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Tytuł:
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Flow-based enzymatic ligation by sortase A.
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Autorzy:
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Policarpo RL; Department of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139 (USA).
Kang H
Liao X
Rabideau AE
Simon MD
Pentelute BL
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Źródło:
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Angewandte Chemie (International ed. in English) [Angew Chem Int Ed Engl] 2014 Aug 25; Vol. 53 (35), pp. 9203-8. Date of Electronic Publication: 2014 Jul 02.
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Typ publikacji:
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Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.
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Język:
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English
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Imprint Name(s):
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Publication: <2004-> : Weinheim : Wiley-VCH
Original Publication: Weinheim/Bergstr. : New York, : Verlag Chemie ; Academic Press, c1962-
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MeSH Terms:
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Aminoacyltransferases/*metabolism
Bacterial Proteins/*metabolism
Cysteine Endopeptidases/*metabolism
Enzymes, Immobilized/*metabolism
Proteins/*chemistry
Proteins/*metabolism
Models, Molecular ; Molecular Structure
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Contributed Indexing:
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Keywords: flow chemistry; immobilization; microreactor; protein modification; sortase A
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Substance Nomenclature:
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0 (Bacterial Proteins)
0 (Enzymes, Immobilized)
0 (Proteins)
EC 2.3.2.- (Aminoacyltransferases)
EC 2.3.2.- (sortase A)
EC 3.4.22.- (Cysteine Endopeptidases)
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Entry Date(s):
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Date Created: 20140704 Date Completed: 20150601 Latest Revision: 20180126
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Update Code:
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20240104
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DOI:
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10.1002/anie.201403582
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PMID:
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24989829
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Sortase-mediated ligation (sortagging) is a versatile, powerful strategy for protein modification. Because the sortase reaction reaches equilibrium, a large excess of polyglycine nucleophile is often employed to drive the reaction forward and suppress sortase-mediated side reactions. A flow-based sortagging platform employing immobilized sortase A within a microreactor was developed that permits efficient sortagging at low nucleophile concentrations. The platform was tested with several reaction partners and used to generate a protein bioconjugate inaccessible by solution-phase batch sortagging.
(© 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.)