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6.5.1.2: DNA ligase (NAD+)

This is an abbreviated version!
For detailed information about DNA ligase (NAD+), go to the full flat file.

Word Map on EC 6.5.1.2

Reaction

(deoxyribonucleotide)n-3'-hydroxyl
+
5'-(5'-diphosphoadenosine)-(deoxyribonucleotide)m
=
(deoxyribonucleotide)n+m
 +
AMP

Synonyms

beta-NAD+ -dependent DNA ligase, beta-NAD+-dependent DNA ligase, Deoxyribonucleate ligase, Deoxyribonucleic acid joinase, Deoxyribonucleic acid ligase, Deoxyribonucleic joinase, Deoxyribonucleic ligase, Deoxyribonucleic repair enzyme, Deoxyribonucleic-joining enzyme, DNA joinase, DNA ligase, DNA ligase (NAD), DNA repair enzyme, DNA-joining enzyme, LigA, Ligase, polynucleotide (nicotinamide adenine dinucleotide), LigN, MimiLIG, MsEPV DNA ligase, MtuLigA, NAD(+)-dependent DNA ligase, NAD+ dependent DNA ligase, NAD+ DNA ligase, NAD+-dependent DNA ligase, NAD+-dependent DNA ligase A, NAD-dependent DNA ligase, NDL, Polydeoxyribonucleotide synthase (NAD+), Polydeoxyribonucleotide synthase [NAD+], Polynucleotide ligase, Polynucleotide synthetase, Polynucleotide synthetase (nicotinamide adenine dinucleotide), Rv3014c, Synthetase, polydeoxyribonucleotide (nicotinamide adenine dinucleotide), T4 DNA ligase, Taq DNA ligase, Tfi DNA ligase, Tth DNA ligase, wBm-LigA

ECTree

     6 Ligases
         6.5 Forming phosphoric-ester bonds
             6.5.1 Ligases that form phosphoric-ester bonds (only sub-subclass identified to date)
                6.5.1.2 DNA ligase (NAD+)

Engineering

Engineering on EC 6.5.1.2 - DNA ligase (NAD+)

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D117A
-
no nick-ligation activity
D27A
-
no effect on activity
D48A
-
reduced adenylate-transfer activity, no effect on DNA-ligation with preadenylated nick
D52A
-
reduced adenylate-transfer activity, no effect on DNA-ligation with preadenylated nick
DEL1-70
-
inactive in overall ligation reaction, fully functional with preadenylated nick
DEL216-532
-
inactive in overall ligation reaction, formation of adenylate-ligase intermediate not affected
K115A
-
no nick-ligation activity
Y39A
-
reduced adenylate-transfer activity, no effect on DNA-ligation with preadenylated nick
Y40A
-
reduced adenylate-transfer activity, no effect on DNA-ligation with preadenylated nick
Y51A
-
adenylate-transfer activity abolished, no effect on DNA-ligation with preadenylated nick
DELTA1-525
-
no DNA-binding
DELTA1-90
-
very low self adenylation activity, active in DNA-ligation, reduced DNA-binding
DELTA1-90,363-719
-
no self adenylation
DELTA1-90,487-719
-
very low self adenylation activity
DELTA363-719
-
full self adenylation activity
DELTA517-719
-
full self adenylation activity
DELTA636-719
-
active in DNA-ligation
K128A
-
mutant enzyme shows no ligation activity
C408A
-
inactive, unable to complement DNA-ligase-deficient yeast
C411A
-
inactive, unable to complement DNA-ligase-deficient yeast
C426A
-
no effect in vivo, 7% of wild type activity
C432A
-
inactive, unable to complement DNA-ligase-deficient yeast
D117A
-
inactive in nick-joining, unable to complement DNA-ligase-deficient yeast
D117E
-
3% of ligase activity of wild-type enzyme, lethal mutation
D117N
-
less than 0.1% of ligase activity of wild-type enzyme, lethal mutation
D138A
-
37% of ligase activity of wild-type enzyme
D283A
-
57% of ligase activity of wild-type enzyme
D285E
-
4% of ligase activity of wild-type enzyme, lethal mutation
D285N
-
less than 0.1% of ligase activity of wild-type enzyme, lethal mutation
D32A
-
traces of nick joining activity
D32E
-
traces of nick joining activity
D32N
-
9% of nick joining activity, strongly reduced self-adenylation
D36A
-
traces of nick joining activity
D36E
-
4% of nick joining activity, strongly reduced self-adenylation
D36N
-
12% of nick joining activity, strongly reduced self-adenylation
