KEGG   ENZYME: 2.4.2.31Help
Entry
EC 2.4.2.31                 Enzyme                                 

Name
NAD+---protein-arginine ADP-ribosyltransferase;
ADP-ribosyltransferase;
mono(ADP-ribosyl)transferase;
NAD+:L-arginine ADP-D-ribosyltransferase;
NAD(P)+-arginine ADP-ribosyltransferase;
NAD(P)+:L-arginine ADP-D-ribosyltransferase;
mono-ADP-ribosyltransferase;
ART;
ART1;
ART2;
ART3;
ART4;
ART5;
ART6;
ART7;
NAD(P)+---protein-arginine ADP-ribosyltransferase;
NAD(P)+:protein-L-arginine ADP-D-ribosyltransferase
Class
Transferases;
Glycosyltransferases;
Pentosyltransferases
BRITE hierarchy
Sysname
NAD+:protein-L-arginine ADP-D-ribosyltransferase
Reaction(IUBMB)
NAD+ + protein L-arginine = nicotinamide + Nomega-(ADP-D-ribosyl)-protein-L-arginine [RN:R00555]
Reaction(KEGG)
Substrate
NAD+ [CPD:C00003];
protein L-arginine
Product
nicotinamide [CPD:C00153];
Nomega-(ADP-D-ribosyl)-protein-L-arginine [CPD:C16011]
Comment
Protein mono-ADP-ribosylation is a reversible post-translational modification that plays a role in the regulation of cellular activities [4]. Arginine residues in proteins act as acceptors. Free arginine, agmatine [(4-aminobutyl)guanidine], arginine methyl ester and guanidine can also do so. The enzyme from some, but not all, species can also use NADP+ as acceptor (giving rise to Nomega-[(2'-phospho-ADP)-D-ribosyl]-protein-L-arginine as the product), but more slowly [1,5]. The enzyme catalyses the NAD+-dependent activation of EC 4.6.1.1, adenylate cyclase. Some bacterial enterotoxins possess similar enzymic activities. (cf. EC 2.4.2.36 NAD+---diphthamide ADP-ribosyltransferase).
History
EC 2.4.2.31 created 1984, modified 1990, modified 2006
Orthology
K00775  
NAD(P)-arginine ADP-ribosyltransferase
K06716  
ADP-ribosyltransferase 1
K06717  
ADP-ribosyltransferase 4
K11416  
mono-ADP-ribosyltransferase sirtuin 6
Genes
HSA: 
116969(ART5) 417(ART1) 419(ART3) 420(ART4) 51548(SIRT6)
PTR: 
450970(ART5) 461241(ART3) 466326(ART1) 473376(ART4) 737026(SIRT6)
PPS: 
100977452(ART4) 100987803(ART5) 100988371(ART1) 100992183(ART3) 100995305(SIRT6)
GGO: 
101127624(SIRT6) 101134639(ART4) 101146612(ART3) 101153293(ART5) 101153661(ART1)
PON: 
100172886(ART3) 100432433(ART4) 100435792(ART1) 100438048(ART5) 100441394(SIRT6)
MCC: 
100424030(ART3) 574238(ART5) 699934(ART4) 714545(SIRT6) 718154(ART1)
MCF: 
102134161(ART4) 102135068(ART3) 102139792(ART5) 102141535(SIRT6) 102142531(ART1)
MMU: 
109978(Art4) 109979(Art3) 11870(Art1) 11871(Art2a-ps) 11872(Art2b) 11875(Art5) 50721(Sirt6)
RNO: 
259167(Art5) 293152(Art2b) 299638(Sirt6) 305235(Art3) 308873(Art1) 312806(Art4)
CGE: 
HGL: 
101706114(Sirt6) 101718202(Art3) 101718884(Art4) 101722974(Art5) 101723321(Art1)
TUP: 
102475139(SIRT6) 102483009(ART1) 102484959(ART3) 102487179 102493683(ART4) 102495500(ART5)
CFA: 
476821(ART1) 478434(ART3) 485045(SIRT6) 485214(ART5) 486668(ART4)
AML: 
FCA: 
101086418(ART1) 101096491(ART4) 101096839(ART5) 101099636(ART3) 101100540(SIRT6)
PTG: 
102949793(ART5) 102950272(ART1) 102956045(ART3) 102956235(SIRT6) 102960724(ART4)
BTA: 
407146(ART4) 407147(ART3) 407148 535416(SIRT6) 539042(ART1) 618664(ART5)
BOM: 
