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

BRENDA support

Literature summary extracted from

  • Fruscione, F.; Sturla, L.; Duncan, G.; Van Etten, J.L.; Valbuzzi, P.; De Flora, A.; Di Zanni, E.; Tonetti, M.
    Differential role of NADP+ and NADPH in the activity and structure of GDP-D-mannose 4,6-dehydratase from two Chlorella viruses (2008), J. Biol. Chem., 283, 184-193.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.2.1.47 expressed in Escherichia coli as glutathione S-transferase fusion protein Paramecium bursaria Chlorella virus-1
4.2.1.47 expressed in Escherichia coli as glutathione S-transferase fusion protein Acanthocystis turfacea chlorella virus 1
4.2.1.47 expression in Escherichia coli Paramecium bursaria Chlorella virus-1
4.2.1.47 expression in Escherichia coli Acanthocystis turfacea chlorella virus 1

General Stability

EC Number General Stability Organism
4.2.1.47 NADPH is essential for stabilization and function of the enzyme Paramecium bursaria Chlorella virus-1
4.2.1.47 NADPH is essential for stabilization and function of the enzyme Acanthocystis turfacea chlorella virus 1

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.2.1.47 NADP+ conversion of NADPH to NADP+ results in complete inactivation of the enzyme Acanthocystis turfacea chlorella virus 1
4.2.1.47 NADP+ conversion of NADPH to NADP+ results in complete inactivation of the enzyme Paramecium bursaria Chlorella virus-1

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.2.1.47 87000
-
 gel filtration Paramecium bursaria Chlorella virus-1

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.47 Acanthocystis turfacea chlorella virus 1
-
-
-
4.2.1.47 Paramecium bursaria Chlorella virus-1
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.2.1.47
-
 Paramecium bursaria Chlorella virus-1
4.2.1.47
-
 Acanthocystis turfacea chlorella virus 1
4.2.1.47 GSH-Sepharose 4B column chromatography Paramecium bursaria Chlorella virus-1
4.2.1.47 GSH-Sepharose 4B column chromatography Acanthocystis turfacea chlorella virus 1

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.2.1.47 0.48
-
-
 Paramecium bursaria Chlorella virus-1
4.2.1.47 0.63
-
-
 Acanthocystis turfacea chlorella virus 1

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.47 GDP-D-mannose
-
 Paramecium bursaria Chlorella virus-1 GDP-4-dehydro-6-deoxy-D-mannose + H2O
-
 ?
4.2.1.47 GDP-D-mannose
-
 Acanthocystis turfacea chlorella virus 1 GDP-4-dehydro-6-deoxy-D-mannose + H2O
-
 ?
4.2.1.47 GDP-mannose ATCV-1GMD has no reductase activity Paramecium bursaria Chlorella virus-1 GDP-4-dehydro-6-deoxy-D-mannose + H2O
-
 ?
4.2.1.47 GDP-mannose ATCV-1GMD has no reductase activity Acanthocystis turfacea chlorella virus 1 GDP-4-dehydro-6-deoxy-D-mannose + H2O
-
 ?

Subunits

EC Number Subunits Comment Organism
4.2.1.47 More NADPH is essential for maintaining the oligomerization status Paramecium bursaria Chlorella virus-1
4.2.1.47 More NADPH is essential for maintaining the oligomerization status Acanthocystis turfacea chlorella virus 1

Synonyms

EC Number Synonyms Comment Organism
4.2.1.47 ATCV-1GMD
-
 Acanthocystis turfacea chlorella virus 1
4.2.1.47 GDP-D-mannose 4,6-dehydratase
-
 Paramecium bursaria Chlorella virus-1
4.2.1.47 GDP-D-mannose 4,6-dehydratase
-
 Acanthocystis turfacea chlorella virus 1
4.2.1.47 GMD
-
 Paramecium bursaria Chlorella virus-1
4.2.1.47 GMD
-
 Acanthocystis turfacea chlorella virus 1
4.2.1.47 PBCV-1 GMD
-
 Paramecium bursaria Chlorella virus-1

Cofactor

EC Number Cofactor Comment Organism Structure
4.2.1.47 additional information the enzyme has a very low affinity for NADP+ Paramecium bursaria Chlorella virus-1
4.2.1.47 additional information the enzyme has a very low affinity for NADP+ Acanthocystis turfacea chlorella virus 1
4.2.1.47 NADPH dependent on Paramecium bursaria Chlorella virus-1
4.2.1.47 NADPH dependent on Acanthocystis turfacea chlorella virus 1
4.2.1.47 NADPH the enzymatically active proteins contain tightly bound NADPH that essential for maintaining the oligomerization status as well as for the stabilization and function of the enzyme Paramecium bursaria Chlorella virus-1
4.2.1.47 NADPH the enzymatically active proteins contain tightly bound NADPH that is essential for maintaining the oligomerization status as well as for the stabilization and function of the enzyme Acanthocystis turfacea chlorella virus 1