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Literature summary extracted from

  • Ohmura, E.; Hayaishi, O.
    Enzymatic conversion of formylaspartic acid to aspartic acid (1957), J. Biol. Chem., 227, 181-190.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.1.8 1.25
-
 N-formyl-L-aspartate formylase I Pseudomonas sp.
3.5.1.8 1.32
-
 N-formyl-L-aspartate formylase I Pseudomonas sp.

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.5.1.8 Co2+
-
 Pseudomonas sp.
3.5.1.8 Fe2+
-
 Pseudomonas sp.
3.5.1.8 Mn2+ only formylase II Pseudomonas sp.

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.8 Pseudomonas sp.
-
 strain ATCC 11299B, formylase I + II
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.1.8
-
 Pseudomonas sp.

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.5.1.8 5940
-
 formylase I Pseudomonas sp.
3.5.1.8 21000
-
 formylase II Pseudomonas sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.8 acetyl-L-glutamic acid + H2O only formylase II Pseudomonas sp. acetate + L-glutamate
-
 ?
3.5.1.8 chloroacetyl L-aspartic acid + H2O addition of Co2+ required Pseudomonas sp. chloroacetate + L-aspartate
-
 ?
3.5.1.8 formylglutamic acid + H2O only formylase II Pseudomonas sp. formate + glutamate
-
 ?
3.5.1.8 N-formyl-L-aspartate + H2O
-
 Pseudomonas sp. formate + L-aspartate
-
 ?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.1.8 7
-
 formylase I Pseudomonas sp.
3.5.1.8 8
-
 formylase II Pseudomonas sp.