2.1.1.148: thymidylate synthase (FAD)
This is an abbreviated version!
For detailed information about thymidylate synthase (FAD), go to the full flat file.
Word Map on EC 2.1.1.148
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2.1.1.148
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medicine
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tuberculosis
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dtmp
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synthases
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thymidine
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dihydrofolate
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maritima
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bursaria
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2'-deoxyuridine
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paramecium
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folate-dependent
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chlorella
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5-substituted
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virus-1
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ch2h4folate
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2'-deoxythymidine-5'-monophosphate
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flavoenzyme
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drug development
- 2.1.1.148
- medicine
- tuberculosis
- dtmp
- synthases
- thymidine
- dihydrofolate
- maritima
- bursaria
- 2'-deoxyuridine
-
paramecium
-
folate-dependent
- chlorella
-
5-substituted
-
virus-1
-
ch2h4folate
-
2'-deoxythymidine-5'-monophosphate
-
flavoenzyme
- drug development
Reaction
Synonyms
A674R, complementing thymidylate synthase, FDTS, flavin dependent thymidylate synthase, flavin-dependent thymidylate synthase, flavin-dependent thymidylate synthase X, flavin-dependent TS, Thy1, thymidylate synthase 1, thymidylate synthase complementing protein, thymidylate synthase ThyX, thymidylate synthase X, ThyX, thyX-encoded thymidylate synthase, TSCP, TTHA1096
ECTree
2.1.1.148 thymidylate synthase (FAD)Advanced search results
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results (Engineering
Engineering on EC 2.1.1.148 - thymidylate synthase (FAD)
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
R74A
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the KM-value for dUMP is 5.1fold higher than the wild-type value, the turnover-number is 4.6fold lower than the wild-type value
R74K
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the KM-value for dUMP is nearly identical to wild-type value, the turnover-number is 6.6fold lower than the wild-type value
S84A
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the KM-value for dUMP is 5.3fold higher than the wild-type value, the turnover-number is 2.1fold lower than the wild-type value. Mutation abolishes thymidylate synthase activity in vivo
S84Y
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the KM-value for dUMP is 1.9fold higher than the wild-type value, the turnover-number is 1.6fold lower than the wild-type value
Y87F
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the KM-value for dUMP is 1.8fold lower than the wild-type value, the turnover-number is nearly identical to the wild-type value
I65M
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no impaired enzyme activity, encodes proteins supporting the growth of Escherichia coli chi2913 strain
I65M/L175M
L175M
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no impaired enzyme activity, encodes proteins supporting the growth of Escherichia coli chi2913 strain
E190G
H177K
Paramecium bursaria Chlorella virus-1
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does not confer thymidine-independent growth to an Escherichia coli strain lacking thymidylate synthase ThyA, 9.5% oxidation activity
H177Q
Paramecium bursaria Chlorella virus-1
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confers thymidine-independent growth to an Escherichia coli strain lacking thymidylate synthase ThyA, 31% oxidation activity
H53K
Paramecium bursaria Chlorella virus-1
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does not confer thymidine-independent growth to an Escherichia coli strain lacking thymidylate synthase ThyA, produces insoluble protein
H53Q
Paramecium bursaria Chlorella virus-1
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does not confer thymidine-independent growth to an Escherichia coli strain lacking thymidylate synthase ThyA, produces insoluble protein
H79K
Paramecium bursaria Chlorella virus-1
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does not confer thymidine-independent growth to an Escherichia coli strain lacking thymidylate synthase ThyA
H79Q
Paramecium bursaria Chlorella virus-1
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confers thymidine-independent growth to an Escherichia coli strain lacking thymidylate synthase ThyA, 94% oxidation activity
R182A
Paramecium bursaria Chlorella virus-1
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does not confer thymidine-independent growth to an Escherichia coli strain lacking thymidylate synthase ThyA, does not copurify with oxidized FAD, but is able to oxidize NADPH in the presence of 0.4 mM FAD
R90A
Paramecium bursaria Chlorella virus-1
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does not confer thymidine-independent growth to an Escherichia coli strain lacking thymidylate synthase ThyA, looses 44% of its oxidation activity and shows no measurable deprotonation activity
H53D
residue H53 is involved in folate binding. Crystal structures of the H53D-FAD and H53D-FAD-dUMP complexes
S88A
mutant retains activity. Residue S88 is not required for catalysis
S88C
mutant retains activity. Residue S88 is not required for catalysis
Y91F
similar to wild-type, at saturating FAD conditions dUMP binding to the protein/FAD complex leads to additional stabilization by about 7 degrees
H53D
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residue H53 is involved in folate binding. Crystal structures of the H53D-FAD and H53D-FAD-dUMP complexes
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Y91F
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similar to wild-type, at saturating FAD conditions dUMP binding to the protein/FAD complex leads to additional stabilization by about 7 degrees
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additional information
E190G
Paramecium bursaria Chlorella virus-1
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does not confer thymidine-independent growth to an Escherichia coli strain lacking thymidylate synthase ThyA, is capable of binding FAD at a wild-type level, but lacks detectable oxidation and deprotonation
additional information
analysis of 67 site-directed mutants and identification of the extended motif Y44X(24)H69X(25)R95HRX(87)S105XRYX(90)R199 of amino acids essential to enzyme activity. Residue H69 is the catalytic residue, S105 the nucleophile
additional information
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analysis of 67 site-directed mutants and identification of the extended motif Y44X(24)H69X(25)R95HRX(87)S105XRYX(90)R199 of amino acids essential to enzyme activity. Residue H69 is the catalytic residue, S105 the nucleophile
additional information
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analysis of 67 site-directed mutants and identification of the extended motif Y44X(24)H69X(25)R95HRX(87)S105XRYX(90)R199 of amino acids essential to enzyme activity. Residue H69 is the catalytic residue, S105 the nucleophile
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