Kinetic mechanism and fidelity of nick sealing by Escherichia coli NAD+-dependent DNA ligase (LigA).
about
Biochemical and Structural Characterisation of DNA Ligases from Bacteria and ArchaeaTwo-metal versus one-metal mechanisms of lysine adenylylation by ATP-dependent and NAD+-dependent polynucleotide ligases.Lethality of MalE-LacZ hybrid protein shares mechanistic attributes with oxidative component of antibiotic lethality.The DNA Repair Repertoire of Mycobacterium smegmatis FenA Includes the Incision of DNA 5' Flaps and the Removal of 5' Adenylylated Products of Aborted Nick Ligation.Crystal structure and mutational analysis of Mycobacterium smegmatis FenA highlight active site amino acids and three metal ions essential for flap endonuclease and 5' exonuclease activities.
P2860
Kinetic mechanism and fidelity of nick sealing by Escherichia coli NAD+-dependent DNA ligase (LigA).
description
2016 nî lūn-bûn
@nan
2016年の論文
@ja
2016年論文
@yue
2016年論文
@zh-hant
2016年論文
@zh-hk
2016年論文
@zh-mo
2016年論文
@zh-tw
2016年论文
@wuu
2016年论文
@zh
2016年论文
@zh-cn
name
Kinetic mechanism and fidelity ...... +-dependent DNA ligase (LigA).
@en
Kinetic mechanism and fidelity ...... coli NAD+-dependent DNA ligase
@nl
type
label
Kinetic mechanism and fidelity ...... +-dependent DNA ligase (LigA).
@en
Kinetic mechanism and fidelity ...... coli NAD+-dependent DNA ligase
@nl
prefLabel
Kinetic mechanism and fidelity ...... +-dependent DNA ligase (LigA).
@en
Kinetic mechanism and fidelity ...... coli NAD+-dependent DNA ligase
@nl
P2860
P356
P1476
Kinetic mechanism and fidelity ...... +-dependent DNA ligase (LigA).
@en
P2093
Mathieu Chauleau
P2860
P304
P356
10.1093/NAR/GKW049
P407
P577
2016-02-08T00:00:00Z