D450A
the helix-hairpin-helix domain mutant retains DNA relaxation function, concordant with the ability to effectively ligate nicks
D452A
mutant with 68% of wild type activity
D551A
DELTA1-38
DELTA1-592
-
fragment corresponding to BRCT domain binds to a wider range of substrates compared to full-length LigA
DELTA1-78
DELTA593-671
-
mutant lacking the BRCT domain, 3fold reduced in vitro ligation activity and reduced DNA binding
E10A
-
90% of nick joining activity
E113A
-
no effect in vivo, increased Km for NAD+, 40% of wild type activity
E143A
-
52% of ligase activity of wild-type enzyme
E173A
-
less than 0.1% of ligase activity of wild-type enzyme, lethal mutation
E173D
-
less than 0.1% of ligase activity of wild-type enzyme, lethal mutation
E173Q
-
less than 0.1% of ligase activity of wild-type enzyme, lethal mutation
E319A
-
no effect in vivo, 69% of wild type activity
E519A
G118A
-
less than 0.1% of ligase activity of wild-type enzyme, lethal mutation
G172A
-
36% of ligase activity of wild-type enzyme
G286A
-
14% of ligase activity of wild-type enzyme
G489A
the mutant retains 25% of wild type activity
G489D
mutant with 0.8% of wild type activity
G489V
mutant with 3.2% of wild type activity
G521A
the mutant is 50fold less active than wild type LigA
G521D
mutant with less than 0.1% of wild type function
G521V
mutant with less than 0.1% of wild type function
G553A
mutant with 38% of wild type activity
G553D
mutant with 2.6% of wild type activity
G553V
mutant with 0.9% of wild type activity
H23A
-
10% of nick joining activity
H23Y
-
88% of nick joining activity
I384A
the mutant is defective for nick sealing, retaining 4% of wild type activity
K115A
-
inactive in nick-joining, unable to complement DNA-ligase-deficient yeast
K115Q
-
less than 0.1% of ligase activity of wild-type enzyme, lethal mutation
K115R
-
less than 0.1% of ligase activity of wild-type enzyme, lethal mutation
K126A
-
inactive
K290A
-
13% of ligase activity of wild-type enzyme, lethal mutation
K314A [DV1]
-
accumulation of the DNA-adenylate intermediate, loss of function in vivo, strongly reduced activity
K314Q
-
less than 0.1% of ligase activity of wild-type enzyme, lethal mutation
K314R
-
5% of ligase activity of wild-type enzyme, lethal mutation
K627A
mutant with 40% of wild type activity
K634A/K635A
mutant with 44% of wild type activity
K648A
mutant with 37% of wild type activity
K651A
mutant with 35% of wild type activity
L119A
-
110% of ligase activity of wild-type enzyme
L15F
-
at 20°C mutant enzyme L15F has 20fold lower ligation activity in vitro, and its activity is reduced at 42°C, resulting in 60fold lower ligation activity than wild-type LigA
N198A
-
26% of ligase activity of wild-type enzyme
N355A
mutant with 30% of wild type activity
Q318A
-
no effect in vivo, 80% of wild type activity
Q330A
the mutation has no apparent effect on nick sealing acivity
Q386A
mutant with 30% of wild type activity
R200A
-
less than 0.1% of ligase activity of wild-type enzyme, lethal mutation
R200K
-
less than 0.1% of ligase activity of wild-type enzyme, lethal mutation
R200Q
-
less than 0.1% of ligase activity of wild-type enzyme, lethal mutation
R208A
-
2% of ligase activity of wild-type enzyme, lethal mutation
R208K
-
1.2% of ligase activity of wild-type enzyme, lethal mutation
R208Q
-
less than 0.1% of ligase activity of wild-type enzyme, lethal mutation
R277A
R277K
-
5.6% of ligase activity of wild-type enzyme, themperature-sensitive mutation, rate of isolated sealing step is 4% of the activity of wild-type enzyme
R277Q
-
1.8% of ligase activity of wild-type enzyme, lethal mutation, rate of isolated sealing step is 10% of the activity of wild-type enzyme
R333A
the oligonucleotide-binding domain mutation strongly suppresses DNA relaxation
R379A
the oligonucleotide-binding domain mutation strongly suppresses DNA relaxation
