AS3MT Human

Arsenic Methyltransferase Human Recombinant
Cat. No.
BT2709
Source
Escherichia Coli.
Synonyms
Arsenite methyltransferase, Methylarsonite methyltransferase, S-adenosyl-L-methionine:arsenic(III) methyltransferase, AS3MT, CYT19, RP11-753C18.6.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

AS3MT Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 399 amino acids (1-375 a.a.) and having a molecular mass of 44.3kDa.
AS3MT is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Arsenic Methyltransferase (AS3MT) is an enzyme that plays a crucial role in arsenic metabolism. It facilitates the transfer of a methyl group from S-adenosyl-L-methionine (AdoMet) to trivalent arsenical. AS3MT catalyzes the methylation of arsenite to produce methylarsonate (Me-AsO3H2), which is subsequently reduced to methylarsonite (Me-As(OH)2) by methylarsonate reductase. Methylarsonite, also a substrate for AS3MT, undergoes further transformation into the significantly less toxic compound dimethylarsinate (cacodylate) (Me2As(O)-OH).
Description
Recombinant human AS3MT, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 399 amino acids, with amino acids 1 to 375 representing the AS3MT sequence, and has a molecular weight of 44.3 kDa. The protein is fused to a 24 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
The AS3MT protein is supplied in a solution at a concentration of 1 mg/ml. The solution also contains 20 mM Tris-HCl buffer (pH 8.0), 10% glycerol, and 0.15 M NaCl.
Stability
For short-term storage (up to 2-4 weeks), the product can be stored at 4°C. For extended storage, it is recommended to freeze the product at -20°C. To ensure long-term stability during frozen storage, it is advisable to add a carrier protein such as HSA or BSA to a final concentration of 0.1%. Avoid repeated freeze-thaw cycles to maintain protein integrity.
Purity
The purity of the AS3MT protein is greater than 90.0%, as determined by SDS-PAGE analysis.
Synonyms
Arsenite methyltransferase, Methylarsonite methyltransferase, S-adenosyl-L-methionine:arsenic(III) methyltransferase, AS3MT, CYT19, RP11-753C18.6.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMAALRD AEIQKDVQTY YGQVLKRSAD LQTNGCVTTA RPVPKHIREA LQNVHEEVAL RYYGCGLVIP EHLENCWILD LGSGSGRDCY VLSQLVGEKG HVTGIDMTKG QVEVAEKYLD YHMEKYGFQA SNVTFIHGYI EKLGEAGIKN ESHDIVVSNC
VINLVPDKQQ VLQEAYRVLK HGGELYFSDV YTSLELPEEI RTHKVLWGEC LGGALYWKEL AVLAQKIGFC PPRLVTANLI TIQNKELERV IGDCRFVSAT FRLFKHSKTG PTKRCQVIYN GGITGHEKEL MFDANFTFKE GEIVEVDEET AAILKNSRFA QDFLIRPIGE KLPTSGGCSA
LELKDIITDP FKLAEESDSM KSRCVPDAAG GCCGTKKSC.

Product Science Overview

Introduction

Arsenic methyltransferase, also known as arsenite methyltransferase (AS3MT), is an enzyme that plays a crucial role in the biomethylation of arsenic. This enzyme is responsible for the conversion of inorganic arsenic into its methylated forms, which are generally less toxic and more easily excreted from the body. The human recombinant form of this enzyme is often used in research to study its structure, function, and role in arsenic metabolism.

Structure and Function

The human AS3MT gene encodes a protein consisting of 375 amino acids with a molecular weight of approximately 41.7 kDa . This enzyme contains several cysteine residues that are essential for its catalytic activity. The cysteine residues form disulfide bonds, which are crucial for the enzyme’s function. For instance, the disulfide bond between Cys250 and Cys32 is reduced by glutathione (GSH) or other reductants before the enzymatic methylation of arsenite .

Catalytic Mechanism

AS3MT catalyzes the transfer of a methyl group from S-adenosyl-L-methionine (AdoMet) to arsenic, producing monomethyl and dimethyl arsenicals . The enzyme’s active site binds to arsenite (iAs^3+) and facilitates its methylation. The methylation process involves the formation of intermediate complexes, such as Cys250-S-adenosylhomocysteine (AdoHcy), which suggests that Cys250 is involved in the transmethylation process .

Importance in Arsenic Detoxification

Arsenic is a ubiquitous environmental contaminant that poses significant health risks. The methylation of arsenic by AS3MT is a critical detoxification pathway that reduces the toxicity of arsenic and enhances its excretion. The methylated forms of arsenic, such as monomethylarsonic acid (MMA) and dimethylarsinic acid (DMA), are less toxic and more water-soluble, facilitating their elimination from the body.

Research and Applications

Recombinant human AS3MT is widely used in research to understand the molecular mechanisms of arsenic methylation and its implications for human health. Studies have shown that mutations in the AS3MT gene can affect the enzyme’s activity and influence an individual’s susceptibility to arsenic toxicity . Additionally, research on AS3MT has provided insights into the role of glutathione and other reductants in the methylation process .

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