Second-Shell Amino Acid R266 Helps Determine
Amino Acid Isomerases
/ chemistry
Amino Acid Sequence
Amino Acid Substitution
Amycolatopsis
/ enzymology
Bacterial Proteins
/ chemistry
Biocatalysis
Carbon-Carbon Lyases
/ chemistry
Catalytic Domain
/ genetics
Conserved Sequence
Crystallography, X-Ray
Enzyme Stability
/ genetics
Evolution, Molecular
Kinetics
Models, Molecular
Mutagenesis, Site-Directed
Recombinant Proteins
/ chemistry
Substrate Specificity
Journal
Biochemistry
ISSN: 1520-4995
Titre abrégé: Biochemistry
Pays: United States
ID NLM: 0370623
Informations de publication
Date de publication:
21 12 2021
21 12 2021
Historique:
pubmed:
1
12
2021
medline:
8
1
2022
entrez:
30
11
2021
Statut:
ppublish
Résumé
Catalytic promiscuity is the coincidental ability to catalyze nonbiological reactions in the same active site as the native biological reaction. Several lines of evidence show that catalytic promiscuity plays a role in the evolution of new enzyme functions. Thus, studying catalytic promiscuity can help identify structural features that predispose an enzyme to evolve new functions. This study identifies a potentially preadaptive residue in a promiscuous
Identifiants
pubmed: 34845903
doi: 10.1021/acs.biochem.1c00627
pmc: PMC8939854
mid: NIHMS1783707
doi:
Substances chimiques
Bacterial Proteins
0
Recombinant Proteins
0
Carbon-Carbon Lyases
EC 4.1.-
o-succinylbenzoic acid synthase
EC 4.1.99.-
Amino Acid Isomerases
EC 5.1.1.-
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Pagination
3829-3840Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM124409
Pays : United States
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