do schránky
Strana 1 od 49 výsledky
A purple acid phosphatase from sweet potato contains an antiferromagnetically coupled binuclear Fe-Mn center.
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A purple acid phosphatase from sweet potato is the first reported example of a protein containing an enzymatically active binuclear Fe-Mn center. Multifield saturation magnetization data over a temperature range of 2 to 200 K indicates that this center is strongly antiferromagnetically coupled.
Purification and characterization of purple acid phosphatase PAP1 from dry powder of sweet potato.
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Purple acid phosphatase (PAP) was purified from sweet potato dry powder, which is used as a food additive. Spectrometric and enzymatic analyses, and analysis of the amino-terminal sequence indicated that the purified purple acid phosphatase was PAP1. High activity in neutral and acidic conditions,
Phosphate forms an unusual tripodal complex with the Fe-Mn center of sweet potato purple acid phosphatase.
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Purple acid phosphatases (PAPs) are a family of binuclear metalloenzymes that catalyze the hydrolysis of phosphoric acid esters and anhydrides. A PAP in sweet potato has a unique, strongly antiferromagnetically coupled Fe(III)-Mn(II) center and is distinguished from other PAPs by its increased
Crystallization and preliminary X-ray diffraction data for a purple acid phosphatase from sweet potato.
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Purple acid phosphatase from sweet potato is a homodimer of 110 kDa. Two forms of the enzyme have been characterized. One contains an Fe-Zn centre similar to that previously reported for red kidney bean purple acid phosphatase. Another isoform, the subject of this work, is the first confirmed
Sweet potato acid phosphatase immobilized on glutaraldehyde-activated aminopropyl controlled-pore glass: activation, repeated use and enzyme fatigue.
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Sweet potato acid phosphatase was covalently coupled with glutaraldehyde to aminopropyl controlled-pore glass, and used as a pre-column enzyme reactor. The immobilized enzyme reactor (IMER) was continuously operated using an automated chromatographic detection system we developed. Functional
An arsenate reductase homologue possessing phosphatase activity from sweet potato (Ipomoea batatas [L.] Lam): kinetic studies and characterization.
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A cDNA encoding a putative arsenate reductase homologue (IbArsR) was cloned from sweet potato (Ib). The deduced protein showed a high level of sequence homology (16-66%) with ArsRs from other organisms. A 3-D homology structure was created based on AtArsR (PDB code 1T3K ) from Arabidopsis thaliana.
Type 2C protein phosphatase ABI1 is a negative regulator of strawberry fruit ripening.
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Although a great deal of progress has been made toward understanding the role of abscisic acid (ABA) in fruit ripening, many components in the ABA signalling pathway remain to be elucidated. Here, a strawberry gene homologous to the Arabidopsis gene ABI1, named FaABI1, was isolated and
Hybrid-DFT study on electronic structures of the active site of sweet potato purple acid phosphatase: the origin of stronger antiferromagnetic couplings than other purple acid phosphatases.
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The electronic structure and magnetic interactions of the active site of sweet potato purple acid phosphatase (PAP) were investigated by using UHF, pure DFT (UBLYP), and hybrid DFT methods (UB3LYP and UB2LYP). PAP catalyzes the hydrolysis of a phosphate ester under acidic conditions and contains a
Binuclear metal centers in plant purple acid phosphatases: Fe-Mn in sweet potato and Fe-Zn in soybean.
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Purple acid phosphatases comprise a family of binuclear metal-containing acid hydrolases, representatives of which have been found in animals, plants, and fungi. The goal of this study was to characterize purple acid phosphatases from sweet potato tubers and soybean seeds and to establish their
Metal-ion mutagenesis: conversion of a purple acid phosphatase from sweet potato to a neutral phosphatase with the formation of an unprecedented catalytically competent Mn(II)Mn(II) active site.
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The currently accepted paradigm is that the purple acid phosphatases (PAPs) require a heterovalent, dinuclear metal-ion center for catalysis. It is believed that this is an essential feature for these enzymes in order for them to operate under acidic conditions. A PAP from sweet potato is unusual in
Recombinant purple acid phosphatase isoform 3 from sweet potato is an enzyme with a diiron metal center.
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Purple acid phosphatases (PAPs) from sweet potato (sp) have been classified on the basis of their primary structure and the dinuclear metal center into isoforms spPAP1 [Fe(III)-Zn(II)] and spPAP2 [Fe(III)-Mn(II)]; for spPAP3 only the cDNA is known. With the aim of unraveling the character of the
The presence of essential histidine residues in manganese(III)-containing acid phosphatase from sweet potato.
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Chemical modification studies of manganese(III)-containing acid phosphatase [EC 3.1.3.2] were carried out to investigate the contributions of specific amino-acid side-chains to the catalytic activity. Incubation of the enzyme with N-ethylmaleimide at pH 7.0 caused a significant loss of the enzyme
Synthesis, structure, properties, and phosphatase-like activity of the first heterodinuclear Fe(III)Mn(II) complex with the unsymmetric ligand H(2)BPBPMP as a model for the PAP in sweet potato.
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The new heterodinuclear mixed valence complex [Fe(III)Mn(II)(BPBPMP)(OAc)(2)]ClO(4) (1) with the unsymmetrical N(5)O(2) donor ligand 2-bis[((2-pyridylmethyl)-aminomethyl)-6-((2-hydroxybenzyl)(2-pyridylmethyl))-aminomethyl]-4-methylphenol (H(2)BPBPMP) has been synthesized and characterized. Compound
Isolation of violet-colored acid phosphatase from sweet potato.
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Studies on violet-colored acid phosphatase of sweet potato. I. Purification and some physical properties.
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