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Literature summary extracted from

  • McIntosh, E.N.; Purko, M.; Wood, W.A.
    Ketopantoate formation by a hydroxymethylation enzyme from Escherichia coli (1957), J. Biol. Chem., 228, 499-510.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.1.2.12 glycerol phosphate
-
Escherichia coli
4.1.2.12 glycylglycine
-
Escherichia coli
4.1.2.12 potassium phosphate
-
Escherichia coli
4.1.2.12 Tris(hydroxymethyl)aminomethane
-
Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.1.2.12 Co2+ activates Escherichia coli
4.1.2.12 Fe2+ slight activation Escherichia coli
4.1.2.12 Mg2+ slight activation Escherichia coli
4.1.2.12 Mn2+ activates Escherichia coli
4.1.2.12 Ni2+ activates Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
4.1.2.12 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.2.12
-
Escherichia coli

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.1.2.12 additional information
-
-
Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.2.12 2-Oxo-3-methylbutanoate + formaldehyde reverse reaction not detected Escherichia coli 2-Dehydropantoate
-
?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.1.2.12 7.8 8.9
-
Escherichia coli

pH Range

EC Number pH Minimum pH Maximum Comment Organism
4.1.2.12 6.5 8.5 low activity below pH 6.5 and above pH 8.5 Escherichia coli