KEGG   ENZYME: 2.7.7.50Help
Entry
EC 2.7.7.50                 Enzyme                                 

Name
mRNA guanylyltransferase;
mRNA capping enzyme;
messenger RNA guanylyltransferase;
Protein lambda2
Class
Transferases;
Transferring phosphorus-containing groups;
Nucleotidyltransferases
BRITE hierarchy
Sysname
GTP:mRNA guanylyltransferase
Reaction(IUBMB)
GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA [RN:R03828]
Reaction(KEGG)
Substrate
GTP [CPD:C00044];
(5')ppPur-mRNA [CPD:C02100]
Product
diphosphate [CPD:C00013];
G(5')pppPur-mRNA [CPD:C02031]
Comment
The enzyme can also modify synthetic poly(A) and poly(G) to form the structures m7G(5')pppAn and m7G(5')pppGn.
History
EC 2.7.7.50 created 1981
Orthology
K00987  mRNA guanylyltransferase
K13917  mRNA-capping enzyme
K21243  Alphabaculovirus DNA-dependent RNA polymerase subunit LEF-4
Genes
HSA: 8732(RNGTT)
PTR: 462878(RNGTT)
PPS: 100993736(RNGTT)
GGO: 101136858(RNGTT)
PON: 100439097(RNGTT)
NLE: 100588336(RNGTT)
MCC: 702334(RNGTT) 721442(RNGTT)
MCF: 102125723(RNGTT)
CSAB: 103240079(RNGTT)
RRO: 104657908(RNGTT)
RBB: 108532637(RNGTT)
CJC: 100394937(RNGTT)
SBQ: 101049020(RNGTT)
MMU: 24018(Rngtt)
RNO: 313131(Rngtt)
CGE: 100770876(Rngtt)
NGI: 103733076(Rngtt)
HGL: 101697192(Rngtt)
OCU: 100340242(RNGTT)
TUP: 102495064(RNGTT)
CFA: 481914(RNGTT)
AML: 100483690(RNGTT)
UMR: 103659864(RNGTT)
ORO: 101370328(RNGTT)
FCA: 101096893(RNGTT)
PTG: 102959264(RNGTT)
AJU: 106972542(RNGTT)
BTA: 511408(RNGTT)
BOM: 102269511(RNGTT)
PHD: 102332851(RNGTT)
CHX: 102177341(RNGTT)
OAS: 101111376(RNGTT)
SSC: 100520874(RNGTT)
CFR: 102516343(RNGTT)
CDK: 105095541(RNGTT)
BACU: 103013048(RNGTT)
LVE: 103074545 103088328(RNGTT)
OOR: 101288281(RNGTT)
ECB: 100065700(RNGTT)
EPZ: 103549521(RNGTT)
EAI: 106826688(RNGTT)
MYB: 102249374(RNGTT)
MYD: 102770454(RNGTT)
HAI: 109389467(RNGTT)
RSS: 109440185 109453524(RNGTT)
PALE: 102887732(RNGTT)
LAV: 100671236(RNGTT)
MDO: 100025582(RNGTT)
SHR: 100921795(RNGTT)
OAA: 100082839(RNGTT)
GGA: 421819(RNGTT)
MGP: 100541550(RNGTT)
CJO: 107311978(RNGTT)
APLA: 101797459(RNGTT)
ACYG: 106035397(RNGTT)
TGU: 100232080(RNGTT)
GFR: 102031604(RNGTT)
FAB: 101811251(RNGTT)
PHI: 102104686(RNGTT)
PMAJ: 107201707(RNGTT)
CCW: 104694262(RNGTT)
FPG: 101910294(RNGTT)
FCH: 102049627(RNGTT)
EGZ: 104135255(RNGTT)
AAM: 106489707(RNGTT)
ASN: 102376947(RNGTT)
AMJ: 102570226(RNGTT)
PSS: 102453098(RNGTT)
CMY: 102935462(RNGTT)
CPIC: 101947951(RNGTT)
ACS: 100560223(rngtt)
PVT: 110076717(RNGTT)
PBI: 103048279(RNGTT)
GJA: 107115389(RNGTT)
XLA: 399383(rngtt.S)
XTR: 407900(rngtt)
NPR: 108785315(RNGTT)
DRE: 405803(rngtt)
SRX: 107731501 107742988(rngtt)
SANH: 107660510 107680298(rngtt)
SGH: 107554925 107562339(rngtt)
IPU: 108256101(rngtt)
AMEX: 103021656 111188703(rngtt)
TRU: 101079531(rngtt)
LCO: 104936194(rngtt)
NCC: 104946493
MZE: 101470505(rngtt)
OLA: 101173353(rngtt)
XMA: 102225982(rngtt)
PRET: 103457371(rngtt)
