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2.4.2.30: NAD+ ADP-ribosyltransferase

This is an abbreviated version!
For detailed information about NAD+ ADP-ribosyltransferase, go to the full flat file.

Word Map on EC 2.4.2.30

Reaction

NAD+
+
(ADP-D-ribosyl)n-acceptor
=
nicotinamide
 +
(ADP-D-ribosyl)n+1-acceptor
 +
H+

Synonyms

(adenosine diphosphoribose)transferase, nicotinamide adenine dinucleotide-protein, 193-kDa vault protein , 2,3,7,8-tetrachlorodibenzo-p-dioxin poly(ADP-ribose) polymerase, adenosine diphosphate ribosyltransferase, ADP-ribosylating thermozyme, ADP-ribosyltransferase, ADP-ribosyltransferase (polymerizing), ADP-ribosyltransferase 3, ADP-ribosyltransferase C3cer, ADP-ribosyltransferase-1, ADPr, ADPRT, ADPRT , ART, ART1, ARTC2.2, ARTD10, ARTD10/PARP10, ARTD11, ARTD14, ARTD3, ARTD7/PARP15, ARTD8, asparagine-specific ADP-ribosyltransferase, B aggressive lymphoma protein 2, C3 exoenzyme, C3-like toxin, C3larvin toxin, C3lim, CRM66, diphtheria toxin-like ADP-ribosyltranferase, ecto-ADP-ribosyltransferase, ecto-ADP-ribosyltransferase 2.2, ecto-ADP-ribosyltransferase ART2.2, EspJ, Exo53, exoenzyme C3, exoenzyme S, exoenzyme T, ExoS, ExoT, exotoxin-S, mART, ModA, ModB, mono ADP-ribosyltransferase, mono(ADP-ribosyl) transferase, mono-ADP-ribosyl transferase C3, mono-ADP-ribosyltransferase, More, msPARP , NAD(+) ADP-ribosyltransferase , NAD+:ADP-ribosyltransferase (polymerizing), NAD-dependent ADP-ribosyltransferase, NAD-protein ADP-ribosyltransferase, NarE, pADPRT, PAR polymerase, PARP, PARP , PARP-1, PARP-7, PARP-related/IalphaI-related H5/proline-rich , PARP1, PARP10, PARP11, PARP14, PARP3, PARPss, pertussis toxin, PH5P , poly (ADP-ribose) polymerase, poly (ADP-ribose) polymerase-1, poly(ADP-ribose) polymerase, poly(ADP-ribose) polymerase family member 11, poly(ADP-ribose) polymerase-1, poly(ADP-ribose) polymerase-11, poly(ADP-ribose) polymerase-like enzyme, poly(ADP-ribose) synthase, poly(ADP-ribose) transferase, poly(ADP-ribosyl)transferase, poly[ADP-ribose] synthetase , PTx, PtxS1, scabin, TANK1, TANK1 , TANK2 , tankyrase I, Tankyrase-like protein , Tankyrase-related protein , TbSIR2RP1, TiPARP, TNKS-1, TRF1-interacting ankyrin-related ADP-ribose polymerase, TRF1-interacting ankyrin-related ADP-ribose polymerase , TTS-ExoS, type III-secreted toxin, VahC, VPARP , vsdc, YART

ECTree

     2 Transferases
         2.4 Glycosyltransferases
             2.4.2 Pentosyltransferases
                2.4.2.30 NAD+ ADP-ribosyltransferase

