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2.7.7.52: RNA uridylyltransferase

This is an abbreviated version!
For detailed information about RNA uridylyltransferase, go to the full flat file.

Word Map on EC 2.7.7.52

Reaction

UTP
+
RNAn
=
diphosphate
 +
RNAn+3'-U

Synonyms

3' terminal uridylyl transferase, 3'-terminal uridylyl transferase 1, At2g45620, caffeine-induced death suppressor protein 1, Cid1, GLD2, HESO1, MEAT1, mitochondrial editosome-like complex associated TUTase 1, More, RET, RET1, RET2, RNA editing TUTase, RNA silencing protein 1, Rsp1, Tailor, TbMP57 TUTase, TbTUT3, TbTUT4, terminal RNA uridylyltransferase, terminal U transferase (TUTase), terminal uridylyl transferase, terminal uridylyltransferase, terminal uridylyltransferase Tailor, TNTase CG1091, TUT, TUT1, TUT2, TUT4, TUT7, TUTase, TUTase 1, TUTase 2, TUTase 3, TUTase 4, TUTase4, TUTase6, TUTase7, U6 snRNA-specific terminal uridylyltransferase, U6-TUTase, uridylyltransferase, terminal, URT1, UTP: RNA uridylyltransferase, UTP:RNA uridylyltransferase 1, Zcchc11, ZCCHC6

ECTree

     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.7 Nucleotidyltransferases
                2.7.7.52 RNA uridylyltransferase

Engineering

Engineering on EC 2.7.7.52 - RNA uridylyltransferase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D491A/D493A
complete loss of activity
D547A
catalytically dead mutant
D491A/D493A
-
complete loss of activity
-
D280A
the mutation abrogates enzyme activity
H294A
the enzymatic activity of the mutant is reduced by about 61% as compared to the wild type enzyme
N347A
the uridylation efficiency of the mutant is reduced dramatically to about 7% when compared with that of wild type enzyme
Q519A
the activity of the mutant is reduced compared to the wild type enzyme. The mutant tails 3'-G, 3'-A and 3'-C substrates with comparable efficiencies
R295A
the enzymatic activity of the mutant is reduced by about 84% as compared to the wild type enzyme
R295K
the enzymatic activity of the mutant is reduced by about 80% as compared to the wild type enzyme
R327A
R327K
V328I
the mutation barely affects the enzyme's binding with RNA substrate and also exhibits a obvious reduction in uridylation efficiency as compared to the wild type enzyme
V328L
the mutation entirely abolishes the enzyme's catalytic activity for truncated miR-1003 bearing 3'G. The mutation barely affects the enzyme's binding with RNA substrate
V328R
the mutation entirely abolishes the enzyme's catalytic activity for truncated miR-1003 bearing 3'G. The mutation barely affects the enzyme's binding with RNA substrate
C306A/C309A
the mutant does not oligo-uridylylate pre-let-7a-1 RNA in the presence of Lin28A
H405A/K452A
the mutant shows reduced oligo-uridylylation of pre-let-7a-1 RNA in the presence of Lin28A compared to the wild type enzyme
K321A/K324A
the mutant shows severely reduced oligo-uridylylation of pre-let-7a-1 RNA in the presence of Lin28A compared to the wild type enzyme
K326A/R327A
the mutant shows severely reduced oligo-uridylylation of pre-let-7a-1 RNA in the presence of Lin28A compared to the wild type enzyme
K329A/K330A
the mutant shows strongly reduced oligo-uridylylation of pre-let-7a-1 RNA in the presence of Lin28A compared to the wild type enzyme
R669A/R670A
the mutant shows strongly reduced oligo-uridylylation of pre-let-7a-1 RNA in the presence of Lin28A compared to the wild type enzyme
R779A/R783A
the mutations reduce the RNA-binding and uridylylation activities of the enzyme
R871A/K874A
the mutations reduce the RNA-binding activity of the enzyme
C83F
-
230% of wild-type activity for transfer to terminal U residue
D297A
Km=0.1728 (UTP), kcat=0.00033/sec (UTP)
D297N
Km=0.0139 (UTP), kcat=0.0000666/sec (UTP)
D97A
-
complete inactivation of uridylyl transfer
E300A
Km=0.3084 (UTP), kcat=0.0066/sec (UTP)
K149A
-
mutant retains partial activity
N147A
Km=0.1153 (UTP), kcat=0.005/sec (UTP)
R121A
Km=0.0028 (UTP), kcat=0.000033/sec (UTP),Km=0.132 (RNA), kcat= 0.005/sec (RNA)
R141A
R144A
-
almost complete inactivation of uridylyl transfer
R307A
Km=0.0004 (UTP), kcat=0.000133/sec (UTP), Km=0.01 (RNA), kcat= 0.00833/sec (RNA)
R435A
-
almost complete inactivation of uridylyl transfer
S148A
Km=0.0873 (UTP), kcat=0.021/sec (UTP), Km=0.0002 (RNA), kcat= 0.0166/sec (RNA)
S188A
Km=0.034 (UTP), kcat=0.0005/sec (UTP), Km=0.0003 (RNA), kcat= 0.00166/sec (RNA)
V271R
-
10-20% of wild-type activity
V271R/C83F
-
240% of wild-type activity for transfer to terminal U residue
Y189F
Km=0.0213 (UTP), kcat=0.015/sec (UTP)
Y319A
-
complete inactivation of uridylyl transfer
additional information
-
mutations of metal coordinating catalytic aspartic residues D66, D68 and D136, render TUT4 inactive but have no effect on UTP binding