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Literature summary for 4.1.1.11 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 4.1.1.11

Protein Variants

Protein Variants Comment Organism
Q377L site-directed mutagenesis, mutation at position 377 from glutamine to leucine in aspartate 1-decarboxylase diminishes its decarboxylation activity to aspartate with no major effect on its cysteine sulfinic acid decarboxylase activity Aedes aegypti

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.04
-
 L-aspartate pH 7.0, 25°C, wild-type enzyme Aedes aegypti
3.18
-
 L-aspartate pH 7.0, 25°C, mutant Q377L Aedes aegypti

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-aspartate Drosophila melanogaster
-
 beta-alanine + CO2
-
 ?
L-aspartate Aedes aegypti
-
 beta-alanine + CO2
-
 ?

Organism

Organism UniProt Comment Textmining
Aedes aegypti
-
-
-
Drosophila melanogaster
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-aspartate
-
 Drosophila melanogaster beta-alanine + CO2
-
 ?
L-aspartate
-
 Aedes aegypti beta-alanine + CO2
-
 ?
additional information the enzyme also shows cysteine sulfinic acid decarboxylase activity, EC 4.1.1.29, catalyzing the decarboxylation of cysteine sulfinic acid and cysteic acid Drosophila melanogaster ?
-
 ?
additional information the enzyme also shows cysteine sulfinic acid decarboxylase activity, EC 4.1.1.29, catalyzing the decarboxylation of cysteine sulfinic acid and cysteic acid. Homology modeling of AeADC and substrate docking suggest that residue Q377, localized at the active site of AeADC, could better interact with aspartate through hydrogen bonding, which may play a role in aspartate selectivity Aedes aegypti ?
-
 ?

Synonyms

Synonyms Comment Organism
ADC
-
 Drosophila melanogaster
ADC
-
 Aedes aegypti
aspartate-alpha-decarboxylase
-
 Drosophila melanogaster
aspartate-alpha-decarboxylase
-
 Aedes aegypti

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Drosophila melanogaster
25
-
 assay at Aedes aegypti

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.11
-
 L-aspartate pH 7.0, 25°C, mutant Q377L Aedes aegypti
7.03
-
 L-aspartate pH 7.0, 25°C, wild-type enzyme Aedes aegypti

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 assay at Drosophila melanogaster
7
-
 assay at Aedes aegypti

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate tautomers of the internal aldimine between PLP and enzyme, overview Aedes aegypti

General Information

General Information Comment Organism
additional information homology modeling and substrate docking, evaluation of potential substrate interacting residues, overview Aedes aegypti

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.66
-
 L-aspartate pH 7.0, 25°C, mutant Q377L Aedes aegypti
3.44
-
 L-aspartate pH 7.0, 25°C, wild-type enzyme Aedes aegypti