Carbamylation of N-Terminal Proline
نویسندگان
چکیده
منابع مشابه
N-terminal carbamylation of the hyaluronic acid-binding region and the link protein from the chondrosarcoma proteoglycan aggregate.
The ternary complex consisting of a 65-kDa peptide originating from the proteoglycan core protein and a 43-kDa link protein bound to hyaluronic acid was purified from a clostripain digest of the rat chondrosarcoma aggregating proteoglycan and 14C-carbamylated with potassium [14C]cyanate. At a pH of 8.0, 14C-carbamylation of the alpha-NH2 groups in the N-terminal amino acids was favored over car...
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Proline dehydrogenase (ProDH) is a ubiquitous flavoenzyme that catalyzes the oxidation of proline to Δ¹-pyrroline-5-carboxylate. Thermus thermophilus ProDH (TtProDH) contains in addition to its flavin-binding domain an N-terminal arm, consisting of helices αA, αB, and αC. Here, we report the biochemical properties of the helical arm truncated TtProDH variants ΔA, ΔAB, and ΔABC, produced with ma...
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To probe the structural implications of the proline residue on its characteristic peptide fragmentation patterns, in particular its unusual cleavage at its C-terminus in formation of a b(2) ion in XxxProZzz sequences, the structures of a series of proline-containing b(2)(+) ions were studied by using action infrared multiphoton dissociation (IRMPD) spectroscopy and fragment ion hydrogen-deuteri...
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The N-terminal Src homology 3 (nSH3) domain of a signaling adaptor protein, CT-10 regulator of kinase II (CrkII), recognizes proline-rich motifs (PRMs) of binding partners, such as cAbl kinase. The interaction between CrkII and cAbl kinase is involved in the regulation of cell spreading, microbial pathogenesis, and cancer metastasis. Here, we report the detailed biophysical characterizations of...
متن کاملCleavage N-terminal to proline: analysis of a database of peptide tandem mass spectra.
Fragmentation at the Xxx-Pro bond was analyzed for a group of peptide mass spectra that were acquired in a Finnigan ion trap mass spectrometer and were generated from proteins digested by enzymes and identified by the Sequest algorithm. Cleavage with formation of a + b + y ions occurred more readily at the Xxx-Pro bond than at other locations in these peptides, and the importance of this cleava...
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ژورنال
عنوان ژورنال: ACS Medicinal Chemistry Letters
سال: 2010
ISSN: 1948-5875,1948-5875
DOI: 10.1021/ml100046d