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tetramer
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4 * 8500-9000, R-plasmid-coded type II reductase
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x * 57000, recombinant detagged enzyme, SDS-PAGE
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x * 21000, calculated from amino acid sequence
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x * 22000, recombinant His6-tagged enzyme, SDS-PAGE, x * 22086, sequence calculation, His-tagged enzyme
?
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? * 23000-24000, SDS-PAGE
?
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? * 18500, SDS-PAGE, isozyme I and II
?
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x * 22000, SDS-PAGE
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?
Halalkalibacterium halodurans
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x + 18855, wild-type, x * 20157, His-tagged enzyme, mass spectrometry
?
Halalkalibacterium halodurans C-125
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x + 18855, wild-type, x * 20157, His-tagged enzyme, mass spectrometry
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?
x * 22000, SDS-PAGE of native enzyme. x * 42000, SDS-PAGE of enzyme modified by small ubiquitin-like modifier 1
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x * 58000, recombinant bifunctional enzyme DHFR-TS, SDS-PAGE
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x * 58000, recombinant bifunctional enzyme DHFR-TS, SDS-PAGE
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x * 58000, recombinant bifunctional enzyme DHFR-TS, SDS-PAGE
dimer
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dimer
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2 * 56700, bifunctional enzyme: thymidylate synthase-dihydrofolate reductase, SDS-PAGE
dimer
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2 * 58000, isoform IIa, SDS-PAGE
dimer
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2 * 56400, methotrexate-resistant, each subunit is a bifunctional thymidylate synthase-dihydrofolate reductase, SDS-PAGE
dimer
2 * 66000, SDS-PAGE
dimer
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2 * 66000, SDS-PAGE
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dimer
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2 * 50000, thymidylate synthase and dihydrofolate reductase cannot be dissociated from each other, SDS-PAGE
dimer
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2 * 19000, recombinant enzyme, SDS-PAGE, mass spectroscopy
dimer
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2 * 19000, SDS-PAGE
homodimer
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monomer
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-
monomer
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isozymes type III
monomer
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1 * 21300, SDS-PAGE
monomer
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1 * 21450, amino acid sequence
monomer
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1 * 25000, recombinant from Escherichia coli, SDS-PAGE
monomer
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1 * 17000-22000
monomer
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1 * 19600, isoenzyme II, amino acid sequence
monomer
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1 * 22500, SDS-PAGE
monomer
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1 * 18250, MB 1428, amino acid sequence
monomer
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preparation of a dimeric variant (Xet-3) of dihydrofolate reductase from Escherichia coli by introducing residues located at the Thermotoga maritima dihydrofolate reductase dimer interface
monomer
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1 * 22500, SDS-PAGE
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monomer
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1 * 21650, amino acid sequence
monomer
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1 * 18694, electrospray mass spectrometry and calculated, 1 * 20000, SDS-PAGE
monomer
Halalkalibacterium halodurans
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1 * 18855, mass spectrometry, dynamic light scattering
monomer
Halalkalibacterium halodurans C-125
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1 * 18855, mass spectrometry, dynamic light scattering
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monomer
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1 * 17643, MALDI-TOF
monomer
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1 * 14900, isozyme I, SDS-PAGE
monomer
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1 * 18300, amino acid sequence
monomer
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1 * 20000, SDS-PAGE
monomer
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1 * 21460, methotrexate resistant L1210 (R) cells, amino acid sequence
monomer
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1 * 17643, MALDI-TOF
monomer
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1 * 17643, MALDI-TOF
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monomer
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1 * 173000, both forms, SDS-PAGE
monomer
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1 * 24000, recombinant enzyme, SDS-PAGE
monomer
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1 * 21500, SDS-PAGE
monomer
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1 * 39000, SDS-PAGE
monomer
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1 * 16900, R-plasmid enzyme, PAGE under denaturating and nondenaturating conditions
monomer
1 * 22000, recombinant enzyme, SDS-PAGE, 1 * 21089, sequence calculation
