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Glycine N-methyltransferase, aa1-295, Recombinant, Human (GNMT)

Cat no: G8166-50C

Glycine N-methyltransferase, aa1-295, Recombinant, Human (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.\n\nSource: \nRecombinant corresponding to aa1-295 from human Glycine N-methyltransferase/GNMT, expressed in E. coli.\n\nMolecular Weight: \n~33kD\n\nEndotoxin Level:\n(same/less than)1EU/1ug (LAL)\n\nBiological Activity:\nMeasured by its ability to transfer a methyl group from S-adenosylmethionine to glycine.\nThe specific activity is >190pmoles/min/ug.\n\nStorage and Stability:\nAliquot to avoid repeated freezing and thawing and store at -70 degrees C. Aliquots are stable for at least 6 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.

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SPECIFICATIONS

Catalog Number

G8166-50C

Size

10ug

Form

Supplied as a liquid in sodium dihydrogen phosphate, sodium chloride, glycerol.

Purity

~95% (SDS-PAGE)

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.

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