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

BRENDA support

Literature summary for 2.7.7.50 extracted from

  • Luongo, C.L.; Reinisch, K.M.; Harrison, S.C.; Nibert, M.L.
    Identification of the guanylyltransferase region and active site in reovirus mRNA capping protein l2 (2000), J. Biol. Chem., 275, 2804-2810.
    View publication on PubMed
Search for more literature for 2.7.7.50

Cloned(Commentary)

Cloned (Comment) Organism
gene L2, expression of wild-type and mutant K226A protein lambda2 in Trichoplusia ni or Spodoptera frugiperda SF21 cells via baculovirus infection Mammalian orthoreovirus 3

Protein Variants

Protein Variants Comment Organism
K171A site-directed mutagenesis, 0.22% of wild-type autoguanylylation activity Mammalian orthoreovirus 3
K190A site-directed mutagenesis, autoguanylylation inactive Mammalian orthoreovirus 3
K197A site-directed mutagenesis, 7.5% of wild-type autoguanylylation activity Mammalian orthoreovirus 3
K226A site-directed mutagenesis, unaltered properties Mammalian orthoreovirus 3
K44A site-directed mutagenesis, approximately wild-type autoguanylylation activity levels Mammalian orthoreovirus 3
K89A site-directed mutagenesis, approximately wild-type autoguanylylation activity levels Mammalian orthoreovirus 3
K94A site-directed mutagenesis, approximately wild-type autoguanylylation activity levels Mammalian orthoreovirus 3

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
42000
-
 42000 kDa fragment harbors the autoguanylylation activity Mammalian orthoreovirus 3

Organism

Organism UniProt Comment Textmining
Mammalian orthoreovirus 3
-
-
-
Mammalian orthoreovirus 3
-
 from infected Trichoplusia ni insect cells via baculovirus
-
Mammalian orthoreovirus 3 Dearing
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant K226A from Trichoplusia ni or Spodoptera frugiperda SF21 cells via baculovirus infection Mammalian orthoreovirus 3

Reaction

Reaction Comment Organism Reaction ID
GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA active site Mammalian orthoreovirus 3
a
GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA active site Lys190 Mammalian orthoreovirus 3
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
GTP + pp(5')RNA GMP is linked to the enzyme via a phosphoamide bond Mammalian orthoreovirus 3 G(5')ppp(5')RNA + diphosphate guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue r
GTP + pp(5')RNA enzyme can transfer its bound GMP to GDP Mammalian orthoreovirus 3 G(5')ppp(5')RNA + diphosphate guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue r
GTP + pp(5')RNA formation of a covalent intermediate enzyme-GMP Mammalian orthoreovirus 3 G(5')ppp(5')RNA + diphosphate guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue r
GTP + pp(5')RNA GMP is linked to the enzyme via a phosphoamide bond Mammalian orthoreovirus 3 Dearing G(5')ppp(5')RNA + diphosphate guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue r
GTP + pp(5')RNA enzyme can transfer its bound GMP to GDP Mammalian orthoreovirus 3 Dearing G(5')ppp(5')RNA + diphosphate guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue r
GTP + pp(5')RNA formation of a covalent intermediate enzyme-GMP Mammalian orthoreovirus 3 Dearing G(5')ppp(5')RNA + diphosphate guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue r
additional information autoguanylylation Mammalian orthoreovirus 3 ?
-
 ?
additional information autoguanylylation Mammalian orthoreovirus 3 Dearing ?
-
 ?

Subunits

Subunits Comment Organism
More 42000 kDa fragment harbors the autoguanylylation activity Mammalian orthoreovirus 3