Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.1.1.56 - mRNA (guanine-N7)-methyltransferase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P32783

for references in articles please use BRENDA:EC2.1.1.56
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.1 Methyltransferases
                2.1.1.56 mRNA (guanine-N7)-methyltransferase
IUBMB Comments
The terminal N7-methylguanosine facilitates gene expression in eukaryotic cells and is recognized by cap-binding proteins.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Saccharomyces cerevisiae
UNIPROT: P32783
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
Synonyms
non-structural protein 1, nsp14, cap methyltransferase, n7-mtase, mrna cap methyltransferase, nonstructural protein 14, tbcmt1, n7-methyltransferase, tbcgm1, guanine-n7 methyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
guanine-7-methyltransferase
-
-
-
-
messenger ribonucleate guanine 7-methyltransferase
-
-
-
-
messenger RNA guanine 7-methyltransferase
-
-
-
-
methyltransferase, messenger ribonucleate guanine 7-
-
-
-
-
mRNA cap (guanine-N7) methyltransferase
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:mRNA (guanine-N7)-methyltransferase
The terminal N7-methylguanosine facilitates gene expression in eukaryotic cells and is recognized by cap-binding proteins.
CAS REGISTRY NUMBER
COMMENTARY hide
56941-25-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
show the reaction diagram
-
-
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
show the reaction diagram
-
methylates also undermethylated poly(A)-rich mRNA
R may be guanosine or adenosine, mRNA containing an N7-methylguanine cap
?
S-adenosyl-L-methionine + GpppA
S-adenosyl-L-homocysteine + m7GpppA
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KCl
-
no activation
Mg2+
-
inactivation
Mn2+
-
inhibition
additional information
-
no activation by NaCl
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-homocysteine
sinefungin
-
extremely potent inhibitor, binds 900fold more avidly than S-adenosylhomocysteine or S-adenosylmethionine, sensitivity to growth inhibition is diminished when Abd1 is overexpressed
additional information
-
inhibition by a natural low-molecular-weight inhibitor in the crude extract, removed during purification
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.002 - 0.006
S-adenosyl-L-methionine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0983
GpppA
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.021
S-adenosyl-L-homocysteine
Saccharomyces cerevisiae
-
-
0.000021
sinefungin
Saccharomyces cerevisiae
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00000235
-
purified enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 8
-
half-maximal activity at pH 5.0, unstable above pH 8.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
49000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 49000, SDS-PAGE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, several months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
His6-Smt3-Abd1 by nickel-nitrilotriacetic acid fast flow column chromatography, Abd1 free of the tag by gel filtration, to homogeneity
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Saccharomyces cerevisiae, His-tagged, amino acid sequence analysis
as a His6-Smt3 fusion protein in Escherichia coli BL21(DE3) CodonPlus RIL using a pET-based pSmt3-TOPO vector
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
-
cap methylation is a principal target of the antifungal activity of sinefungin
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Locht, C.; Beaudart, J.L.; Delcour, J.
Partial purification and characterization of mRNA (guanine-7-) methyltransferase from the yeast Saccharomyces cerevisiae
Eur. J. Biochem.
134
117-121
1983
Saccharomyces cerevisiae, Saccharomyces cerevisiae VY1160
Manually annotated by BRENDA team
Tsukamoto, T.; Shibagaki, Y.; Niikura, Y.; Mizumoto, K.
Cloning and characterization of three human cDNAs encoding mRNA (guanine-7-)-methyltransferase, an mRNA cap methylase
Biochem. Biophys. Res. Commun.
251
27-34
1998
Homo sapiens, Saccharomyces cerevisiae (P32783)
Manually annotated by BRENDA team
Zheng, S.; Hausmann, S.; Liu, Q.; Ghosh, A.; Schwer, B.; Lima, C.D.; Shuman, S.
Mutational analysis of Encephalitozoon cuniculi mRNA cap (guanine-N7) methyltransferase, structure of the enzyme bound to sinefungin, and evidence that cap methyltransferase is the target of sinefungins antifungal activity
J. Biol. Chem.
281
35904-35913
2006
Saccharomyces cerevisiae, Encephalitozoon cuniculi (Q8SR66), Encephalitozoon cuniculi
Manually annotated by BRENDA team