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Literature summary extracted from

  • Drew, D.P.; Lunde, C.; Lahnstein, J.; Fincher, G.B.
    Heterologous expression of cDNAs encoding monodehydroascorbate reductases from the moss, Physcomitrella patens and characterization of the expressed enzymes (2007), Planta, 225, 945-954.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.6.5.4 NADH NADH is the preferred electron donor Physcomitrium patens
1.6.5.4 NADPH NADH is the preferred electron donor Physcomitrium patens

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.6.5.4 expression in Escherichia coli Physcomitrium patens

Protein Variants

EC Number Protein Variants Comment Organism
1.6.5.4 C69A mutation has a negligible effect on enzyme activity under standard reaction conditions. The C69A mutant is more resistant to the inhibitory effects of beta-chloromercuribenzoate than the wild type PpMDHAR2 protein Physcomitrium patens

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.6.5.4 beta-chloromercuribenzoate PpMDHAR1 is almost completely inactivated after a 20 min preincubation with 0.25 mM beta-chloromercuribenzoate. At 0.05 mM the enzyme retains 11% of the initial activity. Physcomitrium patens
1.6.5.4 chloromercuribenzoate at 0.05 mM PpMDHAR3 retains 80% of the initial activity; PpMDHAR2 is almost completely inactivated after a 20 min preincubation with 0.25 mM chloromercuribenzoate. At 0.05 mM the enzyme retains 14% of the initial activity. The C69A mutant is more resistant to the inhibitory effects of chloromercuribenzoate than the wild type PpMDHAR2 protein Physcomitrium patens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.6.5.4 0.0078
-
NADH
-
Physcomitrium patens
1.6.5.4 0.0096
-
NADH
-
Physcomitrium patens
1.6.5.4 0.0178
-
NADH
-
Physcomitrium patens
1.6.5.4 0.088
-
NADPH
-
Physcomitrium patens
1.6.5.4 0.223
-
NADPH
-
Physcomitrium patens
1.6.5.4 0.99
-
NADPH
-
Physcomitrium patens

Organism

EC Number Organism UniProt Comment Textmining
1.6.5.4 Physcomitrium patens Q2I826
-
-
1.6.5.4 Physcomitrium patens Q2I827
-
-
1.6.5.4 Physcomitrium patens Q2I828
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.6.5.4 NADH + H+ + 2 monodehydroascorbate = NAD+ + 2 ascorbate PpMDHARs follow a ping-pong kinetic mechanism Physcomitrium patens

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.6.5.4 152
-
-
Physcomitrium patens
1.6.5.4 164
-
-
Physcomitrium patens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.6.5.4 NADH + monodehydroascorbate
-
Physcomitrium patens NAD+ + ascorbate
-
?
1.6.5.4 NADPH + monodehydroascorbate NADH is the preferred electron donor Physcomitrium patens NADP+ + ascorbate
-
?

Synonyms

EC Number Synonyms Comment Organism
1.6.5.4 MDHAR1
-
Physcomitrium patens
1.6.5.4 MDHAR2
-
Physcomitrium patens
1.6.5.4 MDHAR3
-
Physcomitrium patens
1.6.5.4 monodehydroascorbate reductase
-
Physcomitrium patens
1.6.5.4 PpMDHAR1
-
Physcomitrium patens
1.6.5.4 PpMDHAR2
-
Physcomitrium patens
1.6.5.4 PpMDHAR3
-
Physcomitrium patens

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.6.5.4 119
-
NADH
-
Physcomitrium patens
1.6.5.4 128
-
NADH
-
Physcomitrium patens
1.6.5.4 170
-
NADH
-
Physcomitrium patens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.6.5.4 8.1
-
-
Physcomitrium patens

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.6.5.4 7.6 8.7 85% or greater activity between pH 7.6 and pH 8.7 Physcomitrium patens

Cofactor

EC Number Cofactor Comment Organism Structure
1.6.5.4 FAD contains a single non-covalently bound FAD coenzyme molecule Physcomitrium patens
1.6.5.4 NADH NADH is the preferred electron donor Physcomitrium patens
1.6.5.4 NADPH NADH is the preferred electron donor Physcomitrium patens