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Protein Methylase I
Open accessAbstract
Abstract An enzyme, methylase I, which methylates its endogenous protein has been purified from calf thymus. Acid hydrolysis of the methylated endogenous protein gives rise to two methylated amino acid derivatives. Both derivatives are very sensitive to alkali treatment, and one of the decomposition products is identified as methylurea. These findings, as well as other evidence, indicate that one of the compounds is guanidino-methylated arginine and the other is α-amino-, guanidino-methylated arginine. Various histones comprise approximately 70% of the total endogenous methylated protein, and the radioactivity is widely distributed among the various histones when the enzyme is labeled with S-adenosyl-l-methionine-methyl-14C. Protein methylase I has a pH optimum of 7.4 and a Km of 2.1 x 10-5 m for S-adenosyl-l-methionine.
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Citations
Cited by
Schug, K. A., & Lindner, W. (2005) · Chemical Reviews · doi:10.1021/cr040603j · Cited by 579
Biological significance of endogenous methylarginines that inhibit nitric oxide synthases
Leiper, J. (1999) · Cardiovascular Research · doi:10.1016/s0008-6363(99)00162-5 · Cited by 458
Role of Protein Methylation in Regulation of Transcription
Lee, D. Y., Teyssier, C., Strahl, B. D., & Stallcup, M. R. (2005) · Endocrine Reviews · doi:10.1210/er.2004-0008 · Cited by 455
Metadata
- Authors
- Paik, W. K., & Kim, S.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1968-05
- Volume
- 243
- Issue
- 9
- Pages
- 2108-2114
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1492953040
- Cited by
- 208
- References
- 0
- FWCI
- 5.64
- Type
- journal article
- Language
- en
- Open access
- hybrid
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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