R487A
mutant with 6% of wild type activity
R510A
the helix-hairpin-helix domain mutant retains DNA relaxation function, concordant with the ability to effectively ligate nicks
R614A
mutant with 14% of wild type activity
V288A
-
74% of ligase activity of wild-type enzyme
V383A
the mutant is defective for nick sealing, retaining 4% of wild type activity
Y225A
-
no effect in vivo, increased Km for NAD+, 25% of wild type activity
Y22A
-
traces of nick joining activity, strongly reduced self-adenylation
Y22S
-
9% of nick joining activity
Y35A
-
2% of nick joining activity, strongly reduced self-adenylation
Y35S
-
23% of nick joining activity
L15F
-
at 20°C mutant enzyme L15F has 20fold lower ligation activity in vitro, and its activity is reduced at 42°C, resulting in 60fold lower ligation activity than wild-type LigA
-
DELTA1-396
-
no self adenylation activity, DNA-binding not affected
DELTA319-670
-
full self adenylation activity but strongly reduced DNA-binding and ligation activity
K114A
-
prevention of partial adenylation of the enzyme
D141A
-
adenylation-defective mutant
K139A
-
adenylation-defective mutant
D46A
-
mutant protein displayes only trace sealing activity
D50A
-
nick sealing activity is 6% of wild-type activity
K113A
-
mutant protein is inert
Y36A
-
mutant protein displayes only trace sealing activity
Y49A
-
nick sealing activity is 6% of wild-type activity
DELTA1-390
-
DNA binding, but no self adenylation activity
DELTA316-667
-
active in self adenylation but unable to bind DNA
L75F
-
L75F mutant is as catalytically efficient as wild-type, athough the NAD Km is slightly elevated compared to wild-type, it is still likely well below the concentration of NAD in the bacterium. IC50 for inhibitors elevated compared to wild-type
DELTA582-667
-
lower thermal stability than wild-type enzyme
D286E
-
mutant enzyme shows reduced reaction rate on both match and mismatch nicked substrates compared to wild-type enzyme
G287A
-
mutant enzyme shows reduced reaction rate on both match and mismatch nicked substrates compared to wild-type enzyme. The G287A mutation has a major effect on the second step
K291R
-
mutant enzyme shows reduced reaction rate on both match and mismatch nicked substrates compared to wild-type enzyme
V289I
-
mutant enzyme shows reduced reaction rate on both match and mismatch nicked substrates compared to wild-type enzyme
A644I
-
mutation in BRCT domain, comparable ligation activity with wild-type enzyme with nicked substrate in excess
E654A
-
mutation in BRCT domain, comparable ligation activity with wild-type enzyme with nicked substrate in excess
G617I
-
mutation in BRCT domain, mutant enzyme does not shows any detectable ligation with nicked substrate in excess
G634I
-
mutation in BRCT domain, ligation activity is about 15% of the activity with wild-type enzyme with nicked substrate in excess
G638I
-
mutation in BRCT domain, ligation activity is 30-40% lower than that with wild-type enzyme with nicked substrate in excess
K619R
-
mutation in BRCT domain, comparable ligation activity with wild-type enzyme with nicked substrate in excess
K640R
-
mutation in BRCT domain, comparable ligation activity with wild-type enzyme with nicked substrate in excess
L647A
-
mutation in BRCT domain, comparable ligation activity with wild-type enzyme with nicked substrate in excess
R606A
-
mutation in BRCT domain, ligation activity is 30-40% lower than that with wild-type enzyme with nicked substrate in excess
S623A
-
mutation in BRCT domain, comparable ligation activity with wild-type enzyme with nicked substrate in excess
T599A
-
mutation in BRCT domain, ligation activity is 30-40% lower than that with wild-type enzyme with nicked substrate in excess
V624A
-
mutation in BRCT domain, comparable ligation activity with wild-type enzyme with nicked substrate in excess
