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2.4.2.31: NAD+-protein-arginine ADP-ribosyltransferase

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

Word Map on EC 2.4.2.31

Reaction

NAD+
+
L-arginine
=
nicotinamide
 +
Nomega-(ADP-D-ribosyl)-L-arginine
 +
H+

Synonyms

(adenosine diphosphoribose)transferase, nicotinamide adenine dinucleotide-arginine, actin-specific ADP-ribosyltransferase, ADP-ribosyl-acceptor hydrolase 1, ADP-ribosyltransferase, ADP-ribosyltransferase enzymatic component, ADP-ribosyltransferase-2, ADPRT, alloantigen Rt6.1 , alloantigen Rt6.2 , ALT, arginine ADP-ribosyltransferase 1, arginine specific ADP-ribosyltransferase, arginine specific mono-ADP-ribosyltransferase, arginine-specific adenosine diphosphate ribosyltransferase 1, arginine-specific ADP-ribosyltransferase, arginine-specific ADP-ribosyltransferase 1, arginine-specific ADP-ribosytransferases 1, arginine-specific mono-ADP-ribosyltransferase, arginine-specific mono-ADP-ribosyltransferase 1, arginine-specific mono-ADP-ribosyltransferase A, ARH1, ART, ART1, ART2, ART3, ART4, ART5, Art7.1, Art7.2, ARTase, ARTC1, ARTD15, ARTD15/PARP16, asparagine-specific ADP-ribosyltransferase, AT1 , AT2 , binary toxin, binary toxin A, binary toxin component Ia, C2 toxin, C2I, cARTC2.1, CD196 ADP-ribosyltransferase, CDT, CdtA, cholera toxin, cholix toxin, CTA, Dombrock blood group carrier molecule , exoenzyme C3, glycosylphosphatidylinositol-anchored arginine-specific ADP-ribosyltransferase7.1, i-toxin, iota toxin, MART-A, mono(ADP-ribosyl)transferase , mono-ADP-ribosyl-arginine hydrolase, mono-ADP-ribosyltransferase, mono-ADP-ribosyltransferase A, NAD(P)+-arginine ADP-ribosyltransferase, NAD+:arginine ADP-ribosyltransferase, NAD+:arginine ecto-mono(ADP-ribosyl)transferase, NAD+:L-arginine ADP-D-ribosyltransferase, NAD-arginine ADP-ribosyltransferase, NAD-arginine mono-ADP-ribosyltransferase B, NAD-dependent ADPribosyltransferase, NAD:arginine ADP-ribosyltransferase, NAD:arginine ADP-ribosyltransferase B, NarE, PARP16/ARTD15, RT6, RT6.1, RT6.2, T-cell surface protein Rt6.1 , T-cell surface protein Rt6.2 , TcdB2-TccC3, VIP2, Vis toxin, XAC3230, XopAI

ECTree

     2 Transferases
         2.4 Glycosyltransferases
             2.4.2 Pentosyltransferases
                2.4.2.31 NAD+-protein-arginine ADP-ribosyltransferase

