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

BRENDA support

Literature summary for 4.1.2.12 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

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

Metals/Ions

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.8 8.9
-
Escherichia coli

pH Range

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