Enzyme

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EC Tree
     1. Oxidoreductases
        1.5 Acting on the CH-NH group of donors
            1.5.1 With NAD+ or NADP+ as acceptor
ID:1.5.1.3
Description:Dihydrofolate reductase.
Alternative Name: Tetrahydrofolate dehydrogenase.
Prosite: PDOC00072;
PDB:
PDBScop
4QJZ 8029173; 8041552;
4IXG 8029173; 8041552;
4IXF 8029173; 8041552;
4IXE 8029173; 8041552;
4G8Z 8029173; 8041552;
 » show all

Cath: 1.10.1040.10; 3.30.572.10; 3.40.109.10; 3.40.50.720; 2.30.30.60; 3.40.430.10;

3D structure

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PDB
4QJZ; 4IXG; 4IXF; 4IXE; 4G8Z; 4CD2; 3TD8; 3NZC; 3NZB; 3NZA; 3NZ9; 3NZ6; 3CD2; 2FZI; 2CD2; 1VJ3; 1S3Y; 1LY4; 1LY3; 1KLK; 1E26; 1DYR; 1DAJ; 1CD2; 6DE4; 6DAV; 4KFJ; 4KEB; 4KD7; 4KBN; 4KAK; 2W3M; 2W3B; 2W3A; 2C2T; 2C2S; 1DHF; 6A7E; 6A7C; 5HVE; 5HVB; 5HUI; 5HT5; 5HT4; 5HSU; 5HSR; 5HQZ; 5HQY; 5HPB; 4QJC; 4QHV; 4M6L; 4M6K; 4M6J; 4G95; 4DDR; 3S7A; 3S3V; 3OAF; 3NZD; 3NXY; 3NXX; 3NXV; 3NXT; 3NXR; 3NXO; 3NU0; 3NTZ; 3N0H; 3L3R; 3GYF; 3GI2; 3GHW; 3GHV; 3GHC; 3FS6; 3F91; 3F8Z; 3F8Y; 3EIG; 1YHO; 1U72; 1U71; 1S3W; 1S3V; 1S3U; 1PDB; 1PD9; 1PD8; 1OHK; 1OHJ; 1MVT; 1MVS; 1KMV; 1KMS; 1HFR; 1HFQ; 1HFP; 1DRF; 1DLS; 1DLR; 1BOZ; 1JUV; 4HOF; 4HOE; 4H97; 4H96; 4H95; 3QLW; 3QLS; 3QLR; 1M7A; 1M79; 1M78; 1IA4; 1IA3; 1IA2; 1IA1; 1AOE; 1AI9; 8DFR; 1DR7; 1DR6; 1DR5; 1DR4; 1DR3; 1DR2; 1DR1; 1VDR; 2JYB; 2ITH; 1D1G; 1CZ3; 6DDS; 6DDP; 5JA3; 4M2X; 4KNE; 4KM2; 4KM0; 4KLX; 6DDW; 5UJF; 5U27; 5U26; 4KL9; 2CIG; 1DG7; 1DG5; 1DF7; 3DFR; 2LF1; 2L28; 2HQP; 2HM9; 1LUD; 1DIU; 1DIS; 1BZF; 1AO8; 5UIO; 5UJX; 5UIP; 5EAJ; 5E8Q; 4X5G; 4X5F; 4GH8; 4EJ1; 4EIZ; 4DFR; 3OCH; 3DRC; 2INQ; 2DRC; 2D0K; 1TDR; 1RE7; 1RD7; 1RB3; 1RB2; 1JOL; 1DYJ; 1DYI; 1DYH; 1DRB; 1DRA; 1DHJ; 1DHI; 1DDS; 1DDR; 7DFR; 6MTH; 6MT8; 6MR9; 6DFR; 6CQA; 5Z6M; 5Z6L; 5Z6K; 5Z6J; 5Z6F; 5W3Q; 5UII; 5UIH; 5DFR; 5CCC; 5CC9; 4X5J; 4X5I; 4X5H; 4PDJ; 4NX7; 4NX6; 4KJL; 4KJK; 4KJJ; 4I1N; 4I13; 4FHB; 4EIG; 3R33; 3QYO; 3QYL; 3QL3; 3KFY; 3K74; 3DAU; 2ANQ; 2ANO; 1RX9; 1RX8; 1RX7; 1RX6; 1RX5; 1RX4; 1RX3; 1RX2; 1RX1; 1RH3; 1RG7; 1RF7; 1RC4; 1RA9; 1RA8; 1RA3; 1RA2; 1RA1; 1JOM; 1DRH; 1DRE; 3DGA; 1J3K; 1J3J; 3DG8; 1J3I; 6N1T; 6N1S; 6E4E; 6AOI; 6AOH; 6AOG; 5T0L; 5JG0; 5IST; 5ISQ; 5ISP; 5HF2; 5HF0; 4XEC; 4XE6; 4LEK; 4LAH; 4LAG; 4LAE; 4KYA; 4KY4; 4FGH; 4FGG; 4EIL; 4ECK; 3SRW; 3SRU; 3SRS; 3SRR; 3SRQ; 3SR5; 3SQY; 3SH2; 3SGY; 3RG9; 3QFX; 3M09; 3M08; 3LG4; 3K47; 3K45; 3IX9; 3IRO; 3IRN; 3IRM; 3INV; 3I8A; 3HBB; 3FYW; 3FYV; 3FY9; 3FY8; 3FRF; 3FRE; 3FRD; 3FRB; 3FRA; 3D84; 3D80; 3CLB; 3CL9; 2W9T; 2W9S; 2W9H; 2W9G; 2H2Q; 2FZJ; 2FZH; 2DHF; 2BLC; 2BLB; 2BLA; 2BL9; 1U70; 1DG8;

