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Information on EC 2.7.7.50 - mRNA guanylyltransferase and Organism(s) Mus musculus and UniProt Accession O55236
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2.7.7.50 mRNA guanylyltransferaseIUBMB Comments
The human enzyme is a multi domain protein that also has the activity of EC 3.6.1.74, mRNA 5'-phosphatase.
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Word Map
- 2.7.7.50
- cyclin
- photosystem
- thylakoids
-
photoinhibition
- chloroplast
- cyanobacterium
- chlorophyll
- synechocystis
-
photodamage
-
photochemical
- triphosphatase
- retinoblastoma
-
cyclin-dependent
- vaccinia
- reinhardtii
-
high-light
-
photoprotection
- 5'-triphosphatase
- qa
-
mantle
- plastoquinone
- synechococcus
-
oxygen-evolving
-
thermoluminescence
-
photoinactivation
-
xanthophyl
- 7-methylguanosine
- atrazine
-
water-splitting
- p-tefb
- lhcii
-
non-photochemical
-
alpha-32pgtp
-
water-oxidizing
-
chloroplast-encoded
- biotechnology
- vp3
- diuron
- nsp1
-
low-light
- lincomycin
-
grana
-
herbicide-resistant
- analysis
- psbo
- reoviridae
-
cap-binding
- spt5
-
photoinhibitory
-
flash-induced
-
uncapped
- thermosynechococcus
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
d1 protein, guanylyltransferase, capping enzyme, mrna capping enzyme, rna guanylyltransferase, mrna guanylyltransferase, prntase, rna capping enzyme, mrna-cap, mrna-capping enzyme, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Ceg1
-
-
-
-
messenger RNA guanylyltransferase
-
-
-
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protein lambda2
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-
-
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RNGTT
-
-
-
-
additional information
enzyme is part of the bifunctional capping enzyme, which consists of autonomous and non-overlapping RNA 5'-triphosphatase and a RNA guanylyltransferase domain and activity
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA
guanylyltransferase domain: residues 211-597
GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA
conserved KXDG-motif
GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA
Lys294 is located in the active site in a KXDG-conserved motif
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nucleotidyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
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-
SYSTEMATIC NAME
IUBMB Comments
GTP:mRNA guanylyltransferase
The human enzyme is a multi domain protein that also has the activity of EC 3.6.1.74, mRNA 5'-phosphatase.
CAS REGISTRY NUMBER
COMMENTARY
56941-23-2
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
?
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
the enzymes isolated guanylyltransferase domian, residues 211-597, is catalytically active in vitro
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
?
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
formation of a covalent intermediate enzyme-GMP
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
?
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
mouse guanylyltransferase domain can substitute the deficient enzyme in Saccharomyces cerevisiae mutant in vivo
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
?
additional information
?
-
enzyme also contains RNA 5'-triphosphatase activity, located at the N-terminus
-
-
?
additional information
?
-
-
enzyme also contains RNA 5'-triphosphatase activity, located at the N-terminus
-
-
?
additional information
?
-
phosphorylated C-terminal domain of RNA polymerase II couples capping to transcription elongation, which results in selective capping of RNA polymerase II transcripts
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-
?
additional information
?
-
-
phosphorylated C-terminal domain of RNA polymerase II couples capping to transcription elongation, which results in selective capping of RNA polymerase II transcripts
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
mouse guanylyltransferase domain can substitute the deficient enzyme in Saccharomyces cerevisiae mutant in vivo
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
?
additional information
?
-
phosphorylated C-terminal domain of RNA polymerase II couples capping to transcription elongation, which results in selective capping of RNA polymerase II transcripts
-
-
?
additional information
?
-
-
phosphorylated C-terminal domain of RNA polymerase II couples capping to transcription elongation, which results in selective capping of RNA polymerase II transcripts
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
additional information
Mg2+
enzyme-GMP intermediate formation is strictly dependent on divalent cations, satisfied by Mn2+ or Mg2+, Mn2+ is slightly preferred
Mn2+
enzyme-GMP intermediate formation is strictly dependent on divalent cations, satisfied by Mn2+ or Mg2+, Mn2+ is slightly preferred
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MCE1_MOUSE
597
0
68684
Swiss-Prot
Mitochondrion (Reliability: 4)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
28000
catalytically active residues 211-597, i.e. RNA guanylyltransferase domain, glycerol gradient sedimentation
46000
residues 1-210, i.e. RNA triphosphatase domain, glycerol gradient sedimentation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
1 * 46000, catalytically active residues 211-597, i.e. guanylyltransferase domain, + 1 * 28000, residues 1-210, i.e. RNA triphosphatase domain, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K294A
additional information
K294A
inactive, no functional complementation of the deficient Saccharomyces cerevisiae mutant
K294A
site-directed mutagenesis, no remaining guanylylation activity, no complementation of a deficient Saccharomyces mutant, RNA 5'-triphosphatase activity is retained
additional information
construction of N-terminally truncated mutant consisting of residues 438-597, N-terminal truncation eliminates the RNA 5'-triphosphatase activity
additional information
-
construction of N-terminally truncated mutant consisting of residues 438-597, N-terminal truncation eliminates the RNA 5'-triphosphatase activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged full length enzyme as well as the recombinant His-tagged N-terminal and C-terminal domains from Escherichia coli BL21(DE3)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, expression of truncation mutant in Escherichia coli BL21(DE3) and wild-type and mutant K294A enzyme in Saccharomyces haploid deficient mutant strain, functional complementation of the latter by wild-type enzyme
expression of His-tagged full length enzyme, residues 211-597, comprising the catalytical domain, and residues 1-210 in Escherichia coli BL21(DE3)
expression of wild-type full length enzyme and catalytic domain in deficient Saccharomyces cerevisiae strain YBS2 as His-tagged protein, functional complementation by both of them
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yue, Z.; Maldonado, E.; Pillutla, R.; Cho, H.; Reinberg, D.; Shatkin, A.J.
Mammalian capping enzyme complements mutant Saccharomyces cerevisiae lacking mRNA guanylyltransferase and selectively binds the elongating form of RNA polymerase II
Proc. Natl. Acad. Sci. USA
94
12898-12903
1997
Mus musculus (O55236), Mus musculus, Homo sapiens (O60942), Homo sapiens
Ho, C.K.; Sriskanda, V.; McCracken, S.; Bentley, D.; Schwer, B.; Shuman, S.
The guanylyltransferase domain of mammalian mRNA capping enzyme binds to the phosphorylated carboxyl-terminal domain of RNA polymerase II
J. Biol. Chem.
273
9577-9585
1998
Mus musculus (O55236), Mus musculus
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