D286E
-
mutant enzyme shows reduced reaction rate on both match and mismatch nicked substrates compared to wild-type enzyme
-
G287A
-
mutant enzyme shows reduced reaction rate on both match and mismatch nicked substrates compared to wild-type enzyme. The G287A mutation has a major effect on the second step
-
K291R
-
mutant enzyme shows reduced reaction rate on both match and mismatch nicked substrates compared to wild-type enzyme
-
V289I
-
mutant enzyme shows reduced reaction rate on both match and mismatch nicked substrates compared to wild-type enzyme
-
C412M
-
Site-directed mutants: K118R, K118H, K118L, K118P1(CCC), K118P2(CCG), D120E, D120N, D120Y, D120G, D120A, D120V, K294R, K294Q, K294L1(CTG), K2942(CTC), K294P, K294P, R337K, R337Q, R337E, G339A, G339D, G339E, C412A, C412V, C412T, C412M, C415A, C415V, C415T, C415M, C428A, C428T, C433A, C433V, C433T and C433M. Studies show that residue K118 plays an essential role in the adenylation step, residue D120 may facilitate the deadenylation step, residue G339 and C433 may be involved in formation of the phosphodiester bond
C412T
-
Site-directed mutants: K118R, K118H, K118L, K118P1(CCC), K118P2(CCG), D120E, D120N, D120Y, D120G, D120A, D120V, K294R, K294Q, K294L1(CTG), K2942(CTC), K294P, K294P, R337K, R337Q, R337E, G339A, G339D, G339E, C412A, C412V, C412T, C412M, C415A, C415V, C415T, C415M, C428A, C428T, C433A, C433V, C433T and C433M. Studies show that residue K118 plays an essential role in the adenylation step, residue D120 may facilitate the deadenylation step, residue G339 and C433 may be involved in formation of the phosphodiester bond
C412V
-
Site-directed mutants: K118R, K118H, K118L, K118P1(CCC), K118P2(CCG), D120E, D120N, D120Y, D120G, D120A, D120V, K294R, K294Q, K294L1(CTG), K2942(CTC), K294P, K294P, R337K, R337Q, R337E, G339A, G339D, G339E, C412A, C412V, C412T, C412M, C415A, C415V, C415T, C415M, C428A, C428T, C433A, C433V, C433T and C433M. Studies show that residue K118 plays an essential role in the adenylation step, residue D120 may facilitate the deadenylation step, residue G339 and C433 may be involved in formation of the phosphodiester bond
C415A
-
Site-directed mutants: K118R, K118H, K118L, K118P1(CCC), K118P2(CCG), D120E, D120N, D120Y, D120G, D120A, D120V, K294R, K294Q, K294L1(CTG), K2942(CTC), K294P, K294P, R337K, R337Q, R337E, G339A, G339D, G339E, C412A, C412V, C412T, C412M, C415A, C415V, C415T, C415M, C428A, C428T, C433A, C433V, C433T and C433M. Studies show that residue K118 plays an essential role in the adenylation step, residue D120 may facilitate the deadenylation step, residue G339 and C433 may be involved in formation of the phosphodiester bond
C415M
-
Site-directed mutants: K118R, K118H, K118L, K118P1(CCC), K118P2(CCG), D120E, D120N, D120Y, D120G, D120A, D120V, K294R, K294Q, K294L1(CTG), K2942(CTC), K294P, K294P, R337K, R337Q, R337E, G339A, G339D, G339E, C412A, C412V, C412T, C412M, C415A, C415V, C415T, C415M, C428A, C428T, C433A, C433V, C433T and C433M. Studies show that residue K118 plays an essential role in the adenylation step, residue D120 may facilitate the deadenylation step, residue G339 and C433 may be involved in formation of the phosphodiester bond
C415T
-
Site-directed mutants: K118R, K118H, K118L, K118P1(CCC), K118P2(CCG), D120E, D120N, D120Y, D120G, D120A, D120V, K294R, K294Q, K294L1(CTG), K2942(CTC), K294P, K294P, R337K, R337Q, R337E, G339A, G339D, G339E, C412A, C412V, C412T, C412M, C415A, C415V, C415T, C415M, C428A, C428T, C433A, C433V, C433T and C433M. Studies show that residue K118 plays an essential role in the adenylation step, residue D120 may facilitate the deadenylation step, residue G339 and C433 may be involved in formation of the phosphodiester bond
C415V
-
