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

BRENDA support

Literature summary for 3.5.1.8 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]

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

Metals/Ions

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

Organism

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

Purification (Commentary)

Purification (Comment) Organism
-
Pseudomonas sp.

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

pH Optimum

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