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Literature summary for 3.4.11.25 extracted from

  • Heck, T.; Kohler, H.P.; Limbach, M.; Fl๖gel, O.; Seebach, D.; Geueke, B.
    Enzyme-catalyzed formation of beta-peptides: beta-peptidyl aminopeptidases BapA and DmpA acting as beta-peptide-synthesizing enzymes (2007), Chem. Biodivers., 4, 2016-2030.
    View publication on PubMed

Application

Application Comment Organism
synthesis attachment of a beta-amino acid to the N-terminus of a natural alpha-peptide. N-terminal beta-amino acid residues may be considered as protective groups against proteolytic enzymes in vitro and in vivo Sphingosinicella xenopeptidilytica
synthesis attachment of a beta-amino acid to the N-terminus of a natural alpha-peptide. N-terminal beta-amino acid residues may be considered as protective groups against proteolytic enzymes in vitro and in vivo Sphingosinicella microcystinivorans

Organism

Organism UniProt Comment Textmining
Sphingosinicella microcystinivorans A0MTQ2
-
-
Sphingosinicella microcystinivorans Y2 A0MTQ2
-
-
Sphingosinicella xenopeptidilytica Q52VH2
-
-
Sphingosinicella xenopeptidilytica 3-2W4 Q52VH2
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information in the reverse direction the enzyme catalyzes the oligomerization of beta-amino acids and the synthesis of mixed peptides with N-terminal beta-amino acid residues. As substrates the beta-homoamino acid derivatives beta-Ala-p-nitroanilide, beta-homoAla-p-nitroanilide, (R)-beta-homoAla-p-nitroanilide, beta-homoPhe-p-nitroanilide, (R)-beta-homoPhe-p-nitroanilide, and beta-homoLeu-p-nitroanilide are utilized Sphingosinicella microcystinivorans ?
-
?
additional information in the reverse reaction the enzyme catalyzes the oligomerization of beta-amino acids and the synthesis of mixed peptides with N-terminal beta-amino acid residues. As substrates the beta-homoamino acid derivatives beta-Ala-p-nitroanilide, beta-homoAla-p-nitroanilide, (R)-beta-homoAla-p-nitroanilide, beta-homoPhe-p-nitroanilide, (R)-beta-homoPhe-p-nitroanilide, and beta-homoLeu-p-nitroanilide are utilized Sphingosinicella xenopeptidilytica ?
-
?
additional information in the reverse reaction the enzyme catalyzes the oligomerization of beta-amino acids and the synthesis of mixed peptides with N-terminal beta-amino acid residues. As substrates the beta-homoamino acid derivatives beta-Ala-p-nitroanilide, beta-homoAla-p-nitroanilide, (R)-beta-homoAla-p-nitroanilide, beta-homoPhe-p-nitroanilide, (R)-beta-homoPhe-p-nitroanilide, and beta-homoLeu-p-nitroanilide are utilized Sphingosinicella xenopeptidilytica 3-2W4 ?
-
?
additional information in the reverse direction the enzyme catalyzes the oligomerization of beta-amino acids and the synthesis of mixed peptides with N-terminal beta-amino acid residues. As substrates the beta-homoamino acid derivatives beta-Ala-p-nitroanilide, beta-homoAla-p-nitroanilide, (R)-beta-homoAla-p-nitroanilide, beta-homoPhe-p-nitroanilide, (R)-beta-homoPhe-p-nitroanilide, and beta-homoLeu-p-nitroanilide are utilized Sphingosinicella microcystinivorans Y2 ?
-
?

Synonyms

Synonyms Comment Organism
3-2W4 BapA
-
Sphingosinicella xenopeptidilytica
Y2 BapA
-
Sphingosinicella microcystinivorans