NFU: 107377729(rngtt)
KMR: 108233334(rngtt)
CSEM: 103381224(rngtt)
LCF: 108873496(rngtt)
SDU: 111239258(rngtt)
HCQ: 109508037(rngtt)
BPEC: 110173038(rngtt)
MALB: 109962341(rngtt)
SASA: 100380472(rngtt)
OTW: 112217500(rngtt)
ELS: 105017860(rngtt)
SFM: 108929338(rngtt)
LCM: 102352811 102363178(RNGTT)
CMK: 103186202(rngtt)
CIN: 100175699
SPU: 577418(RNGTT)
APLC: 110986220
SKO: 100369688
DME: Dmel_CG1810(mRNA-cap)
DER: 6550097
DSI: Dsimw501_GD15855(Dsim_GD15855)
DWI: 6648910
MDE: 101893695
AAG: 5575290
AME: 414001
BIM: 105680547
BTER: 105666294
SOC: 105198938
AEC: 105146621
ACEP: 105622221
PBAR: 105431161
HST: 105187685
DQU: 106746949
CFO: 105258636
LHU: 105671842
PGC: 109857824
PCF: 106787740
MDL: 106693755
TCA: 660879
DPA: 109537385
PMAC: 106714213
PRAP: 110994202
HAW: 110371116
PXY: 105397920
CLEC: 106667964
ZNE: 110830940
TUT: 107364579
CEL: CELE_C03D6.3(cel-1)
CBR: CBG03700(Cbr-cel-1) CBG03761
TSP: Tsp_02609
CRG: 105322687
MYI: 110442300
OBI: 106879186
LAK: 106153886
SHX: MS3_10256
EGL: EGR_03034
EPA: 110234355
ADF: 107343274
HMG: 100205625
CPAP: 110814241
CIT: 102609768
TCC: 18597604
EGR: 104426395
LJA: Lj0g3v0256839.1(Lj0g3v0256839.1) Lj0g3v0256839.2(Lj0g3v0256839.2) Lj1g3v0270180.1(Lj1g3v0270180.1) Lj1g3v4419670.1(Lj1g3v4419670.1) Lj1g3v4419670.2(Lj1g3v4419670.2) Lj1g3v4419670.3(Lj1g3v4419670.3) Lj3g3v1603870.1(Lj3g3v1603870.1) Lj3g3v1603870.2(Lj3g3v1603870.2)
CSV: 101209960
CMO: 103491007
MCHA: 111019426
CPEP: 111803494
VVI: 100256199
SIND: 105161563
OEU: 111373839
BVG: 104908854
SOE: 110804970
NNU: 104597018
DOSA: Os11t0217500-01(Os11g0217500) Os12t0193200-01(Os12g0193200)
ATS: 109749722(LOC109749722) 109782048(LOC109782048)
ZMA: 100193119(pco130460) 103646942
SITA: 101755911
MUS: 103992112
DCT: 110110603
PEQ: 110021775
ATR: 18436476
PPP: 112283864
CRE: CHLREDRAFT_191164(MRCE1)
SCE: YGL130W(CEG1)
ERC: Ecym_2188
KMX: KLMA_40549(CEG1)
NCS: NCAS_0D04100(NCAS0D04100)
NDI: NDAI_0I00830(NDAI0I00830)
TPF: TPHA_0E02770(TPHA0E02770)
TBL: TBLA_0A02070(TBLA0A02070)
TDL: TDEL_0E05370(TDEL0E05370)
KAF: KAFR_0K02360(KAFR0K02360)
PIC: PICST_34053(CEG1)
CAL: CAALFM_C405760WA(CGT1)
CDU: CD36_45420(CGT1)
CAUR: QG37_06650
SLB: AWJ20_1325(CEG1)
NCR: NCU06260
NTE: NEUTE1DRAFT81441(NEUTE1DRAFT_81441)
MGR: MGG_12831
TMN: UCRPA7_86
SSCK: SPSK_07590
MAW: MAC_03147
MAJ: MAA_05816
CMT: CCM_02636
BFU: BCIN_13g00390(Bcceg1)
MBE: MBM_04493
ANI: AN7473.2
ANG: ANI_1_1966024(An02g14240)
ABE: ARB_04899
TVE: TRV_05912
PTE: PTT_12153
SPO: SPBC2F12.08c(ceg1)
CNE: CNB01130
CNB: CNBB4580
MRR: Moror_853
ABP: AGABI1DRAFT52628(AGABI1DRAFT_52628)
ABV: AGABI2DRAFT148425(AGABI2DRAFT_148425)
MGL: MGL_4188
EHI: EHI_035610(17.t00048)
PYO: PY17X_1030500(PY05095)
TAN: TA12700
TPV: TP02_0352
BBO: BBOV_III006110(17.m07541)
CPV: cgd6_2380
SMIN: v1.2.036690.t1(symbB.v1.2.036690.t1)
 » show all
Taxonomy
Reference
1  [PMID:1058472]
  Authors
Ensinger MJ, Martin SA, Paoletti E, Moss B.