Engineering

Engineering on EC 2.4.2.31 - NAD+-protein-arginine ADP-ribosyltransferase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E301A
-
no NADase activity detected
E378S
mutation eliminates ADP-ribosylation activity and reduces the weak NAD+ glycohydrolase activity in absence of actin to 50%
E380A
mutation eliminates both ADP-ribosylation activity and the weak NAD+ glycohydrolase activity in absence of actin
E380S
mutation eliminates both ADP-ribosylation activity and the weak NAD+ glycohydrolase activity in absence of actin
F349A
-
the ratio of turnover-number to Km-value in the NADase reaction is 1% of the wild-type ratio. The ratio of turnover-number to Km-value in the ADP-ribosyltransferase activity is 1.9% of the wild-type ratio with rabbit muscle actin as substrate and 4% of the wild-type ratio with non-muscle actin from human platelets as substrate
F349Y
-
the ratio of turnover-number to Km-value in the NADase reaction is 110% of the wild-type ratio
N255A
-
the ratio of turnover-number to Km-value in the NADase reaction is 90% of the wild-type ratio. The ratio of turnover-number to Km-value in the ADP-ribosyltransferase activity is 20% of the wild-type ratio with rabbit muscle actin as substrate and 77% of the wild-type ratio with non-muscle actin from human platelets as substrate
R352A
Y246A
-
the ratio of turnover-number to Km-value in the NADase reaction is 90% of the wild-type ratio. The ratio of turnover-number to Km-value in the ADP-ribosyltransferase activity is 1.9% of the wild-type ratio with rabbit muscle actin as substrate and 19% of the wild-type ratio with non-muscle actin from human platelets as substrate
Y251A
-
the ratio of turnover-number to Km-value in the NADase reaction is 10% of the wild-type ratio
Y251F
-
the ratio of turnover-number to Km-value in the NADase reaction is 40% of the wild-type ratio
E207G/E209G
-
abolished ADP-ribosyltransferase activity. Mutated protein localises to the plasma membrane
E209G
-
single point mutant of cARTC2.1 cannot hydrolyse NAD+, although it retains low arginine-specific ADP-ribosyltransferase activity. Mutated protein localises to the plasma membrane
E219Q
-
site-directed mutagenesis, almost inactive mutant
Q217E
-
site-directed mutagenesis, the mutation results in inhibition of the enzyme's ADP-ribosyltransferase activity toward RhoA, the mutant protein is still capable of NAD+-binding and possesses NAD+ glycohydrolase activity, the mutant is capable of ADP-ribosylation of poly-arginine but not poly-asparagine
R151A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R61A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R86A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
DELTA278-322
a deletion mutant lacking the region encompassing the putative transmembrane domain (aminoacids 278-322) shows a diffuse, cytosolic localization compared with full length ARTD15
K242E
-
displays no activity
Y187R
-
displays no activity
Y187R/K242E
-
double mutant contains the R-S-EXE motif, but displays no activity, thus additional residues besides the intact R-S-EXE motif are involved in catalyzing the enzymatic reaction
C201F
-
mutant enzyme of RT6.1, mutant enzyme loses thiol-dependency
C80S
-
mutant enzyme of RT6.1 remains thiol-dependent
C11S
the mutation results in an auto-ADP-ribosylation comparable to the wild type enzyme
C128S
the mutant does not have a stable Fe-S cluster and reduced auto-ADP-ribosylation activity
C130S
the mutation results in an auto-ADP-ribosylation comparable to the wild type enzyme
C67S
the mutant does not have a stable Fe-S cluster and reduced auto-ADP-ribosylation activity
E109D
the mutation results in an auto-ADP-ribosylation comparable to the wild type enzyme
E111D
E120D
R204E
-
isoform ART2b, no auto-ADP-ribosylation
R204K
-
isoform ART2b, no auto-ADP-ribosylation
R204Y
-
isoform ART2b, no auto-ADP-ribosylation
Y204R
-
isoform ART2a, unlike wild-type, is autoribosylated and has increased enzymic activity
E579Q
the mutant shows reduced biotinylation intensity compared to the wild type enzyme
E581Q
