Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Loveridge, E.; Rodriguez, R.; Swanwick, R.; Allemann, R.
    Effect of dimerization on the stability and catalytic activity of dihydrofolate reductase from the hyperthermophile Thermotoga maritima (2009), Biochemistry, 48, 5922-5933 .
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.5.1.3 V11D the single amino acid replacement is sufficient to favor the monomeric form of the enzyme in the presence of the nondenaturing zwitterionic detergent 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate. The free energy of stabilization of monomeric mutant enzyme V11D is 15 kJ/mol lower than that of the wild-type dimer. Both the steady-state turnover numbers and rates of hydride transfer are reduced in V11D Thermotoga maritima
1.5.1.3 V126E mutant enzyme remains as a dimer, steady-state turnover numbers and rates of hydride transfer are reduced Thermotoga maritima

Organism

EC Number Organism UniProt Comment Textmining
1.5.1.3 Thermotoga maritima Q60034
-
-
1.5.1.3 Thermotoga maritima DSM 3109 Q60034
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.5.1.3
-
 Thermotoga maritima

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.1.3 7,8-dihydrofolate + NADPH + H+
-
 Thermotoga maritima 5,6,7,8-tetrahydrofolate + NADP+
-
 ?
1.5.1.3 7,8-dihydrofolate + NADPH + H+
-
 Thermotoga maritima DSM 3109 5,6,7,8-tetrahydrofolate + NADP+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.5.1.3 homodimer
-
 Thermotoga maritima

Synonyms

EC Number Synonyms Comment Organism
1.5.1.3 DHFR
-
 Thermotoga maritima

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.5.1.3 40
-
 assay at Thermotoga maritima

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.5.1.3 additional information
-
 the free energy of stabilization of monomeric mutant enzyme V11D is 15 kJ/mol lower than that of the wild-type dimer, while the melting temperature of monomeric mutant enzyme V11D is comparable to that of monomeric DHFR from the thermophile Bacillus stearothermophilus, supporting the hypothesis that oligomerization is required to achieve the thermal stabilities necessary for activity at temperatures optimal for growth of hyperthermophiles Thermotoga maritima

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.5.1.3 7
-
 assay at Thermotoga maritima

Cofactor

EC Number Cofactor Comment Organism Structure
1.5.1.3 NADPH
-
 Thermotoga maritima