Site-directed mutants: K118R, K118H, K118L, K118P1(CCC), K118P2(CCG), D120E, D120N, D120Y, D120G, D120A, D120V, K294R, K294Q, K294L1(CTG), K2942(CTC), K294P, K294P, R337K, R337Q, R337E, G339A, G339D, G339E, C412A, C412V, C412T, C412M, C415A, C415V, C415T, C415M, C428A, C428T, C433A, C433V, C433T and C433M. Studies show that residue K118 plays an essential role in the adenylation step, residue D120 may facilitate the deadenylation step, residue G339 and C433 may be involved in formation of the phosphodiester bond
C428T
-
Site-directed mutants: K118R, K118H, K118L, K118P1(CCC), K118P2(CCG), D120E, D120N, D120Y, D120G, D120A, D120V, K294R, K294Q, K294L1(CTG), K2942(CTC), K294P, K294P, R337K, R337Q, R337E, G339A, G339D, G339E, C412A, C412V, C412T, C412M, C415A, C415V, C415T, C415M, C428A, C428T, C433A, C433V, C433T and C433M. Studies show that residue K118 plays an essential role in the adenylation step, residue D120 may facilitate the deadenylation step, residue G339 and C433 may be involved in formation of the phosphodiester bond
C433A
-
Site-directed mutants: K118R, K118H, K118L, K118P1(CCC), K118P2(CCG), D120E, D120N, D120Y, D120G, D120A, D120V, K294R, K294Q, K294L1(CTG), K2942(CTC), K294P, K294P, R337K, R337Q, R337E, G339A, G339D, G339E, C412A, C412V, C412T, C412M, C415A, C415V, C415T, C415M, C428A, C428T, C433A, C433V, C433T and C433M. Studies show that residue K118 plays an essential role in the adenylation step, residue D120 may facilitate the deadenylation step, residue G339 and C433 may be involved in formation of the phosphodiester bond
C433M
-
Site-directed mutants: K118R, K118H, K118L, K118P1(CCC), K118P2(CCG), D120E, D120N, D120Y, D120G, D120A, D120V, K294R, K294Q, K294L1(CTG), K2942(CTC), K294P, K294P, R337K, R337Q, R337E, G339A, G339D, G339E, C412A, C412V, C412T, C412M, C415A, C415V, C415T, C415M, C428A, C428T, C433A, C433V, C433T and C433M. Studies show that residue K118 plays an essential role in the adenylation step, residue D120 may facilitate the deadenylation step, residue G339 and C433 may be involved in formation of the phosphodiester bond
C433T
-
Site-directed mutants: K118R, K118H, K118L, K118P1(CCC), K118P2(CCG), D120E, D120N, D120Y, D120G, D120A, D120V, K294R, K294Q, K294L1(CTG), K2942(CTC), K294P, K294P, R337K, R337Q, R337E, G339A, G339D, G339E, C412A, C412V, C412T, C412M, C415A, C415V, C415T, C415M, C428A, C428T, C433A, C433V, C433T and C433M. Studies show that residue K118 plays an essential role in the adenylation step, residue D120 may facilitate the deadenylation step, residue G339 and C433 may be involved in formation of the phosphodiester bond
C433V
-
Site-directed mutants: K118R, K118H, K118L, K118P1(CCC), K118P2(CCG), D120E, D120N, D120Y, D120G, D120A, D120V, K294R, K294Q, K294L1(CTG), K2942(CTC), K294P, K294P, R337K, R337Q, R337E, G339A, G339D, G339E, C412A, C412V, C412T, C412M, C415A, C415V, C415T, C415M, C428A, C428T, C433A, C433V, C433T and C433M. Studies show that residue K118 plays an essential role in the adenylation step, residue D120 may facilitate the deadenylation step, residue G339 and C433 may be involved in formation of the phosphodiester bond
D120A
-
Site-directed mutants: K118R, K118H, K118L, K118P1(CCC), K118P2(CCG), D120E, D120N, D120Y, D120G, D120A, D120V, K294R, K294Q, K294L1(CTG), K2942(CTC), K294P, K294P, R337K, R337Q, R337E, G339A, G339D, G339E, C412A, C412V, C412T, C412M, C415A, C415V, C415T, C415M, C428A, C428T, C433A, C433V, C433T and C433M. Studies show that residue K118 plays an essential role in the adenylation step, residue D120 may facilitate the deadenylation step, residue G339 and C433 may be involved in formation of the phosphodiester bond
D120E
-
Site-directed mutants: K118R, K118H, K118L, K118P1(CCC), K118P2(CCG), D120E, D120N, D120Y, D120G, D120A, D120V, K294R, K294Q, K294L1(CTG), K2942(CTC), K294P, K294P, R337K, R337Q, R337E, G339A, G339D, G339E, C412A, C412V, C412T, C412M, C415A, C415V, C415T, C415M, C428A, C428T, C433A, C433V, C433T and C433M. Studies show that residue K118 plays an essential role in the adenylation step, residue D120 may facilitate the deadenylation step, residue G339 and C433 may be involved in formation of the phosphodiester bond
