Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 6.3.1.20 extracted from

  • Hauke, S.; Best, M.; Schmidt, T.T.; Baalmann, M.; Krause, A.; Wombacher, R.
    Two-step protein labeling utilizing lipoic acid ligase and Sonogashira cross-coupling (2014), Bioconjug. Chem., 25, 1632-1637 .
    View publication on PubMed
Search for more literature for 6.3.1.20

Application

Application Comment Organism
synthesis the enzyme can be used for a two-step labeling strategy that combines high selectivity of enzyme-mediated labeling with the chemoselectivity of palladium-catalyzed Sonogashira cross-coupling, overview Escherichia coli

Protein Variants

Protein Variants Comment Organism
additional information the enzyme is used for a two-step labeling procedure for the attachment of various fluorescent probes to a small peptide sequence (13 amino acids) via enzyme-mediated peptide labeling in combination with palladium-catalyzed Sonogashira cross-coupling, method, overview. 4-Iodophenyl derivatives from a small library can be covalently attached to a lysine residue within a specific 13-amino-acid peptide sequence by Escherichia coli lipoic acid ligase A (LplA). The derivatization with 4-iodophenyl subsequently serves as a reactive handle for bioorthogonal transition metal-catalyzed Sonogashira cross-coupling with alkyne-functionalized fluorophores on both the peptide as well as on the protein level Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Synonyms

Synonyms Comment Organism
lipoic acid ligase
-
 Escherichia coli
lipoic acid ligase A
-
 Escherichia coli
LPLA
-
 Escherichia coli