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Literature summary for 4.1.1.71 extracted from

  • Bjornstad, L.G.; Zoppellaro, G.; Tomter, A.B.; Falnes, P.O.; Andersson, K.K.
    Spectroscopic and magnetic studies of wild-type and mutant forms of the Fe(II)- and 2-oxoglutarate-dependent decarboxylase ALKBH4 (2011), Biochem. J., 434, 391-398.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21-CodonPlus(DE3)-RIPL cells Homo sapiens

Protein Variants

Protein Variants Comment Organism
C15A/C17A the mutant displays a decarboxylation activity similar to that of the wild type enzyme Homo sapiens
H169A/D171A the mutant is devoid of the ability to perform 2-oxoglutarate turnover Homo sapiens

General Stability

General Stability Organism
the isolated proteins (ALKBH4 and mutants), even when kept in iced-cooled solutions (4°C), aggregate and then precipitate at concentrations higher than 0.5 mM. The process is accelerated greatly when an excess (e.g. 5fold) of dithionite is added to the solution when anaerobic Fe(II)-reconstitution procedures are carried out Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ dependent on Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
glutathione-Sepharose column chromatography, gel filtration Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-oxoglutarate
-
Homo sapiens succinate semialdehyde + CO2
-
?

Synonyms

Synonyms Comment Organism
ALKBH4
-
Homo sapiens
Fe(II)/2OG-dependent decarboxylase
-
Homo sapiens