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P1435

Phosphatase, Acid from sweet potato

Name: Phosphatase, Acid from sweet potato
Brand: SIGMA

ammonium sulfate suspension, ≥10.0 units/mg protein (modified Warburg-Christian)

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Synonym(s):

(Orthophosphoric-monoester phosphohydrolase [acid optimum] )

CAS Number:

9001-77-8

Enzyme Commission number:

3.1.3.2 (BRENDA, IUBMB)

EC Number:

232-630-9

MDL number:

MFCD00131847

NACRES:

NA.54

form

ammonium sulfate suspension

Quality Level

300

specific activity

≥10.0 units/mg protein (modified Warburg-Christian)

secondary activity

≤9.9 units/mg protein ATPase

mol wt

110 kDa

storage temp.

2-8°C

InChI

1S/C6H10O2/c1-3-4-8-5-6(2)7/h1,6-7H,4-5H2,2H3

InChI key

GZCWLCBFPRFLKL-UHFFFAOYSA-N

General description

Acid phosphatase from sweet potato is a phosphomonoesterase, which can appear in multiple molecular forms of similar molecular mass but with different isoelectric points.

Application

Potato acid phosphatase is used as a dephosphorylating reagent in thiochrome assays for the detection of thiamin in biological samples. In this assay, it was shown to be more effective than acid phosphatases from wheat germ or α-amylase.

Sweet potato acid phosphatase has been used in a study as a pre-column enzyme reactor via a covalent bond with glutaraldehyde and aminopropyl controlled-pore glass. It has also been used in a study to investigate the use of tyrosine, histidine, and cysteine as ligands for Mn(III) in sweet potato phosphatase.

Biochem/physiol Actions

Acid phosphatases (APase) are a family of enzymes that non-specifically catalyze the hydrolysis of monoesters and anhydrides of phosphoric acid to produce inorganic phosphate at an optimum pH of 4 to 7 by the following reaction: APaseR-PO₄ + H₂O --------------- R-OH + HOPO₃ ²⁺Their function in the production, transport, and recycling of phosphate is critical for the metabolic and energy transduction processes of the cell. As a group, Apases may be as important as kinases in regulatory processes.

Unit Definition

One unit will hydrolyze 1.0 μmole of p-nitrophenyl phosphate per min at pH 4.8 at 37 °C.

Physical form

Suspension in 1.8 M (NH₄)₂SO₄, 10 mM MgCl₂, pH 5.3

Pictograms

GHS08

Signal Word

Danger

Hazard Statements

H334

Precautionary Statements

P261 - P284 - P501

Hazard Classifications

Resp. Sens. 1

Storage Class Code

10 - Combustible liquids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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An unstable manganese(III) complex incorporating ligand donor types proposed for an acid phosphatase from sweet potato: (p-nitrobenzenethiolato)[N,N'-ethylenebis(salicylideneaminato)]manganese(III)

Gohdes, J. and W. Armstrong

Inorganic Chemistry, 27, 1841-1842 (1988)

Selectivity in Enzymatic Phosphorus Recycling from Biopolymers: Isotope Effect, Reactivity Kinetics, and Molecular Docking with Fungal and Plant Phosphatases.

Mina Solhtalab et al.

Environmental science & technology, 56(22), 16441-16452 (2022-10-26)

Among ubiquitous phosphorus (P) reserves in environmental matrices are ribonucleic acid (RNA) and polyphosphate (polyP), which are, respectively, organic and inorganic P-containing biopolymers. Relevant to P recycling from these biopolymers, much remains unknown about the kinetics and mechanisms of different

Purification and characterization of purple acid phosphatase PAP1 from dry powder of sweet potato.

Tatsuya Kusudo et al.

Bioscience, biotechnology, and biochemistry, 67(7), 1609-1611 (2003-08-13)

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

Factors affecting a cyanogen bromide-based assay of thiamin.

D T Wyatt et al.

Clinical chemistry, 35(11), 2173-2178 (1989-11-01)

We analyzed extensively a modified thiochrome method for thiamin analysis. Acid phosphatase (EC 3.1.3.2) from potato was superior to either alpha-amylase or acid phosphatase from wheat germ as a dephosphorylating agent. Timing of cyanogen bromide exposure was important, but the

Mn(III)-containing acid phosphatase. Properties of Fe(III)-substituted enzyme and function of Mn(III) and Fe(III) in plant and mammalian acid phosphatases.

H Kawabe et al.

Biochimica et biophysica acta, 784(1), 81-89 (1984-01-18)

The function of Mn(III) in plant acid phosphatase has been investigated by a metal-substitution study, and some properties of the Fe(III)-substituted enzyme were compared with those of the native Mn(III) enzyme and mammalian Fe(III)-containing acid phosphatases. 19F nuclear magnetic resonance

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