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2.4.2.28: S-methyl-5'-thioadenosine phosphorylase

This is an abbreviated version!
For detailed information about S-methyl-5'-thioadenosine phosphorylase, go to the full flat file.

Word Map on EC 2.4.2.28

Reaction

S-methyl-5'-thioadenosine
+
phosphate
=
adenine
 +
S-methyl-5-thio-alpha-D-ribose 1-phosphate

Synonyms

5'-deoxy-5'-methylthioadenosine phosphorylase, 5'-deoxy-5'-methylthioadenosine phosphorylase II, 5'-deoxy-5'-methylthioadenosine:orthophosphate methylthioribosyltransferase, 5'-methylthioadenosine nucleosidase, 5'-methylthioadenosine phosphorylase, 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase, 5-methylthioadenosine phosphorylase, 5’-methylthioadenosine phosphorylase, MeSAdo phosphorylase, MeSAdo/Ado phosphorylase, methylthioadenosine nucleosidase, methylthioadenosine nucleoside phosphorylase, methylthioadenosine phosphorylase, MTA phosphorylase, MTAN, MTAN1, MTAN2, MTAP, Mtap protein, MTAPase, MTN1, MTN2, PfMTAP, phosphorylase, methylthioadenosine, RSFP, Rv0535, SsMTAP, SsMTAP II, SsMTAPII, SSO2343

ECTree

     2 Transferases
         2.4 Glycosyltransferases
             2.4.2 Pentosyltransferases
                2.4.2.28 S-methyl-5'-thioadenosine phosphorylase

Engineering

Engineering on EC 2.4.2.28 - S-methyl-5'-thioadenosine phosphorylase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F135L
can reduce steric hindrance at the end of the 5'-alkylthio binding subsite, so that longer 5'-substituents may be accommodated more easily in the MTAN2 active site
F148L
can reduce steric hindrance at the end of the 5'-alkylthio binding subsite
I132V
no significant structural change
I145V
no significant structural change
L168M
has a more extended side chain, may affect the binding of ligands at the 5'-alkylthio position
L181M
has a more extended side chain, may affect the binding of ligands at the 5'-alkylthio position
A15M
the mutant shows 14.5% catalytic efficiency compared to the wild type enzyme
D168A
the mutation completely abolishes activity
D168N
the mutation completely abolishes activity
E145A
the mutation completely abolishes activity
E145Q
the mutation completely abolishes activity
E18A
the mutation completely abolishes activity
E18Q
the mutation completely abolishes activity
M144A
the mutant shows 0.4% catalytic efficiency compared to the wild type enzyme
R164A
the mutant shows 15% catalytic efficiency compared to the wild type enzyme
R85A
the mutant shows 6.3% catalytic efficiency compared to the wild type enzyme
R85H
the mutant shows 7.1% catalytic efficiency compared to the wild type enzyme
S167A
the mutant shows 3.3% catalytic efficiency compared to the wild type enzyme
V34A
the mutant shows 12.5% catalytic efficiency compared to the wild type enzyme
V34I
the mutant shows 13.9% catalytic efficiency compared to the wild type enzyme
W179A
the mutant shows 3.3% catalytic efficiency compared to the wild type enzyme
W179F
the mutant shows 2.0% catalytic efficiency compared to the wild type enzyme
Y134A
the mutant shows 8.1% catalytic efficiency compared to the wild type enzyme
Y134F
the mutant shows 0.6% catalytic efficiency compared to the wild type enzyme
C136S
-
mutant is insensitive to oxidative inhibition
C223S
-
mutant is insensitive to oxidative inhibition
medicine
the enzyme is a therapeutic target for prostate cancer
V56I
-
natural polymorphism present in 7 of 9 melanoma cell lines, not in SK-Mel-28 and in HTZ19d
C136S
mutant is insensitive to oxidative inhibition
C223S
mutant is insensitive to oxidative inhibition
C259S/C261S
C259S/C261S/C262S
mutation significantly reduces the optimal temperature for the catalytic activity. Strong destabilization for the folded structure of the enzyme, as inferred from the temperature for half inactivation, which decreases from 112°C (wild-type) to 91°C. Specific activity is similar to the activity of the wild-type enzyme
C259S/C261S/C262S/C200S/C205S
mutation significantly reduces the optimal temperature for the catalytic activity. Strong destabilization for the folded structure of the enzyme, as inferred from the temperature for half inactivation, which decreases from 112°C (wild-type) to 73°C. Specific activity is similar to the activity of the wild-type enzyme
C259S/C261S/C262S/C200S/C205S/C138S
mutation significantly reduces the optimal temperature for the catalytic activity. Strong destabilization for the folded structure of the enzyme, as inferred from the temperature for half inactivation, which decreases from 112°C (wild-type) to 78°C. Specific activity is similar to the activity of the wild-type enzyme
C259S/C261S/C262S/C200S/C205S/C138S/C164S
mutation significantly reduces the optimal temperature for the catalytic activity. Strong destabilization for the folded structure of the enzyme, as inferred from the temperature for half inactivation, which decreases from 112°C (wild-type) to 73°C. Specific activity is similar to the activity of the wild-type enzyme
C262S
C259S/C261S
-
mutation significantly reduces the optimal temperature for the catalytic activity. Strong destabilization for the folded structure of the enzyme, as inferred from the temperature for half inactivation, which decreases from 112°C (wild-type) to 102°C. Specific activity is similar to the activity of the wild-type enzyme
-
C259S/C261S/C262S
-
mutation significantly reduces the optimal temperature for the catalytic activity. Strong destabilization for the folded structure of the enzyme, as inferred from the temperature for half inactivation, which decreases from 112°C (wild-type) to 91°C. Specific activity is similar to the activity of the wild-type enzyme
-
C259S/C261S/C262S/C200S/C205S
-
mutation significantly reduces the optimal temperature for the catalytic activity. Strong destabilization for the folded structure of the enzyme, as inferred from the temperature for half inactivation, which decreases from 112°C (wild-type) to 73°C. Specific activity is similar to the activity of the wild-type enzyme
-
C259S/C261S/C262S/C200S/C205S/C138S
-
mutation significantly reduces the optimal temperature for the catalytic activity. Strong destabilization for the folded structure of the enzyme, as inferred from the temperature for half inactivation, which decreases from 112°C (wild-type) to 78°C. Specific activity is similar to the activity of the wild-type enzyme
-
C262S
-
mutation significantly reduces the optimal temperature for the catalytic activity. Strong destabilization for the folded structure of the enzyme, as inferred from the temperature for half inactivation, which decreases from 112°C (wild-type) to 106°C. Specific activity is similar to the activity of the wild-type enzyme
-
N87T
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
Q289L
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
S12T
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
S12T/N87T
the mutant shows increased catalytic efficiencies with 5'-deoxy-5'-methylthioadenosine and 2'-deoxyadenosine and decreased catalytic efficiency with adenosine compared to the wild type enzyme
S12T/N87T/Q289L
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
additional information