Investigation into isomerization reaction of phenylalanine aminomutase from Pantoea agglomerans.
NH(2)-H pair exchange pathway
Pantoea agglomerans
Phenylalanine aminomutase
Reaction mechanism
Journal
Enzyme and microbial technology
ISSN: 1879-0909
Titre abrégé: Enzyme Microb Technol
Pays: United States
ID NLM: 8003761
Informations de publication
Date de publication:
Jan 2020
Jan 2020
Historique:
received:
07
07
2019
revised:
30
08
2019
accepted:
10
09
2019
entrez:
17
11
2019
pubmed:
17
11
2019
medline:
10
4
2020
Statut:
ppublish
Résumé
Phenylalanine aminomutase (PaPAM) from Pantoea agglomerans is a member of the MIO (4-methylene-imidazol-5-one) family of enzymes, which isomerizes α-phenylalanine to β-phenylalanine, and could be used to synthesize unnatural β-arylalanine. However, the mechanism of isomerization reaction is not clear. To investigate the mechanism, the gene (pam), which encodes PaPAM, was first expressed in E.coli, and recombinant PaPAM was prepared using affinity chromatography. Then,
Identifiants
pubmed: 31731949
pii: S0141-0229(19)30166-8
doi: 10.1016/j.enzmictec.2019.109428
pii:
doi:
Substances chimiques
Bacterial Proteins
0
Phenylalanine
47E5O17Y3R
Hydrogen
7YNJ3PO35Z
Intramolecular Transferases
EC 5.4.-
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
109428Informations de copyright
Copyright © 2019 Elsevier Inc. All rights reserved.