  Title
Modification of the 5'-terminus of mRNA by soluble guanylyl and methyl transferases from vaccinia virus.
  Journal
Proc Natl Acad Sci U S A 72:2525-9 (1975)
DOI:10.1073/pnas.72.7.2525
Reference
2  [PMID:629955]
  Authors
Groner Y, Gilboa E, Aviv H.
  Title
Methylation and capping of RNA polymerase II primary transcripts by HeLa nuclear homogenates.
  Journal
Biochemistry 17:977-82 (1978)
Reference
3  [PMID:3029058]
  Authors
Itoh N, Yamada H, Kaziro Y, Mizumoto K.
  Title
Messenger RNA guanylyltransferase from Saccharomyces cerevisiae. Large scale purification, subunit functions, and subcellular localization.
  Journal
J Biol Chem 262:1989-95 (1987)
  Sequence
[sce:YGL130W]
Reference
4  [PMID:1194287]
  Authors
Martin SA, Moss B.
  Title
Modification of RNA by mRNA guanylyltransferase and mRNA (guanine-7-)methyltransferase from vaccinia virions.
  Journal
J Biol Chem 250:9330-5 (1975)
Reference
5  [PMID:1194286]
  Authors
Martin SA, Paoletti E, Moss B.
  Title
Purification of mRNA guanylyltransferase and mRNA (guanine-7-) methyltransferase from vaccinia virions.
  Journal
J Biol Chem 250:9322-9 (1975)
Other DBs
ExplorEnz - The Enzyme Database: 2.7.7.50
IUBMB Enzyme Nomenclature: 2.7.7.50
ExPASy - ENZYME nomenclature database: 2.7.7.50
BRENDA, the Enzyme Database: 2.7.7.50
CAS: 56941-23-2

KEGG   ENZYME: 3.1.3.33Help
Entry
EC 3.1.3.33                 Enzyme                                 

Name
polynucleotide 5'-phosphatase;
5'-polynucleotidase
Class
Hydrolases;
Acting on ester bonds;
Phosphoric-monoester hydrolases
BRITE hierarchy
Sysname
polynucleotide 5'-phosphohydrolase
Reaction(IUBMB)
a 5'-phosphopolynucleotide + H2O = a polynucleotide + phosphate [RN:R02249]
Reaction(KEGG)
Substrate
5'-phosphopolynucleotide [CPD:C03475];
H2O [CPD:C00001]
Product
polynucleotide [CPD:C00419];
phosphate [CPD:C00009]
Comment
Does not act on nucleoside monophosphates. Induced in Escherichia coli by T-even phages.
History
EC 3.1.3.33 created 1972
Reference
1  [PMID:4289819]
  Authors
Becker A, Hurwitz J.
  Title
The enzymatic cleavage of phosphate termini from polynucleotides.
  Journal
J Biol Chem 242:936-50 (1967)
Other DBs
ExplorEnz - The Enzyme Database: 3.1.3.33
IUBMB Enzyme Nomenclature: 3.1.3.33
ExPASy - ENZYME nomenclature database: 3.1.3.33
BRENDA, the Enzyme Database: 3.1.3.33
CAS: 37288-17-8

DBGET integrated database retrieval system