Transient kinetic analysis of oxidative dealkylation by the direct reversal DNA repair enzyme AlkB.
AlkB Enzymes
/ chemistry
AlkB Homolog 2, Alpha-Ketoglutarate-Dependent Dioxygenase
/ chemistry
AlkB Homolog 3, Alpha-Ketoglutarate-Dependent Dioxygenase
/ chemistry
DNA
/ chemistry
DNA Repair
DNA, Bacterial
/ chemistry
DNA, Single-Stranded
/ chemistry
Escherichia coli
/ enzymology
Escherichia coli Proteins
/ chemistry
Humans
ALKBH
AlkA
AlkB
DNA adduct
DNA damage
DNA repair
Escherichia coli (E. coli)
adaptive response
oxidative dealkylation
pre-steady-state kinetics
substrate specificity
Journal
The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R
Informations de publication
Date de publication:
22 05 2020
22 05 2020
Historique:
received:
21
03
2020
revised:
10
04
2020
pubmed:
15
4
2020
medline:
29
12
2020
entrez:
15
4
2020
Statut:
ppublish
Résumé
AlkB is a bacterial Fe(II)- and 2-oxoglutarate-dependent dioxygenase that repairs a wide range of alkylated nucleobases in DNA and RNA as part of the adaptive response to exogenous nucleic acid-alkylating agents. Although there has been longstanding interest in the structure and specificity of
Identifiants
pubmed: 32284330
pii: S0021-9258(17)50265-3
doi: 10.1074/jbc.RA120.013517
pmc: PMC7247310
pii:
doi:
Substances chimiques
DNA, Bacterial
0
DNA, Single-Stranded
0
Escherichia coli Proteins
0
DNA
9007-49-2
ALKBH3 protein, human
EC 1.14.11.-
AlkB Homolog 3, Alpha-Ketoglutarate-Dependent Dioxygenase
EC 1.14.11.-
ALKBH2 protein, human
EC 1.14.11.33
AlkB Enzymes
EC 1.14.11.33
AlkB Homolog 2, Alpha-Ketoglutarate-Dependent Dioxygenase
EC 1.14.11.33
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Pagination
7317-7326Subventions
Organisme : NCI NIH HHS
ID : P30 CA046592
Pays : United States
Informations de copyright
© 2020 Baldwin et al.
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