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

BRENDA support

Literature summary for 4.1.1.29 extracted from

  • Liu, P.; Torrens-Spence, M.P.; Ding, H.; Christensen, B.M.; Li, J.
    Mechanism of cysteine-dependent inactivation of aspartate/glutamate/cysteine sulfinic acid alpha-decarboxylases (2013), Amino Acids, 44, 391-404.
    View publication on PubMed
Search for more literature for 4.1.1.29

Inhibitors

Inhibitors Comment Organism Structure
cysteine cysteine is able to enter the active site of the enzyme, interact with the pyridoxal 5'-phosphate-lysine internal aldimine, form a cysteine-pyridoxal 5'-phosphate aldimine and undergo intramolecular nucleophilic cyclization through its sulfhydryl group, leading to irreversible inactivation. Reaction is similar for aspartate decarboxylase, glutamate decarboxylase and cysteine sulfinic acid decarboxylase Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.61
-
 presence of 5 mM cysteine, pH 7.0, temperature not specified in the publication Homo sapiens
4.89
-
 pH 7.0, temperature not specified in the publication Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-Cysteine sulfinate
-
 Homo sapiens 2-Aminoethane sulfinate + CO2
-
 ?