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An enzyme(s) that converts glutaminyl-peptides into pyroglutamyl-peptides. Presence in pituitary, brain, adrenal medulla, and lymphocytes.
Open accessAbstract
The mechanism for the post-translational conversion of glutamine to pyroglutamic acid on the N terminus of newly synthesized peptides and proteins is unknown. An assay is reported that permits measurement of the rate of conversion of Gln-His-Pro-NH2 to pyroGlu-His-Pro-NH2 (TRH). Using this assay, we demonstrate that the spontaneous cyclization of the N-terminal glutamine of this peptide occurs only slowly under physiological conditions. Furthermore, we describe the presence in rat brain, porcine pituitary, and human B lymphocytes of an enzyme(s) which converts Gln-His-Pro-NH2 into pyroGlu-His-Pro-NH2. The enzyme(s) appears to be a glycoprotein, is maximally active at neutral pH, has a Mr of 55,000, and contains catalytically significant sulfhydryl groups. The product of the enzymatic reaction was confirmed by high resolution fast atom bombardment-mass spectrometry. In preliminary studies, we find that over 90% of the enzyme in bovine adrenal medulla is contained in the soluble chromaffin vesicle fraction. These findings indicate that in vivo the post-translational conversion of a glutaminyl-peptide into a pyroglutamyl-peptide is neither spontaneous nor abiotic as has been previously proposed.
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Cited by
Sakurai, T., Amemiya, A., Ishii, M., Matsuzaki, I., Chemelli, R. M., Tanaka, H., Williams, S. C., Richardson, J. A., Kozlowski, G. P., Wilson, S., et al. (1998) · Cell · doi:10.1016/s0092-8674(00)80949-6 · Cited by 5,501
Payne, C. M., Knott, B. C., Mayes, H. B., Hansson, H., Himmel, M. E., Sandgren, M., Ståhlberg, J., & Beckham, G. T. (2015) · Chemical Reviews · doi:10.1021/cr500351c · Cited by 855
On the Seeding and Oligomerization of pGlu-Amyloid Peptides (in vitro)
Schilling, S., Lauber, T., Schaupp, M., Manhart, S., Scheel, E., Böhm, G., & Demuth, H.-U. (2006) · Biochemistry · doi:10.1021/bi0612667 · Cited by 254
Tomidokoro, Y., Lashley, T., Rostagno, A., Neubert, T. A., Bojsen-Møller, M., Braendgaard, H., Plant, G., Holton, J., Frangione, B., Révész, T., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m504038200 · Cited by 68
Genetic Alterations of the BRI2 gene: Familial British and Danish Dementias
J, G., A, R., Y, T., T, L., M, B.-M., H, B., G, P., J, H., R, L., T, R., et al. (2006) · Brain Pathology · doi:10.1111/j.1750-3639.2006.tb00563.x · Cited by 44
Metadata
- Authors
- Busby, W. H., Quackenbush, G. E., Humm, J., Youngblood, W. W., & Kizer, J. S.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1987-06
- Volume
- 262
- Issue
- 18
- Pages
- 8532-8536
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1516427878
- Cited by
- 186
- References
- 0
- FWCI
- 3.89
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- CoChat. (2026). Citation check: An enzyme(s) that converts glutaminyl-peptides into pyroglutamyl-peptides. Presence in pituitary, brain, adrenal medulla, and lymphocytes. https://app.cochat.ai/papers/10.1016/s0021-9258(18)47446-7
- The paper
- Busby, W. H., Quackenbush, G. E., Humm, J., Youngblood, W. W., & Kizer, J. S. (1987). An enzyme(s) that converts glutaminyl-peptides into pyroglutamyl-peptides. Presence in pituitary, brain, adrenal medulla, and lymphocytes. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)47446-7
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