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3.2.2.16: methylthioadenosine nucleosidase

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

Word Map on EC 3.2.2.16

Reaction

S-methyl-5'-thioadenosine
+
H2O
=
S-methyl-5-thio-D-ribose
 +
adenine

Synonyms

5'-deoxy-5'-methylthioadenosine nucleosidase, 5'-methylthioadenosine nucleosidase, 5'-methylthioadenosine/S-adenosyl-L-homocysteine nucleosidase, 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase, 5-methylthioadenosine nucleosidase, 5-methylthioadenosine/S-adenosylhomocysteine nucleosidase, 50-methylthioadenosine/S-adenosylhomocysteine nucleosidase, adoHcy/MTA nucleosidase, Bgp protein, glycosaminoglycan-binding protein, HpyMqnB, lupin MeSAdo nucleosidase, MeSAdo nucleosidase, methylthioadenosine nucleosidase, methylthioadenosine/S-adenosylhomocysteine nucleosidase, MqnB, MTA nucleosidase, MTA ribohydrolase, MTA/SAH nucleosidase, MTAN, MTAN1, MTAN2, MTN, Pfs, Pfs protein, plant specific MTA nucleosidase, S-adenosylhomocysteine/5'-methylthioadenosine nucleosidase

ECTree

     3 Hydrolases
         3.2 Glycosylases
             3.2.2 Hydrolysing N-glycosyl compounds
                3.2.2.16 methylthioadenosine nucleosidase

Engineering

Engineering on EC 3.2.2.16 - methylthioadenosine nucleosidase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A15M
the mutant exhibits less than 16% catalytic efficiency compared to the wild type
M144A
the mutant exhibits less than 1% catalytic efficiency compared to the wild type
R164A
the variant displays catalytic efficiencies of less than 20% compared to the wild type
R85A
the mutant exhibits less than 8% catalytic efficiency compared to the wild type
R85H
the mutant exhibits less than 9% catalytic efficiency compared to the wild type
S167A
the mutant exhibits less than 6% catalytic efficiency compared to the wild type
V34A
the mutant exhibits less than 19% catalytic efficiency compared to the wild type
V34I
the mutant exhibits less than 22% catalytic efficiency compared to the wild type
W179A
the mutant exhibits less than 7% catalytic efficiency compared to the wild type
W179F
the mutant exhibits less than 3% catalytic efficiency compared to the wild type
Y134A
the mutant exhibits less than 1% catalytic efficiency compared to the wild type
Y134F
the mutant exhibits less than 1% catalytic efficiency compared to the wild type
E174Q
-
site-directed mutagenesis, structure comparison with the wild-type enzyme
D199A
D199N
F107A
the mutant shows reduced activity compared to the wild type enzyme
H109A
the mutant shows reduced activity compared to the wild type enzyme
D211N
-
the mutation completely abolishes enzyme activity
E188Q
-
the mutant shows only trace amounts of activity towards 5'-methylthioadenosine
E24Q
-
the mutation completely abolishes enzyme activity
F134L
-
the mutant acquires the ability to hydrolyze S-adenosyl-L-homocysteine
F104C/C186S
the mutant shows reduced activity compared to the wild type
A113P
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
A113P/V153I
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
A113P/V153I/R158G
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
V153I
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
additional information
-
residues L181/M168 and F148/L135 in isoforms MTAN1 and MTAN2, respectively, are responsible for the divergence in specificity of the isoforms