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Sequence of DYR21_ECOLX

EC Number:1.5.1.3

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
dihydrofolate reductase
P00383
Escherichia coli
78
8446
Reaction
5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH + H+
Other sequences found for EC No. 1.5.1.3

General information:

Sequence
show sequence in fasta format
 0 MERSSNEVSN PVAGNFVFPS NATFGMGDRV RKKSGAAWQG QIVGWYCTNL TPEGYAVESE
60 AHPGSVQIYP VAALERIN
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
412176
Brisson N.,Hohn T.
Nucleotide sequence of the dihydrofolate-reductase gene borne by the plasmid R67 and conferring methotrexate resistance.
Gene
28
271-275
1984
412177
Stone D.,Smith S.L.
The amino acid sequence of the trimethoprim-resistant dihydrofolate reductase specified in Escherichia coli by R-plasmid R67.
J. Biol. Chem.
254
10857-10861
1979
412178
Strader M.B.,Smiley R.D.,Stinnett L.G.,VerBerkmoes N.C.,Howell E.E.
Role of S65, Q67, I68, and Y69 residues in homotetrameric R67 dihydrofolate reductase.
Biochemistry
40
11344-11352
2001
412179
Narayana N.,Matthews D.A.,Howell E.E.,Nguyen-Huu X.
A plasmid-encoded dihydrofolate reductase from trimethoprim-resistant bacteria has a novel D2-symmetric active site.
Nat. Struct. Biol.
2
1018-1025
1995
412180
Narayana N.
High-resolution structure of a plasmid-encoded dihydrofolate reductase: pentagonal network of water molecules in the D2-symmetric active site.
Acta Crystallogr. D
62
695-706
2006
412181
Krahn J.M.,Jackson M.R.,DeRose E.F.,Howell E.E.,London R.E.
Crystal structure of a type II dihydrofolate reductase catalytic ternary complex.
Biochemistry
46
14878-14888
2007
412182
Divya N.,Grifith E.,Narayana N.
Structure of the Q67H mutant of R67 dihydrofolate reductase-NADP+ complex reveals a novel cofactor binding mode.
Protein Sci.
16
1063-1068
2007