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BRENDA No.
Title
Journal
Volume
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PubMed ID
3.4.11.25
708080
Enzyme-catalyzed formation of beta-peptides: beta-peptidyl aminopeptidases BapA and DmpA acting as beta-peptide-synthesizing enzymes
Chem. Biodivers.
4
2016-2030
2007
Sphingosinicella microcystinivorans
17886858
3.4.11.25
708080
Enzyme-catalyzed formation of beta-peptides: beta-peptidyl aminopeptidases BapA and DmpA acting as beta-peptide-synthesizing enzymes
Chem. Biodivers.
4
2016-2030
2007
Sphingosinicella xenopeptidilytica
17886858
3.4.11.25
708080
Enzyme-catalyzed formation of beta-peptides: beta-peptidyl aminopeptidases BapA and DmpA acting as beta-peptide-synthesizing enzymes
Chem. Biodivers.
4
2016-2030
2007
Sphingosinicella xenopeptidilytica 3-2W4
17886858
3.4.11.25
708080
Enzyme-catalyzed formation of beta-peptides: beta-peptidyl aminopeptidases BapA and DmpA acting as beta-peptide-synthesizing enzymes
Chem. Biodivers.
4
2016-2030
2007
Sphingosinicella microcystinivorans Y2
17886858
3.4.11.25
731203
Mutation of active site serine residue with cysteine displays change in acyl-acceptor preference of beta-peptidyl aminopeptidase from Pseudomonas aeruginosa PAO1
Appl. Microbiol. Biotechnol.
98
1631-1640
2014
Pseudomonas aeruginosa
23728237
3.4.11.25
753761
Labeling and protecting N-terminal protein positions by beta-peptidyl aminopeptidase-catalyzed attachment of beta-amino-acid residues - insulin as a first example
Helv. Chim. Acta
101
e1700259
2018
Sphingosinicella xenopeptidilytica
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