KEGG   ENZYME: 3.2.2.6Help
Entry
EC 3.2.2.6                  Enzyme                                 

Name
ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase;
NAD+ nucleosidase;
NADase (ambiguous);
DPNase (ambiguous);
DPN hydrolase (ambiguous);
NAD hydrolase (ambiguous);
nicotinamide adenine dinucleotide nucleosidase (ambiguous);
NAD glycohydrolase (misleading);
NAD nucleosidase (ambiguous);
nicotinamide adenine dinucleotide glycohydrolase (misleading);
CD38 (gene name);
BST1 (gene name)
Class
Hydrolases;
Glycosylases;
Hydrolysing N-glycosyl compounds
BRITE hierarchy
Sysname
NAD+ glycohydrolase (cyclic ADP-ribose-forming)
Reaction(IUBMB)
NAD+ + H2O = ADP-D-ribose + nicotinamide (overall reaction) [RN:R00102];
(1a) NAD+ = cyclic ADP-ribose + nicotinamide [RN:R10629];
(1b) cyclic ADP-ribose + H2O = ADP-D-ribose [RN:R10630]
Reaction(KEGG)
Substrate
NAD+ [CPD:C00003];
H2O [CPD:C00001];
cyclic ADP-ribose [CPD:C13050]
Product
ADP-D-ribose [CPD:C00301];
nicotinamide [CPD:C00153];
cyclic ADP-ribose [CPD:C13050]
Comment
This multiunctional enzyme acts on NAD+, catalysing both the synthesis and hydrolysis of cyclic ADP-ribose, a calcium messenger that can mobilize intracellular Ca2+ stores and activate Ca2+ influx to regulate a wide range of physiological processes. In addition, the enzyme also catalyses EC 2.4.99.20, 2'-phospho-ADP-ribosyl cyclase/2'-phospho-cyclic-ADP-ribose transferase. It is also able to act on beta-nicotinamide D-ribonucleotide. cf. EC 3.2.2.5, NAD+ glycohydrolase.
History
EC 3.2.2.6 created 1961, modified 2004, modified 2014, modified 2018
Pathway
ec00760  Nicotinate and nicotinamide metabolism
ec01100  Metabolic pathways
Orthology
K01242  ADP-ribosyl cyclase 1
K18152  ADP-ribosyl cyclase 2
Genes
HSA: 683(BST1) 952(CD38)
PTR: 461126(BST1) 745433(CD38)
PPS: 100972434(BST1) 100974952(CD38)
GGO: 101145401(BST1) 101149825(CD38)
PON: 100174150(BST1) 100457558(CD38)
NLE: 100606064(BST1) 100606960(CD38)
MCC: 714399(CD38) 722848(BST1)
MCF: 101926698(BST1) 102126394(CD38)
CSAB: 103246326(CD38) 103246328(BST1)
RRO: 104658167(BST1) 104658170(CD38)
RBB: 108531741(CD38) 108531746(BST1)
CJC: 100387937(CD38) 100402445(BST1)
SBQ: 101035567(BST1) 101036203(CD38)
MMU: 12182(Bst1) 12494(Cd38)
RNO: 25668(Cd38) 81506(Bst1)
CGE: 100773187(Cd38) 100773468(Bst1)
NGI: 103728882(Cd38) 103728884(Bst1)
HGL: 101713685(Bst1) 101720283(Cd38)
CCAN: 109691561(Cd38) 109691564(Bst1)
OCU: 100009409(CD38) 100351817(BST1)
TUP: 102468679(BST1) 102480083(CD38)
CFA: 403756(CD38) 488820(BST1)
AML: 100463977(BST1) 100481326(CD38)
UMR: 103658313(BST1) 103658362(CD38)
ORO: 101364829(CD38) 101365133(BST1)
FCA: 101101052(BST1) 101101308(CD38)
PTG: 102955186(CD38) 102962771(BST1)
AJU: 106975627(BST1) 106975653(CD38)
BTA: 327677(CD38) 616757(BST1)
BOM: 102271683(BST1) 102273331(CD38)
BIU: 109560088(BST1) 109560687(CD38)
PHD: 102322294(CD38) 102322993(BST1)
CHX: 102169848(BST1) 102172881(CD38)
OAS: 101116575(BST1)
SSC: 100511702(CD38) 100625942(BST1)
CFR: 102508026(CD38) 102508256(BST1)
CDK: 105098338(BST1) 105098339(CD38)
BACU: 103000954(BST1) 103020545(CD38)
LVE: 103087769(CD38) 103088314(BST1)
OOR: 101284537(CD38) 101284786(BST1)
ECB: 100068959(CD38) 100068968(BST1)
EPZ: 103565758(BST1) 103565759(CD38)
EAI: 106827091(CD38) 106827092(BST1)
MYB: 102252244(CD38) 102252530(BST1)
MYD: 102759158(CD38) 102770056(BST1)
HAI: 109372167(CD38) 109372831(BST1)