the mutant exhibits strongly reduced biotinylation intensity compared to the wild type enzyme
R426A
the mutant exhibits lower levels of NAD+ glycohydrolase activity than the wild type enzyme
R426K/R451K/R473K/R479K/R506K/R519K/R522K/R525K/R535K/R540K/R543K/R566K/R629K
the mutant shows no auto-ADP-ribosylation activity and reduced NAD+ glycohydrolase activity compared to the wild type enzyme
R426K/R451K/R473K/R479K/R506K/R519K/R522K/R535K/R540K/R543K/R566K/R629K
the mutant shows no auto-ADP-ribosylation activity and reduced NAD+ glycohydrolase activity compared to the wild type enzyme
R426K/R451K/R473K/R506K/R519K/R522K/R525K/R535K/R540K/R543K/R566K/R629K
the mutant shows reduced auto-ADP-ribosylation activity and severely reduced NAD+ glycohydrolase activity compared to the wild type enzyme
R426K/R451K/R473K/R506K/R519K/R522K/R535K/R540K/R543K/R566K/R629K
the mutant shows reduced auto-ADP-ribosylation activity and reduced NAD+ glycohydrolase activity compared to the wild type enzyme
R426K/R451K/R473K/R506K/R519K/R522K/R540K/R543K/R566K/R629K
the mutant shows reduced auto-ADP-ribosylation activity and reduced NAD+ glycohydrolase activity compared to the wild type enzyme
R426K/R473K/R479K/R506K/R519K/R522K/R566K/R629K
the mutant shows reduced auto-ADP-ribosylation activity and reduced NAD+ glycohydrolase activity compared to the wild type enzyme
R426K/R473K/R506K/R519K/R522K/R540K/R543K/R566K/R629K
the mutant shows reduced auto-ADP-ribosylation activity and reduced NAD+ glycohydrolase activity compared to the wild type enzyme
R426K/R473K/R506K/R519K/R522K/R540K/R566K/R629K
the mutant shows reduced auto-ADP-ribosylation activity and reduced NAD+ glycohydrolase activity compared to the wild type enzyme
R426K/R473K/R506K/R519K/R522K/R543K/R566K/R629K
the mutant shows reduced auto-ADP-ribosylation activity and reduced NAD+ glycohydrolase activity compared to the wild type enzyme
R426K/R473K/R506K/R519K/R522K/R566K/R629K
the mutant shows increased auto-ADP-ribosylation activity and reduced NAD+ glycohydrolase activity compared to the wild type enzyme
R426K/R473K/R506K/R566K/R629K
the mutant shows reduced auto-ADP-ribosylation activity and reduced NAD+ glycohydrolase activity compared to the wild type enzyme
R451A
the mutant exhibits lower levels of NAD+ glycohydrolase activity than the wild type enzyme
R473A
the mutant exhibits lower levels of NAD+ glycohydrolase activity than the wild type enzyme
R479A
the mutant exhibits lower levels of NAD+ glycohydrolase activity than the wild type enzyme
R506A
the mutant exhibits lower levels of NAD+ glycohydrolase activity than the wild type enzyme
R506K
the mutant exhibits lower levels of NAD+ glycohydrolase activity than the wild type enzyme
R506K/R566K
the mutant shows reduced auto-ADP-ribosylation activity and reduced NAD+ glycohydrolase activity compared to the wild type enzyme
R506Q
the mutant exhibits lower levels of NAD+ glycohydrolase activity than the wild type enzyme
R519A
the mutant exhibits lower levels of NAD+ glycohydrolase activity than the wild type enzyme
R522A
the mutant exhibits lower levels of NAD+ glycohydrolase activity than the wild type enzyme
R525A
the mutant exhibits lower levels of NAD+ glycohydrolase activity than the wild type enzyme
R525K
the mutant exhibits lower levels of NAD+ glycohydrolase activity than the wild type enzyme
R525Q
the mutant exhibits lower levels of NAD+ glycohydrolase activity than the wild type enzyme
R530A
the mutant exhibits lower levels of NAD+ glycohydrolase activity than the wild type enzyme
R530K
inactive
R530Q
inactive
R535A
the mutant exhibits lower levels of NAD+ glycohydrolase activity than the wild type enzyme
R540A
the mutant exhibits lower levels of NAD+ glycohydrolase activity than the wild type enzyme
R543A
the mutant exhibits lower levels of NAD+ glycohydrolase activity than the wild type enzyme
R566A
the mutant exhibits lower levels of NAD+ glycohydrolase activity than the wild type enzyme
R629A
the mutant exhibits lower levels of NAD+ glycohydrolase activity than the wild type enzyme
Y493A
inactive
Y493A/E579Q/E581Q
inactive
Y493A/E581Q
inactive
additional information