Engineering

Engineering on EC 2.4.2.30 - NAD+ ADP-ribosyltransferase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E213A
kcat highly decreased compared to wild-type, Km similar to wild-type
E215A
kcat highly decreased compared to wild-type, Km (ADP-D-ribosyl)n-actin similar to wild-type, Km (NAD+) increased compared to wild-type
N86A
kcat moderately decreased compared to wild-type, Km decreased compared to wild-type
S178A
kcat decreased compared to wild-type, Km increased compared to wild-type
Y77A
kcat decreased compared to wild-type, Km increased compared to wild-type
Y82A
kcat decreased compared to wild-type, Km increased compared to wild-type
C19A
-
ADP-ribosyltransferase activity is 118% of the wild-type activity
E185Q
-
no ADP-ribosyltransferase activity
E431D
-
inactive
Q183E
-
no ADP-ribosyltransferase activity
R155E
-
ADP-ribosyltransferase activity is 0.2% of the wild-type activity
R59K
-
ADP-ribosyltransferase activity is 1.1% of the wild-type activity
R59K/R97K
-
no ADP-ribosyltransferase activity
R97K
-
ADP-ribosyltransferase activity is 1.9% of the wild-type activity
T178A
-
ADP-ribosyltransferase activity is 1.3% of the wild-type activity
T178A/Q183E
-
no ADP-ribosyltransferase activity
Y151V
-
ADP-ribosyltransferase activity is 1.6% of the wild-type activity
Y180T
-
no ADP-ribosyltransferase activity
C19A
-
ADP-ribosyltransferase activity is 118% of the wild-type activity
-
R155E
-
ADP-ribosyltransferase activity is 0.2% of the wild-type activity
-
R59K
-
ADP-ribosyltransferase activity is 1.1% of the wild-type activity
-
R59K/R97K
-
no ADP-ribosyltransferase activity
-
R97K
-
ADP-ribosyltransferase activity is 1.9% of the wild-type activity
-
E431D
-
inactive
-
Q127D/E129D
D187A
-
catalytically inactive
E219Q
-
site-directed mutagenesis, inactive mutant
Q217E
-
site-directed mutagenesis, the point mutation alters the asparagine-specificity of the enzyme to an arginie-specificity, the mutant does not show ADP-ribosyltransferase activity towards RhoA, but is still capable of NAD-binding and possesses NAD+ glycohydrolase activity, the mutant exoenzyme C3 is capable of ADP-ribosylation of poly-arginine, but not poly-asparagine, and shows high activity with Arg residues of soybean trypsin inhibitor
R151A
-
site-directed mutagenesis, the mutation does not alter the enzyme activity or its potential as substrate for the C3 mutant Q217E
R61A
-
site-directed mutagenesis, the mutation does not alter the enzyme activity or its potential as substrate for the C3 mutant Q217E
R86A
-
site-directed mutagenesis, the mutation does not alter the enzyme activity but its potential as substrate for the C3 mutant Q217E, which cannot ADP-ribosylate this mutant
G888W
H532A
inactive
I163A
the enzyme shows wild type activity
Y564A
inactive
DELTA106-288
-
mutant enzyme has NADase activity, lack of transferase activity
DELTA24–288
-
signal sequences necessary for export from the ER (at the amino terminus) and addition of a GPI-anchor (at the carboxyl terminus) are deleted. The resulting mutants retain the catalytic properties of the mature wild-type ART1. Their NADase activities relative to transferase activities are very low, and nicotinamide release is enhanced in the presence of the ADP-ribose acceptor, agmatine
DELTA24–293
-
signal sequences necessary for export from the ER (at the amino terminus) and addition of a GPI-anchor (at the carboxyl terminus) are deleted. The resulting mutants retain the catalytic properties of the mature wild-type ART1. Their NADase activities relative to transferase activities are very low, and nicotinamide release is enhanced in the presence of the ADP-ribose acceptor, agmatine
E111D
-
catalytic activity close to wild-type
E120D
-
catalytic activity highly decreased
A425K
-
site-directed mutagenesis, phenotypic analysis
D424A
-
site-directed mutagenesis, phenotypic analysis
D424A/D427A
-
site-directed mutagenesis, reduced interaction with 14-3-3, phenotypic analysis
D424A/L426A/D427A/L428A
-
site-directed mutagenesis, the mutant shows a highly reduced expression level, phenotypic analysis
D427A
-
site-directed mutagenesis, the mutant shows a reduced expression level, phenotypic analysis
DELTAN222
DELTAN222/E381A
-
possesses 0.02% of the ADP-ribosyltransferase activity of DELTAN222. KM-value for (ADP-D-ribosyl)n-soybean-trypsin-inhibitor is 8.7fold higher than the KM-value for DELTAN222
DELTAN222/E381D
-
possesses 0.6% of the ADP-ribosyltransferase activity of DELTAN222. KM-value for (ADP-D-ribosyl)n-soybean-trypsin-inhibitor is 7.9fold higher than the KM-value for DELTAN222
DELTAN222/E381S
-
possesses 0.01% of the ADP-ribosyltransferase activity of DELTAN222. KM-value for (ADP-D-ribosyl)n-soybean-trypsin-inhibitor is 4.7fold higher than the KM-value for DELTAN222