D120G
-
Site-directed mutants: K118R, K118H, K118L, K118P1(CCC), K118P2(CCG), D120E, D120N, D120Y, D120G, D120A, D120V, K294R, K294Q, K294L1(CTG), K2942(CTC), K294P, K294P, R337K, R337Q, R337E, G339A, G339D, G339E, C412A, C412V, C412T, C412M, C415A, C415V, C415T, C415M, C428A, C428T, C433A, C433V, C433T and C433M. Studies show that residue K118 plays an essential role in the adenylation step, residue D120 may facilitate the deadenylation step, residue G339 and C433 may be involved in formation of the phosphodiester bond
D120N
-
Site-directed mutants: K118R, K118H, K118L, K118P1(CCC), K118P2(CCG), D120E, D120N, D120Y, D120G, D120A, D120V, K294R, K294Q, K294L1(CTG), K2942(CTC), K294P, K294P, R337K, R337Q, R337E, G339A, G339D, G339E, C412A, C412V, C412T, C412M, C415A, C415V, C415T, C415M, C428A, C428T, C433A, C433V, C433T and C433M. Studies show that residue K118 plays an essential role in the adenylation step, residue D120 may facilitate the deadenylation step, residue G339 and C433 may be involved in formation of the phosphodiester bond
D120V
-
Site-directed mutants: K118R, K118H, K118L, K118P1(CCC), K118P2(CCG), D120E, D120N, D120Y, D120G, D120A, D120V, K294R, K294Q, K294L1(CTG), K2942(CTC), K294P, K294P, R337K, R337Q, R337E, G339A, G339D, G339E, C412A, C412V, C412T, C412M, C415A, C415V, C415T, C415M, C428A, C428T, C433A, C433V, C433T and C433M. Studies show that residue K118 plays an essential role in the adenylation step, residue D120 may facilitate the deadenylation step, residue G339 and C433 may be involved in formation of the phosphodiester bond
D120Y
-
Site-directed mutants: K118R, K118H, K118L, K118P1(CCC), K118P2(CCG), D120E, D120N, D120Y, D120G, D120A, D120V, K294R, K294Q, K294L1(CTG), K2942(CTC), K294P, K294P, R337K, R337Q, R337E, G339A, G339D, G339E, C412A, C412V, C412T, C412M, C415A, C415V, C415T, C415M, C428A, C428T, C433A, C433V, C433T and C433M. Studies show that residue K118 plays an essential role in the adenylation step, residue D120 may facilitate the deadenylation step, residue G339 and C433 may be involved in formation of the phosphodiester bond
G339A
-
Site-directed mutants: K118R, K118H, K118L, K118P1(CCC), K118P2(CCG), D120E, D120N, D120Y, D120G, D120A, D120V, K294R, K294Q, K294L1(CTG), K2942(CTC), K294P, K294P, R337K, R337Q, R337E, G339A, G339D, G339E, C412A, C412V, C412T, C412M, C415A, C415V, C415T, C415M, C428A, C428T, C433A, C433V, C433T and C433M. Studies show that residue K118 plays an essential role in the adenylation step, residue D120 may facilitate the deadenylation step, residue G339 and C433 may be involved in formation of the phosphodiester bond
G339D
-
Site-directed mutants: K118R, K118H, K118L, K118P1(CCC), K118P2(CCG), D120E, D120N, D120Y, D120G, D120A, D120V, K294R, K294Q, K294L1(CTG), K2942(CTC), K294P, K294P, R337K, R337Q, R337E, G339A, G339D, G339E, C412A, C412V, C412T, C412M, C415A, C415V, C415T, C415M, C428A, C428T, C433A, C433V, C433T and C433M. Studies show that residue K118 plays an essential role in the adenylation step, residue D120 may facilitate the deadenylation step, residue G339 and C433 may be involved in formation of the phosphodiester bond
G339E
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Site-directed mutants: K118R, K118H, K118L, K118P1(CCC), K118P2(CCG), D120E, D120N, D120Y, D120G, D120A, D120V, K294R, K294Q, K294L1(CTG), K2942(CTC), K294P, K294P, R337K, R337Q, R337E, G339A, G339D, G339E, C412A, C412V, C412T, C412M, C415A, C415V, C415T, C415M, C428A, C428T, C433A, C433V, C433T and C433M. Studies show that residue K118 plays an essential role in the adenylation step, residue D120 may facilitate the deadenylation step, residue G339 and C433 may be involved in formation of the phosphodiester bond