References

External Links

UniProtKB Enzyme Link: UniProtKB 1.5.1.3
BRENDA Enzyme Link: BRENDA 1.5.1.3
KEGG Enzyme Link: KEGG1.5.1.3
BioCyc Enzyme Link: BioCyc 1.5.1.3
ExPASy Enzyme Link: ExPASy1.5.1.3
EC2PDB Enzyme Link: EC2PDB 1.5.1.3
ExplorEnz Enzyme Link: ExplorEnz 1.5.1.3
PRIAM enzyme-specific profiles Link: PRIAM 1.5.1.3
IntEnz Enzyme Link: IntEnz 1.5.1.3
MEDLINE Enzyme Link: MEDLINE 1.5.1.3
MSA:

1.5.1.3;

Phylogenetic Tree:

1.5.1.3;

Uniprot:
M-CSA:
RHEA:15009 (6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH
RULE(radius=1) [*:1]-[CH;+0:2](-[*:3])-[NH;+0:4]-[*:5].[*:6]-[n+;H0:7]1:[cH;+0:8]:[cH;+0:9]:[cH;+0:10]:[c;H0;+0:11](-[*:12]):[cH;+0:13]:1>>[*:1]-[C;H0;+0:2](-[*:3])=[N;H0;+0:4]-[*:5].[*:6]-[N;H0;+0:7]1-[CH;+0:8]=[CH;+0:9]-[CH2;+0:10]-[C;H0;+0:11](-[*:12])=[CH;+0:13]-1
Reaction
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References

TitleAuthorsDatePubMed ID
Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 A resolution. I. General features and binding of methotrexate.Bolin JT, Filman DJ, Matthews DA, Hamlin RC, Kraut J1982 Nov 256815178
Studies on dihydrofolic reductase. I. Purification and properties of dihydrofolic reductase from chicken liver.Kaufman BT, Gardiner RC1966 Mar 254379915
Regulation of the enzymes involved in the biosynthesis of 2,3-dihydroxybenzoic acid in Aerobacter aerogenes and Escherichia coli.Young IG, Gibson F1969 May 64306838