Sources of S-adenosyl-l-homocysteine background in measuring protein arginine N-methyltransferase activity using tandem mass spectrometry

Analytical Biochemistry

Volumn 396, Issue 1, 2010, Pages 158-160

  Lakowski, Ted M ^a   Frankel, Adam ^a  

^a UNIVERSITY OF BRITISH COLUMBIA   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; MASS SPECTROMETRY; PROTEINS;

BACKGROUND SIGNALS; METHYLTRANSFERASE ACTIVITY; METHYLTRANSFERASES; POTENTIAL MECHANISM; PSEUDO-FIRST-ORDER; S ADENOSYL L METHIONINES; TANDEM MASS SPECTROMETRY; ULTRAHIGH PERFORMANCE LIQUID CHROMATOGRAPHY-TANDEM MASS SPECTROMETRIES;

LIQUID CHROMATOGRAPHY;

PROTEIN ARGININE METHYLTRANSFERASE; S ADENOSYLHOMOCYSTEINE;

AMINO ACID SYNTHESIS; ARTICLE; CHEMICAL REACTION; CONTROLLED STUDY; DECOMPOSITION; ENZYME ACTIVITY; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; METHYLATION; PRIORITY JOURNAL; SIGNAL PROCESSING; TANDEM MASS SPECTROMETRY;

EID: 70449633253     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2009.08.043     Document Type: Article

References (7)

1. Wooderchak W.L., Zang T., Zhou Z.S., Acuna M., Tahara S.M., and Hevel J.M. Substrate profiling of PRMT1 reveals amino acid sequences that extend beyond the "RGG" paradigm. Biochemistry 47 (2008) 9456-9466
2. Frankel A., Yadav N., Lee J., Branscombe T.L., Clarke S., and Bedford M.T. The novel human protein arginine N-methyltransferase PRMT6 is a nuclear enzyme displaying unique substrate specificity. J. Biol. Chem. 277 (2002) 3537-3543
3. Lakowski T.M., and Frankel A. Kinetic analysis of human protein arginine N-methyltransferase 2: formation of monomethyl- and asymmetric dimethylarginine residues on histone H4. Biochem. J. 421 (2009) 253-261
4. Tang J., Gary J.D., Clarke S., and Herschman H.R. PRMT 3, a type I protein arginine N-methyltransferase that differs from PRMT1 in its oligomerization, subcellular localization, substrate specificity, and regulation. J. Biol. Chem. 273 (1998) 16935-16945
5. Lakowski T.M., and Frankel A. A kinetic study of human protein arginine N-methyltransferase 6 reveals a distributive mechanism. J. Biol. Chem. 283 (2008) 10015-10025
6. Parks L.W., and Schlenk F. The stability and hydrolysis of S-adenosylmethionine: isolation of S-ribosylmethionine. J. Biol. Chem. 230 (1958) 295-305
7. Wu S.E., Huskey W.P., Borchardt R.T., and Schowen R.L. Chiral instability at sulfur of S-adenosylmethionine. Biochemistry 22 (1983) 2828-2832