K118H
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Site-directed mutants: K118R, K118H, K118L, K118P1(CCC), K118P2(CCG), D120E, D120N, D120Y, D120G, D120A, D120V, K294R, K294Q, K294L1(CTG), K2942(CTC), K294P, K294P, R337K, R337Q, R337E, G339A, G339D, G339E, C412A, C412V, C412T, C412M, C415A, C415V, C415T, C415M, C428A, C428T, C433A, C433V, C433T and C433M. Studies show that residue K118 plays an essential role in the adenylation step, residue D120 may facilitate the deadenylation step, residue G339 and C433 may be involved in formation of the phosphodiester bond
K118L
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Site-directed mutants: K118R, K118H, K118L, K118P1(CCC), K118P2(CCG), D120E, D120N, D120Y, D120G, D120A, D120V, K294R, K294Q, K294L1(CTG), K2942(CTC), K294P, K294P, R337K, R337Q, R337E, G339A, G339D, G339E, C412A, C412V, C412T, C412M, C415A, C415V, C415T, C415M, C428A, C428T, C433A, C433V, C433T and C433M. Studies show that residue K118 plays an essential role in the adenylation step, residue D120 may facilitate the deadenylation step, residue G339 and C433 may be involved in formation of the phosphodiester bond
K118P1(CCC)
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Site-directed mutants: K118R, K118H, K118L, K118P1(CCC), K118P2(CCG), D120E, D120N, D120Y, D120G, D120A, D120V, K294R, K294Q, K294L1(CTG), K2942(CTC), K294P, K294P, R337K, R337Q, R337E, G339A, G339D, G339E, C412A, C412V, C412T, C412M, C415A, C415V, C415T, C415M, C428A, C428T, C433A, C433V, C433T and C433M. Studies show that residue K118 plays an essential role in the adenylation step, residue D120 may facilitate the deadenylation step, residue G339 and C433 may be involved in formation of the phosphodiester bond
K118P2(CCG)
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Site-directed mutants: K118R, K118H, K118L, K118P1(CCC), K118P2(CCG), D120E, D120N, D120Y, D120G, D120A, D120V, K294R, K294Q, K294L1(CTG), K2942(CTC), K294P, K294P, R337K, R337Q, R337E, G339A, G339D, G339E, C412A, C412V, C412T, C412M, C415A, C415V, C415T, C415M, C428A, C428T, C433A, C433V, C433T and C433M. Studies show that residue K118 plays an essential role in the adenylation step, residue D120 may facilitate the deadenylation step, residue G339 and C433 may be involved in formation of the phosphodiester bond
K118R
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Site-directed mutants: K118R, K118H, K118L, K118P1(CCC), K118P2(CCG), D120E, D120N, D120Y, D120G, D120A, D120V, K294R, K294Q, K294L1(CTG), K2942(CTC), K294P, K294P, R337K, R337Q, R337E, G339A, G339D, G339E, C412A, C412V, C412T, C412M, C415A, C415V, C415T, C415M, C428A, C428T, C433A, C433V, C433T and C433M. Studies show that residue K118 plays an essential role in the adenylation step, residue D120 may facilitate the deadenylation step, residue G339 and C433 may be involved in formation of the phosphodiester bond
K2942(CTC)
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Site-directed mutants: K118R, K118H, K118L, K118P1(CCC), K118P2(CCG), D120E, D120N, D120Y, D120G, D120A, D120V, K294R, K294Q, K294L1(CTG), K2942(CTC), K294P, K294P, R337K, R337Q, R337E, G339A, G339D, G339E, C412A, C412V, C412T, C412M, C415A, C415V, C415T, C415M, C428A, C428T, C433A, C433V, C433T and C433M. Studies show that residue K118 plays an essential role in the adenylation step, residue D120 may facilitate the deadenylation step, residue G339 and C433 may be involved in formation of the phosphodiester bond
K294L1(CTG)
