Recombinant Human Glycine N-methyltransferase/GNMT, CF

R&D Systems, part of Bio-Techne | Catalog # 6526-MT

R&D Systems, part of Bio-Techne
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6526-MT-010
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Key Product Details

Source

E. coli

Accession #

Q14749

Conjugate

Unconjugated

Applications

Enzyme Activity

View all Glycine N-Methyltransferase/GNMT Proteins and Enzymes »

Product Specifications

Source

E. coli-derived human Glycine N-Methyltransferase/GNMT protein
Met1-Asp295

Purity

>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.

Endotoxin Level

<1.0 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

Val2

Predicted Molecular Mass

33 kDa

SDS-PAGE

31-35 kDa, reducing conditions

Activity

Measured by its ability to transfer a methyl group from S-adenosylmethionine to glycine.
The specific activity is >190 pmol/min/μg.

Formulation, Preparation and Storage

6526-MT
Formulation Supplied as a 0.2 μm filtered solution in NaH2PO4, NaCl and Glycerol.
Shipping The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -70 °C as supplied.
  • 3 months, -70 °C under sterile conditions after opening.

Background: Glycine N-Methyltransferase/GNMT

Glycine N-methyltransferase (GNMT) is a tetrameric cytosolic protein which catalyzes the transfer of a methyl group from S-adenosylmethionine (AdoMet) to glycine producing S-adenosylhomocysteine (AdoHcy) and sarcosine (1). GNMT plays a major role in maintaining normal AdoMet levels. GNMT is abundant in the liver where it is a major folate-binding protein. It binds 5-methyltetrahydrofolate pentaglutamate in vivo and in vitro, and the binding of the folate inhibits the activity of GNMT. A study of the rat enzyme showed differences in the kinetic parameters between recombinant GNMT and the protein isolated from liver (2). Based on structural information, the N-terminal part of the protein plays a major role in the transfer of the methyl group from AdoMet to glycine (3). It has been proposed that the difference in folate inhibitor binding between recombinant GNMT and the liver enzyme may be due to differential acetylation of the N-terminal valine (4). Hypermethioninemia is caused by defects in GNMT.

References

  1. Luka, Z. et al. (2009) J. Biol. Chem. 284:22507.
  2. Ogawa, H. et al. (1997) Biochem. J. 327:407.
  3. Takata, Y. et al. (2003) Biochemistry. 42:8394.
  4. Luka, Z. et al. (2008) Biochim. Biophys. Acta. 1784:1342.

Alternate Names

Glycine NMethyltransferase, GNMT

Entrez Gene IDs

27232 (Human); 14711 (Mouse); 25134 (Rat)

Gene Symbol

GNMT

UniProt

Q14749 (Human)

Additional Glycine N-Methyltransferase/GNMT Products

Product Documents for Recombinant Human Glycine N-methyltransferase/GNMT, CF

Product Datasheets

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Product Specific Notices for Recombinant Human Glycine N-methyltransferase/GNMT, CF

For research use only

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