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Literature summary for 4.1.1.29 extracted from

  • Liu, P.; Ding, H.; Christensen, B.M.; Li, J.
    Cysteine sulfinic acid decarboxylase activity of Aedes aegypti aspartate 1-decarboxylase: the structural basis of its substrate selectivity (2012), Insect Biochem. Mol. Biol., 42, 396-403.
    View publication on PubMed
Search for more literature for 4.1.1.29

Crystallization (Commentary)

Crystallization (Comment) Organism
homology modeling and substrate docking suggest that residue Q377, localized at the active site of aspartate decarboxylase, can better interact with aspartate through hydrogen bonding, which may play a role in aspartate selectivity. A leucine residue in mammalian CSADC occupies the same position Aedes aegypti

Protein Variants

Protein Variants Comment Organism
Q377L mutation diminishes the decarboxylation activity to aspartate with no major effect on its activity to cysteine sulfinic acid. Mutation leads to increase in the zwitterion form of the internal aldimine tautomer Aedes aegypti

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14
-
 L-cysteine sulfinate mutant Q37L, 25°C, pH not specified in the publication Aedes aegypti
1.16
-
 L-cysteine sulfinate wild-type, 25°C, pH not specified in the publication Aedes aegypti

Organism

Organism UniProt Comment Textmining
Aedes aegypti
-
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
6.7
-
 wild-type, 25°C, pH not specified in the publication Aedes aegypti

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-Cysteine sulfinate besides its activity to aspartate, the mosquito enzyme catalyzes the decarboxylation of cysteine sulfinic acid and cysteic acid as efficiently as those of mammalian CSADC under the same testing conditions Aedes aegypti 2-Aminoethane sulfinate + CO2
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5.52
-
 L-cysteine sulfinate mutant Q377L, 25°C, pH not specified in the publication Aedes aegypti
5.86
-
 L-cysteine sulfinate wild-type, 25°C, pH not specified in the publication Aedes aegypti

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
4.84
-
 L-cysteine sulfinate mutant Q37L, 25°C, pH not specified in the publication Aedes aegypti
5.05
-
 L-cysteine sulfinate wild-type, 25°C, pH not specified in the publication Aedes aegypti