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Literature summary extracted from

  • Wang, N.; McCammon, J.A.
    Substrate channeling between the human dihydrofolate reductase and thymidylate synthase (2016), Protein Sci., 25, 79-86 .
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.5.1.3 7,8-dihydrofolate + NADPH + H+ Homo sapiens
-
 5,6,7,8-tetrahydrofolate + NADP+
-
 r
2.1.1.45 5,10-methylenetetrahydrofolate + dUMP Homo sapiens
-
 dihydrofolate + dTMP
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.5.1.3 Homo sapiens P00374
-
-
2.1.1.45 Homo sapiens P04818
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.1.3 7,8-dihydrofolate + NADPH + H+
-
 Homo sapiens 5,6,7,8-tetrahydrofolate + NADP+
-
 r
2.1.1.45 5,10-methylenetetrahydrofolate + dUMP
-
 Homo sapiens dihydrofolate + dTMP
-
 ?

Subunits

EC Number Subunits Comment Organism
1.5.1.3 monomer
-
 Homo sapiens
2.1.1.45 dimer
-
 Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
1.5.1.3 DHFR
-
 Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.5.1.3 NADP+
-
 Homo sapiens
1.5.1.3 NADPH
-
 Homo sapiens

General Information

EC Number General Information Comment Organism
1.5.1.3 additional information in vitro, one human thymidylate synthase dimer binds to up to six human dihydrofolate reductase monomers, protein-protein docking process, overview. Existence of bound-state conformations of the human DHFR and TS proteins where a continuous positive surface potential region, connecting the TS and DHFR active sites, is formed Homo sapiens
1.5.1.3 physiological function the human thymidylate synthase and dihydrofolate reductase catalyse two consecutive reactions in the folate metabolism pathway and are very likely to bind in the same multi-enzyme complex in vivo, substrate channeling occurs between the human thymidylate synthase and dihydrofolate reductase, analysis by protein-protein docking, electrostatics calculations, and Brownian dynamics, overview. The non-covalently non-covalently bound human thymidylate synthase and dihydrofolate reductase are capable of substrate channeling and the formation of the surface electrostatic highway. The substrate channeling efficiency between the two can be reasonably high and comparable to that of the bifunctional protozoan enzyme Homo sapiens
2.1.1.45 additional information in vitro, one human thymidylate synthase dimer binds to up to six human dihydrofolate reductase monomers, protein-protein docking process, overview. Existence of bound-state conformations of the human DHFR and TS proteins where a continuous positive surface potential region, connecting the TS and DHFR active sites, is formed Homo sapiens
2.1.1.45 physiological function the human thymidylate synthase and dihydrofolate reductase catalyse two consecutive reactions in the folate metabolism pathway and are very likely to bind in the same multi-enzyme complex in vivo, substrate channeling occurs between the human thymidylate synthase and dihydrofolate reductase, analysis by protein-protein docking, electrostatics calculations, and Brownian dynamics, overview. The non-covalently bound human thymidylate synthase and dihydrofolate reductase are capable of substrate channeling and the formation of the surface electrostatic highway. The substrate channeling efficiency between the two can be reasonably high and comparable to that of the bifunctional protozoan enzyme Homo sapiens