Structural characterization and Kemp eliminase activity of the Mycobacterium smegmatis Ketosteroid Isomerase.
Crystal structure
Kemp elimination
MsKSI
Mycobacterium smegmatis
Journal
Biochemical and biophysical research communications
ISSN: 1090-2104
Titre abrégé: Biochem Biophys Res Commun
Pays: United States
ID NLM: 0372516
Informations de publication
Date de publication:
30 06 2021
30 06 2021
Historique:
received:
03
05
2021
accepted:
04
05
2021
pubmed:
17
5
2021
medline:
27
8
2021
entrez:
16
5
2021
Statut:
ppublish
Résumé
The Kemp elimination reaction, involving the ring-opening of benzoxazole and its derivatives under the action of natural enzymes or chemical catalysts, has been of interest to researchers since its discovery. Because this reaction does not exist in all currently known metabolic pathways, the computational design of Kemp eliminases has provided valuable insights into principles of enzymatic catalysis. However, it was discovered that the naturally occurring promiscuous enzymes ydbC, xapA and ketosteroid isomerase also can catalyze Kemp elimination. Here, we report the crystal structure of ketosteroid isomerase (KSI) from Mycobacterium smegmatis MC2 155. MsKSI crystallizes in the P2
Identifiants
pubmed: 33992958
pii: S0006-291X(21)00776-2
doi: 10.1016/j.bbrc.2021.05.007
pii:
doi:
Substances chimiques
Bacterial Proteins
0
Protein Subunits
0
Steroid Isomerases
EC 5.3.3.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
159-164Informations de copyright
Copyright © 2021 Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.