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Literature summary for 2.7.7.50 extracted from

  • 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 (1998), J. Biol. Chem., 273, 9577-9585.
    View publication on PubMed
Search for more literature for 2.7.7.50

Cloned(Commentary)

Cloned (Comment) Organism
expression of His-tagged full length enzyme, residues 211-597, comprising the catalytical domain, and residues 1-210 in Escherichia coli BL21(DE3) Mus musculus
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 Mus musculus
mRNA capping enzyme, DNA sequence determination and analysis Mus musculus

Protein Variants

Protein Variants Comment Organism
K294A inactive, no functional complementation of the deficient Saccharomyces cerevisiae mutant Mus musculus

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ optimal at 5-10 mM Mus musculus
Mg2+ enzyme-GMP intermediate formation is strictly dependent on divalent cations, satisfied by Mn2+ or Mg2+, Mn2+ is slightly preferred Mus musculus
Mn2+ enzyme-GMP intermediate formation is strictly dependent on divalent cations, satisfied by Mn2+ or Mg2+, Mn2+ is slightly preferred Mus musculus
Mn2+ optimal at 1-2 mM Mus musculus
additional information requirement for divalent cations Mus musculus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
28000
-
 catalytically active residues 211-597, i.e. RNA guanylyltransferase domain, glycerol gradient sedimentation Mus musculus
46000
-
 residues 1-210, i.e. RNA triphosphatase domain, glycerol gradient sedimentation Mus musculus
68000
-
 mRNA capping enzyme, glycerol density gradient sedimentation Mus musculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
GTP + pp(5')RNA Mus musculus mouse guanylyltransferase domain can substitute the deficient enzyme in Saccharomyces cerevisiae mutant in vivo G(5')ppp(5')RNA + diphosphate guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue ?

Organism

Organism UniProt Comment Textmining
Mus musculus O55236 mRNA capping enzyme
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged full length enzyme as well as the recombinant His-tagged N-terminal and C-terminal domains from Escherichia coli BL21(DE3) Mus musculus

Reaction

Reaction Comment Organism Reaction ID
GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA guanylyltransferase domain: residues 211-597 Mus musculus
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
GTP + pp(5')RNA the enzymes isolated guanylyltransferase domian, residues 211-597, is catalytically active in vitro Mus musculus 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 formation of a covalent intermediate enzyme-GMP Mus musculus 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 mouse guanylyltransferase domain can substitute the deficient enzyme in Saccharomyces cerevisiae mutant in vivo Mus musculus G(5')ppp(5')RNA + diphosphate guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue ?

Subunits

Subunits Comment Organism
monomer 1 * 46000, catalytically active residues 211-597, i.e. guanylyltransferase domain, + 1 * 28000, residues 1-210, i.e. RNA triphosphatase domain, SDS-PAGE Mus musculus

Synonyms

Synonyms Comment Organism
More 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 Mus musculus