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Literature summary for 1.5.1.3 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
Search for more literature for 1.5.1.3

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
7,8-dihydrofolate + NADPH + H+ Homo sapiens
-
 5,6,7,8-tetrahydrofolate + NADP+
-
 r

Organism

Organism UniProt Comment Textmining
Homo sapiens P00374
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7,8-dihydrofolate + NADPH + H+
-
 Homo sapiens 5,6,7,8-tetrahydrofolate + NADP+
-
 r

Subunits

Subunits Comment Organism
monomer
-
 Homo sapiens

Synonyms

Synonyms Comment Organism
DHFR
-
 Homo sapiens

Cofactor

Cofactor Comment Organism Structure
NADP+
-
 Homo sapiens
NADPH
-
 Homo sapiens

General Information

General Information Comment Organism
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
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