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Site-directed mutants: K118R, K118H, K118L, K118P1(CCC), K118P2(CCG), D120E, D120N, D120Y, D120G, D120A, D120V, K294R, K294Q, K294L1(CTG), K2942(CTC), K294P, K294P, R337K, R337Q, R337E, G339A, G339D, G339E, C412A, C412V, C412T, C412M, C415A, C415V, C415T, C415M, C428A, C428T, C433A, C433V, C433T and C433M. Studies show that residue K118 plays an essential role in the adenylation step, residue D120 may facilitate the deadenylation step, residue G339 and C433 may be involved in formation of the phosphodiester bond
K294P
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Site-directed mutants: K118R, K118H, K118L, K118P1(CCC), K118P2(CCG), D120E, D120N, D120Y, D120G, D120A, D120V, K294R, K294Q, K294L1(CTG), K2942(CTC), K294P, K294P, R337K, R337Q, R337E, G339A, G339D, G339E, C412A, C412V, C412T, C412M, C415A, C415V, C415T, C415M, C428A, C428T, C433A, C433V, C433T and C433M. Studies show that residue K118 plays an essential role in the adenylation step, residue D120 may facilitate the deadenylation step, residue G339 and C433 may be involved in formation of the phosphodiester bond
K294Q
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Site-directed mutants: K118R, K118H, K118L, K118P1(CCC), K118P2(CCG), D120E, D120N, D120Y, D120G, D120A, D120V, K294R, K294Q, K294L1(CTG), K2942(CTC), K294P, K294P, R337K, R337Q, R337E, G339A, G339D, G339E, C412A, C412V, C412T, C412M, C415A, C415V, C415T, C415M, C428A, C428T, C433A, C433V, C433T and C433M. Studies show that residue K118 plays an essential role in the adenylation step, residue D120 may facilitate the deadenylation step, residue G339 and C433 may be involved in formation of the phosphodiester bond
K294R
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Site-directed mutants: K118R, K118H, K118L, K118P1(CCC), K118P2(CCG), D120E, D120N, D120Y, D120G, D120A, D120V, K294R, K294Q, K294L1(CTG), K2942(CTC), K294P, K294P, R337K, R337Q, R337E, G339A, G339D, G339E, C412A, C412V, C412T, C412M, C415A, C415V, C415T, C415M, C428A, C428T, C433A, C433V, C433T and C433M. Studies show that residue K118 plays an essential role in the adenylation step, residue D120 may facilitate the deadenylation step, residue G339 and C433 may be involved in formation of the phosphodiester bond
R337E
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Site-directed mutants: K118R, K118H, K118L, K118P1(CCC), K118P2(CCG), D120E, D120N, D120Y, D120G, D120A, D120V, K294R, K294Q, K294L1(CTG), K2942(CTC), K294P, K294P, R337K, R337Q, R337E, G339A, G339D, G339E, C412A, C412V, C412T, C412M, C415A, C415V, C415T, C415M, C428A, C428T, C433A, C433V, C433T and C433M. Studies show that residue K118 plays an essential role in the adenylation step, residue D120 may facilitate the deadenylation step, residue G339 and C433 may be involved in formation of the phosphodiester bond
R337K
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Site-directed mutants: K118R, K118H, K118L, K118P1(CCC), K118P2(CCG), D120E, D120N, D120Y, D120G, D120A, D120V, K294R, K294Q, K294L1(CTG), K2942(CTC), K294P, K294P, R337K, R337Q, R337E, G339A, G339D, G339E, C412A, C412V, C412T, C412M, C415A, C415V, C415T, C415M, C428A, C428T, C433A, C433V, C433T and C433M. Studies show that residue K118 plays an essential role in the adenylation step, residue D120 may facilitate the deadenylation step, residue G339 and C433 may be involved in formation of the phosphodiester bond
R337Q
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Site-directed mutants: K118R, K118H, K118L, K118P1(CCC), K118P2(CCG), D120E, D120N, D120Y, D120G, D120A, D120V, K294R, K294Q, K294L1(CTG), K2942(CTC), K294P, K294P, R337K, R337Q, R337E, G339A, G339D, G339E, C412A, C412V, C412T, C412M, C415A, C415V, C415T, C415M, C428A, C428T, C433A, C433V, C433T and C433M. Studies show that residue K118 plays an essential role in the adenylation step, residue D120 may facilitate the deadenylation step, residue G339 and C433 may be involved in formation of the phosphodiester bond
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