monomer
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1 * 22500, SDS-PAGE
monomer
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1 * 21450, amino acid sequence
monomer
Tequatrovirus T4
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-
monomer
Tequatrovirus T4
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1 * 29000, SDS-PAGE
monomer
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1 * 19000, SDS-PAGE
additional information
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overview
additional information
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overview
additional information
-
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additional information
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bifunctional, homodimers with DHFR and TS domains for each monomer
additional information
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overview
additional information
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enzyme complex with dihydrofolate reductase activity, thymidylate synthase activity and three other polypeptides of unknown function, 286000 MW complex, 45000 MW dihydrofolate reductase subunit and 4 other polypeptide chains: 95000, 70000, 50000, 26000
additional information
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overview
additional information
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polymer, SDS-PAGE
additional information
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dihydrofolate reductase is a substrate of ubiquitin ligase MDM2. MDM2 binds directly to dihydrofolate reductase and catalyzes its monoubiquitination. It reduces dihydrofolate reductase activity in a p53-independent manner, but has no effect on the steady-state level of expression. The ability of MDM2 to inhibit dihydrofolate reductase deoends on an active MDM2 RING-finger domain
additional information
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bifunctional, homodimers with DHFR and TS domains for each monomer
additional information
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a major band at 35000 Da and minor bands at 35000 Da and 42000 Da detected on SDS-PAGE
additional information
protozoa
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overview
additional information
protozoa
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overview
additional information
the DHFR enzyme structure exhibits the canonical DHFR fold
additional information
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the DHFR enzyme structure exhibits the canonical DHFR fold
additional information
Tequatrovirus T4
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overview
additional information
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overview
additional information
three-dimensional structures of Toxoplasma gondii enzyme TS-DHFR at 3.7 A and of a loop truncated TS-DHFR enzyme, removing several flexible surface loops in the DHFR domain, improving resolution to 2.2 A. The TS-DHFR homodimer includes a junctional region containing a linked crossover helix between the DHFR domains of the two adjacent monomers, a long linker connecting the TS and DHFR domains, and a DHFR domain that is positively charged, importance of this region not only in DHFR catalysis but also in modulating the distal TS activity suggests a role for TS-DHFR interdomain interactions. The interactions between the TS and the DHFR domains within the same monomer are comprised of both electrostatic and hydrophobic interactions that are predominately hydrophobic, these include hydrophobic contacts between F231, F319, and M297 as well as P242, I573, and V596
additional information
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three-dimensional structures of Toxoplasma gondii enzyme TS-DHFR at 3.7 A and of a loop truncated TS-DHFR enzyme, removing several flexible surface loops in the DHFR domain, improving resolution to 2.2 A. The TS-DHFR homodimer includes a junctional region containing a linked crossover helix between the DHFR domains of the two adjacent monomers, a long linker connecting the TS and DHFR domains, and a DHFR domain that is positively charged, importance of this region not only in DHFR catalysis but also in modulating the distal TS activity suggests a role for TS-DHFR interdomain interactions. The interactions between the TS and the DHFR domains within the same monomer are comprised of both electrostatic and hydrophobic interactions that are predominately hydrophobic, these include hydrophobic contacts between F231, F319, and M297 as well as P242, I573, and V596
additional information
the bifunctional folate and pyrimidine-metabolising enzyme dihydrofolate reductase-thymidylate synthase dihydrofolate reductase-thymidylate synthase is expressed from a single gene as a homodimer comprising of an N-terminal DHFR domain fused via a linker peptide to a TS domain at the C-terminus
additional information
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the bifunctional folate and pyrimidine-metabolising enzyme dihydrofolate reductase-thymidylate synthase dihydrofolate reductase-thymidylate synthase is expressed from a single gene as a homodimer comprising of an N-terminal DHFR domain fused via a linker peptide to a TS domain at the C-terminus
additional information
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the bifunctional folate and pyrimidine-metabolising enzyme dihydrofolate reductase-thymidylate synthase dihydrofolate reductase-thymidylate synthase is expressed from a single gene as a homodimer comprising of an N-terminal DHFR domain fused via a linker peptide to a TS domain at the C-terminus
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