PHD: 
CHX: 
SSC: 
100126274(SIRT6) 100152653(ART4) 100522086(ART3) 100522939(ART5) 100525416(ART1)
CFR: 
102507660(ART4) 102512361(ART1) 102518432(ART5) 102519858(SIRT6) 102521392(ART3)
BACU: 
103000152 103001223(ART3) 103017769(SIRT6) 103018183(ART1) 103018994(ART5) 103020109(ART4)
LVE: 
103073305(ART3) 103079853(ART4) 103083699(ART5) 103083970(ART1) 103091498(SIRT6)
ECB: 
100051066(ART3) 100052937(ART1) 100063125(SIRT6) 100066272(ART5) 100067242(ART4)
MYB: 
102240257(ART3) 102244974(SIRT6) 102246125(ART4) 102249629(ART5) 102252898 102259501(ART1)
MYD: 
102757008(SIRT6) 102757044(ART5) 102757324(ART1) 102761825(ART4) 102771960(ART3) 102773420
PALE: 
102880138(ART3) 102884668(ART4) 102893459(SIRT6) 102895427 102896718(ART5) 102896969(ART1)
MDO: 
100016231(ART5) 100016271(ART1) 100022578(SIRT6) 100026013(ART3)
SHR: 
OAA: 
GGA: 
427879(ART4) 428123(MADPRT) 428124(ART7B) 428332(SIRT6) 429485(ART1) 430227(ART5)
MGP: 
TGU: 
FAB: 
PHI: 
APLA: 
FPG: 
FCH: 
CLV: 
ASN: 
AMJ: 
PSS: 
CMY: 
ACS: 
PBI: 
XLA: 
100037190 100126635(art1) 444018(sirt6) 779229(art5)
XTR: 
394980(sirt6) 496773(art5) 780139(art1)
DRE: 
415161(sirt6)
TRU: 
MZE: 
OLA: 
XMA: 
LCM: 
CMK: 
BFO: 
CIN: 
100170015(sir2-d)
SPU: 
DME: 
DAN: 
DER: 
DSE: 
DSI: 
DWI: 
DYA: 
DGR: 
DMO: 
DVI: 
AGA: 
AAG: 
CQU: 
AME: 
412846(Sirt6)
NVI: 
TCA: 
BMOR: 
API: 
PHU: 
ISC: 
CBR: 
CBG03922(Cbr-sir-2.4)
BMY: 
LOA: 
NVE: 
HMG: 
TAD: 
AQU: 
ATH: 
AT5G55760(SRT1)
ALY: 
CRB: 
EUS: 
CIT: 
CIC: 
TCC: 
GMX: 
PVU: 
CAM: 
FVE: 
PPER: 
CSV: 
RCU: 
POP: 
POPTR_0001s37680g(POPTRDRAFT_798160)
VVI: 
SLY: 
SOT: 
OSA: 
DOSA: 
Os04t0271000-01(Os04g0271000)
OBR: 
BDI: 
ZMA: 
542568(cl3393_1)
SITA: 
ATR: 
s00006p00244250(AMTR_s00006p00244250)
SMO: 
PPP: 
CRE: 
VCN: 
BPG: 
MIS: 
MPP: 
CSL: 
CVR: 
CME: 
GSL: 
CCP: 
PAN: 
NHE: 
MBR: 
ACAN: 
PTI: 
TPS: 
PIF: 
EHX: 
GTT: 
NGR: 
 » show all
Taxonomy
Reference
1  [PMID:225315]
  Authors
Moss J, Stanley SJ, Oppenheimer NJ.
  Title
Substrate specificity and partial purification of a stereospecific NAD- and guanidine-dependent ADP-ribosyltransferase from avian erythrocytes.
  Journal
J. Biol. Chem. 254 (1979) 8891-4.
  Organism
Meleagris gallopavo
Reference
2  [PMID:6247348]
  Authors
Moss J, Stanley SJ, Watkins PA.
  Title
Isolation and properties of an NAD- and guanidine-dependent ADP-ribosyltransferase from turkey erythrocytes.
  Journal
J. Biol. Chem. 255 (1980) 5838-40.
  Organism
Meleagris gallopavo
Reference
3  [PMID:3927821]
  Authors
Ueda K, Hayaishi O.
  Title
ADP-ribosylation.
  Journal
Annu. Rev. Biochem. 54 (1985) 73-100.
Reference
4  [PMID:12727863]
  Authors
Corda D, Di Girolamo M.
  Title
Functional aspects of protein mono-ADP-ribosylation.
  Journal
EMBO. J. 22 (2003) 1953-8.
  Organism
Homo sapiens, Mus musculus
Reference
5  [PMID:16627471]
  Authors
Paone G, Stevens LA, Levine RL, Bourgeois C, Steagall WK, Gochuico BR, Moss J
  Title
ADP-ribosyltransferase-specific modification of human neutrophil peptide-1.
  Journal
J. Biol. Chem. 281 (2006) 17054-60.
  Organism
Homo sapiens
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
81457-93-4

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