Literature summary for 3.4.11.25 extracted from

Kolesinska, B.; Wasko, J.; Kaminski, Z.; Geueke, B.; Kohler, H.; Seebach, D.
Labeling and protecting N-terminal protein positions by beta-peptidyl aminopeptidase-catalyzed attachment of beta-amino-acid residues - insulin as a first example (2018), Helv. Chim. Acta, 101, e1700259 .

No PubMed abstract available

Search for more literature for 3.4.11.25

Application

Application	Comment	Organism
synthesis	BapA catalyzes reversible protein acylation at the N-terminus. The selective modification can also be applied for protein labeling and tagging and should be generally useful, also to protect peptides and proteins from attack by common aminopeptidase	Sphingosinicella xenopeptidilytica

Organism

Organism	UniProt	Comment	Textmining
Sphingosinicella xenopeptidilytica	Q52VH2	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
insulin + rac-3-aminobutanamide	enatioselectivity for beta-alanine is more than 300:1	Sphingosinicella xenopeptidilytica	?	-	r

Synonyms

Synonyms	Comment	Organism
BapA	-	Sphingosinicella xenopeptidilytica

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)