RSS: 109435264(CD38) 109452142(BST1)
PALE: 102884937(BST1) 102889755(CD38)
LAV: 100659997(BST1) 100660287(CD38)
MDO: 100015733(BST1) 103094598(CD38)
SHR: 100915627(BST1) 105751033(CD38)
OAA: 100074315(CD38) 100079912(BST1)
GGA: 422827(CD38) 422828(BST1)
MGP: 100546297(BST1) 100548136(CD38)
CJO: 107313950(BST1) 107313951(CD38)
APLA: 101799363(BST1)
ACYG: 106033418(CD38) 106035386(BST1)
TGU: 100224783(BST1) 101232999(CD38)
GFR: 102032481(BST1) 102032646(CD38)
FAB: 101808664(BST1) 101813225(CD38)
PHI: 102100836(CD38) 102101014(BST1)
CCW: 104690721 104690901(CD38)
FPG: 101912278(CD38) 101917967(BST1)
FCH: 102048375(CD38) 102048871(BST1)
CLV: 102089855(BST1)
EGZ: 104134476(BST1) 104134477(CD38)
ASN: 102376962(BST1)
AMJ: 102559494(BST1)
PSS: 102444728(BST1) 102444963(CD38)
CMY: 102933631(BST1) 102933862(CD38)
CPIC: 101935271(BST1) 101935553(CD38)
ACS: 100566030(cd38)
PVT: 110085956(CD38)
PBI: 103059310
GJA: 107120012(CD38)
XLA: 100036901(cd38.L) 100873156(cd38b) 101027297(bst1.L)
XTR: 101733556(bst1) 496666(cd38)
NPR: 108799310(BST1) 108799313
DRE: 101886891
SRX: 107750973(cd38)
SANH: 107693813
SGH: 107568972
CCAR: 109104929(cd38)
AMEX: 103029242
HCQ: 109517521
ELS: 105031580
SPU: 100126187(arc3) 100859964(arc4) 576085(arc2) 580868(arc1)
SKO: 100370260
CRG: 105319809
 » show all
Taxonomy
Reference
1  [PMID:2613697]
  Authors
Imai T
  Title
Purification and characterization of a pyridine nucleotide glycohydrolase from rabbit spleen.
  Journal
J Biochem 106:928-37 (1989)
Reference
2  [PMID:8235624]
  Authors
Howard M, Grimaldi JC, Bazan JF, Lund FE, Santos-Argumedo L, Parkhouse RM, Walseth TF, Lee HC
  Title
Formation and hydrolysis of cyclic ADP-ribose catalyzed by lymphocyte antigen CD38.
  Journal
Science 262:1056-9 (1993)
DOI:10.1126/science.8235624
Reference
3  [PMID:8253715]
  Authors
Takasawa S, Tohgo A, Noguchi N, Koguma T, Nata K, Sugimoto T, Yonekura H, Okamoto H
  Title
Synthesis and hydrolysis of cyclic ADP-ribose by human leukocyte antigen CD38 and inhibition of the hydrolysis by ATP.
  Journal
J Biol Chem 268:26052-4 (1993)
  Sequence
[hsa:952]
Reference
4  [PMID:7961800]
  Authors
Tohgo A, Takasawa S, Noguchi N, Koguma T, Nata K, Sugimoto T, Furuya Y, Yonekura H, Okamoto H
  Title
Essential cysteine residues for cyclic ADP-ribose synthesis and hydrolysis by CD38.
  Journal
J Biol Chem 269:28555-7 (1994)
Reference
5  [PMID:7663169]
  Authors
Fryxell KB, O'Donoghue K, Graeff RM, Lee HC, Branton WD
  Title
Functional expression of soluble forms of human CD38 in Escherichia coli and Pichia pastoris.
  Journal
Protein Expr Purif 6:329-36 (1995)
DOI:10.1006/prep.1995.1043
Reference
6  [PMID:11866528]
  Authors
Yamamoto-Katayama S, Ariyoshi M, Ishihara K, Hirano T, Jingami H, Morikawa K.
  Title
Crystallographic studies on human BST-1/CD157 with ADP-ribosyl cyclase and NAD glycohydrolase activities.
  Journal
J Mol Biol 316:711-23 (2002)
DOI:10.1006/jmbi.2001.5386
  Sequence
[hsa:683]
Reference
7  [PMID:16154090]
  Authors
Liu Q, Kriksunov IA, Graeff R, Munshi C, Lee HC, Hao Q
  Title
Crystal structure of human CD38 extracellular domain.
  Journal
Structure 13:1331-9 (2005)
DOI:10.1016/j.str.2005.05.012
  Sequence
[hsa:952]
Other DBs
ExplorEnz - The Enzyme Database: 3.2.2.6
IUBMB Enzyme Nomenclature: 3.2.2.6
ExPASy - ENZYME nomenclature database: 3.2.2.6
BRENDA, the Enzyme Database: 3.2.2.6
CAS: 9032-65-9

DBGET integrated database retrieval system