DELTAN222/E387A
-
possesses 31% of the ADP-ribosyltransferase activity of DELTAN222
DELTAN222/E399A
-
possesses 28% of the ADP-ribosyltransferase activity of DELTAN222
DELTAN222/E414A
-
possesses 20% of the ADP-ribosyltransferase activity of DELTAN222
E379D
-
mutation inhibits expression of ADP-ribosyltransferase activity, but has little effect on the expression of NAD glycohydrolase activity
E381D
G421A
-
site-directed mutagenesis, phenotypic analysis
L422A
-
site-directed mutagenesis, phenotypic analysis
L423A
-
site-directed mutagenesis, phenotypic analysis
L426A
-
site-directed mutagenesis, phenotypic analysis
L426A/D427A
-
site-directed mutagenesis, the mutant shows a highly reduced expression level and slightly reduced cytotoxicity, no interaction with 14-3-3, phenotypic analysis
L426A/D427A/L428A
-
site-directed mutagenesis, the mutant shows a highly reduced expression level and cytotoxicity, no interaction with 14-3-3, phenotypic analysis
L428A
-
site-directed mutagenesis, reduced interaction with 14-3-3, the mutant shows highly reduced cytotoxicity, phenotypic analysis
Q420A
-
site-directed mutagenesis, phenotypic analysis
R146K
-
site-directed mutagenesis, the mutation within the active site for the RhoGAP domain
R146K/E379/381D
-
inactive mutant, does not inhibit Pseudomonas aeruginosa internalization into ExoS-transfected HeLa cells in contrast to the wild-type enzyme
S419I
-
site-directed mutagenesis, phenotypic analysis
Y426H
-
in native conformation, CRM66 shows limited ability to modify EF-2 covalently. Upon activation with urea and dithiothreitol CRM66 loses ADP-ribosylation activity entirely, yet it retains the ability to bind NAD+. Replacement of Tyr-426 with histidine in CRM66 completely restores cytotoxicity and ADP-ribosyltransferase activity
E381D
R146K
-
site-directed mutagenesis, the mutation within the active site for the RhoGAP domain
-
R146K/E379/381D
-
inactive mutant, does not inhibit Pseudomonas aeruginosa internalization into ExoS-transfected HeLa cells in contrast to the wild-type enzyme
-
E189A
-
about 5200fold decrease in NAD+ hydrolysis activity
E189I
-
20000fold decrease in NAD+ hydrolysis activity
E189S
-
about 5200fold decrease in NAD+ hydrolysis activity
Q187A/E189A
-
50000fold decrease in NAD+ hydrolysis activity
Q158A/E160A
E118A
Tequatrovirus T4
mutation reduces the toxicity of the enzyme and still allows small colonies to grow
E163A
Tequatrovirus T4
mutation reduces toxicity of ModA to a minor extent
E165A
Tequatrovirus T4
mutation in ModA reduces the toxicity to colony growth
E171A
Tequatrovirus T4
mutation reduces the toxicity of the enzyme and still allows small colonies to grow
E173A
Tequatrovirus T4
mutation largly abolishes enzyme activity
F127A
Tequatrovirus T4
mutation in ModA reduces the toxicity to colony growth
F129A
I176A
Tequatrovirus T4
mutation reduces the toxicity of the enzyme and still allows small colonies to grow
L71A
Tequatrovirus T4
mutation largly abolishes enzyme activity
N128A
Tequatrovirus T4
mutation reduces toxicity of ModA to a minor extent
N130A
Tequatrovirus T4
mutant enzyme with toxicity close to that of wild-type enzyme
Q116A
Tequatrovirus T4
mutation reduces toxicity of ModA to a minor extent
Q164A
Tequatrovirus T4
mutation reduces toxicity of ModA to a minor extent
Q172A
Tequatrovirus T4
mutant enzyme with toxicity close to that of wild-type enzyme
R72A
Tequatrovirus T4
mutation in ModA reduces the toxicity to colony growth
R73A
Tequatrovirus T4
mutation largly abolishes enzyme activity
S109A
Tequatrovirus T4
mutation in ModA reduces the toxicity to colony growth
S111A
Tequatrovirus T4
mutant enzyme with toxicity close to that of wild-type enzyme
Y131A
Tequatrovirus T4
mutation largly abolishes enzyme activity
E118A
Tequatrovirus T4 ModA
-
mutation reduces the toxicity of the enzyme and still allows small colonies to grow
-
E173A
Tequatrovirus T4 ModA
-
mutation largly abolishes enzyme activity
-
Q116A
Tequatrovirus T4 ModA
-
mutation reduces toxicity of ModA to a minor extent
-
R72A
Tequatrovirus T4 ModA
-
mutation in ModA reduces the toxicity to colony growth
-
Y131A
Tequatrovirus T4 ModA
-
mutation largly abolishes enzyme activity
-
E118A
Tequatrovirus T4 ModB
-
mutation reduces the toxicity of the enzyme and still allows small colonies to grow
-
E173A
Tequatrovirus T4 ModB
-
mutation largly abolishes enzyme activity
-
Q116A
Tequatrovirus T4 ModB
-
mutation reduces toxicity of ModA to a minor extent
-
R72A
Tequatrovirus T4 ModB
-
mutation in ModA reduces the toxicity to colony growth
-
Y131A
Tequatrovirus T4 ModB
-
mutation largly abolishes enzyme activity
-
E160A
-
inactive
additional information