Zobrazeno 1 - 7
of 7
pro vyhledávání: '"M G, Kopczynski"'
Publikováno v:
Journal of Biological Chemistry. 265:8001-8008
Biologically active peptides are initially synthesized in the form of protein precursors, and the peptides are liberated by post-translational processing from the precursors in a tissue-specific manner. Mammalian proglucagon, which is synthesized in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e9624439cbd38829862d21d6fbffa604
https://doi.org/10.1016/s0021-9258(19)39030-1
https://doi.org/10.1016/s0021-9258(19)39030-1
Publikováno v:
The Journal of biological chemistry. 265(14)
Biologically active peptides are initially synthesized in the form of protein precursors, and the peptides are liberated by post-translational processing from the precursors in a tissue-specific manner. Mammalian proglucagon, which is synthesized in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::73a127f39a07c9492654c7cb7c60db75
https://pubmed.ncbi.nlm.nih.gov/1692320
https://pubmed.ncbi.nlm.nih.gov/1692320
Publikováno v:
Journal of Biological Chemistry. 260:16131-16136
Ethanolamine ammonia-lyase catalyzes the adenosylcobalamin (AdoCbl)-dependent conversion of ethanolamine to acetaldehyde and ammonia. During this reaction, a hydrogen atom migrates from the carbinol carbon of ethanolamine to the methyl carbon of acet
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::689a3f04f8ac05b1740e611e2f3c9e73
https://doi.org/10.1016/s0021-9258(17)36210-5
https://doi.org/10.1016/s0021-9258(17)36210-5
Autor:
M. G. Kopczynski, William H. Orme-Johnson, William W. Bachovchin, Swee Lian Tan, B. M. Babior
Publikováno v:
Journal of Biological Chemistry. 261:3483-3485
During the deamination of S-2-aminopropanol by the AdoCbl-dependent ethanolamine ammonia-lyase of Clostridia sp., a catalytic intermediate accumulates whose active site contains two paramagnetic species: cob(II)alamin and a free radical derived from
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d3c013dba0a57feac7f54950b0e5e0fa
https://doi.org/10.1016/s0021-9258(17)35673-9
https://doi.org/10.1016/s0021-9258(17)35673-9
Autor:
M G Kopczynski, B M Babior
Publikováno v:
Journal of Biological Chemistry. 259:7652-7654
Ethanolamine ammonia-lyase is an adenosylcobalamin-dependent enzyme that catalyzes the rearrangement of ethanolamine and other vicinal amino alcohols to oxo-compounds and ammonia. Treatment of this enzyme with the sulfhydryl group-blocking reagent me
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6bfd421924f1733c44e0ddb57dde6913
https://doi.org/10.1016/s0021-9258(17)42841-9
https://doi.org/10.1016/s0021-9258(17)42841-9
Publikováno v:
The Journal of biological chemistry. 260(30)
Ethanolamine ammonia-lyase catalyzes the adenosylcobalamin (AdoCbl)-dependent conversion of ethanolamine to acetaldehyde and ammonia. During this reaction, a hydrogen atom migrates from the carbinol carbon of ethanolamine to the methyl carbon of acet
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::ae3bd5d9181b7fa44732d9e37499322d
https://pubmed.ncbi.nlm.nih.gov/3905806
https://pubmed.ncbi.nlm.nih.gov/3905806
Publikováno v:
The Journal of biological chemistry. 261(8)
During the deamination of S-2-aminopropanol by the AdoCbl-dependent ethanolamine ammonia-lyase of Clostridia sp., a catalytic intermediate accumulates whose active site contains two paramagnetic species: cob(II)alamin and a free radical derived from
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::1c32c61574ec9e73f97d9472cbd2f6f7
https://pubmed.ncbi.nlm.nih.gov/3949775
https://pubmed.ncbi.nlm.nih.gov/3949775