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Information on EC 4.1.1.12 - aspartate 4-decarboxylase and Organism(s) Comamonas testosteroni and UniProt Accession Q93QX0

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.12 aspartate 4-decarboxylase
IUBMB Comments
A pyridoxal-phosphate protein. Also catalyses the decarboxylation of aminomalonate (formerly listed as EC 4.1.1.10), and the desulfination of 3-sulfino-L-alanine to sulfite and alanine.
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This record set is specific for:
Comamonas testosteroni
UNIPROT: Q93QX0
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Word Map
The taxonomic range for the selected organisms is: Comamonas testosteroni
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
desulfinase, aspartate beta-decarboxylase, l-aspartate beta-decarboxylase, l-aspartate 4-decarboxylase, aspartate 4-decarboxylase, aspartate-beta-decarboxylase, aspartate 4-carboxylyase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
L-Aspartate beta-decarboxylase
-
Aminomalonic decarboxylase
-
-
-
-
Aspartate beta-decarboxylase
-
-
-
-
Aspartate omega-decarboxylase
-
-
-
-
Aspartic beta-decarboxylase
-
-
-
-
Aspartic omega-decarboxylase
-
-
-
-
Cysteine sulfinic desulfinase
-
-
-
-
Decarboxylase, aspartate 4-
-
-
-
-
Desulfinase
-
-
-
-
L-Asparate 4-carboxy-lyase
-
-
-
-
L-Aspartate beta-decarboxylase
-
-
-
-
L-Cysteine sulfinate acid desulfinase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
-
-
-
-
desulfination
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
L-aspartate 4-carboxy-lyase (L-alanine-forming)
A pyridoxal-phosphate protein. Also catalyses the decarboxylation of aminomalonate (formerly listed as EC 4.1.1.10), and the desulfination of 3-sulfino-L-alanine to sulfite and alanine.
CAS REGISTRY NUMBER
COMMENTARY hide
9024-57-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-Asp
L-Ala + CO2
show the reaction diagram
-
-
-
?
L-aspartate
L-alanine + CO2
show the reaction diagram
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-aspartate
L-alanine + CO2
show the reaction diagram
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
dependent on, pyridoxal 5'-phosphate is bound covalently to Lys315 in the active site
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
259 - 442
L-Asp
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
75.45
35°C, pH 6.8
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 8
approx. 25% of maximal activity at pH 8.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
recombinant Asd
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 55
approx. 25% of maximal activity at 55°C and 20°C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
predicted from amino acid sequence
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ASDA_COMTE
533
0
59584
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
59580
x * 59580, deduced from nucleotide sequence
61000
x * 61000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homododecamer
x-ray crystallography
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 15% (w/v) PEG4000 and 0.1 M lithium sulfate in 0.1 M Tris-HCl buffer (pH 7.4-8.5)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E84K/E88K
the mutant retains 13% activity compared to the wild type enzyme
K17A
the mutant shows 131.2% activity compared to the wild type enzyme
K315A
the mutant shows 36.7% activity compared to the wild type enzyme
R37A
the mutant shows 10.4% activity compared to the wild type enzyme
R425A
the mutant retains 2.5% activity compared to the wild type enzyme
R487A
completely inactive mutant
S67A/Y68A/M69A
the mutant retains less than 1% activity compared to the wild type enzyme
S67E/Y68E/M69E
the mutations produce an inactive dimer
S67R/Y68R/M69R
the mutations produce an inactive dimer
Y134F
the mutant shows 40.3% activity compared to the wild type enzyme
Y207F
the mutant shows 10.7% activity compared to the wild type enzyme
Y441F
the mutant shows 40.8% activity compared to the wild type enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography and HPLC gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expression Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chen, C.C.; Chou, T.L.; Lee, C.Y.
Cloning, expression and characterization of L-aspartate beta-decarboxylase gene from Alcaligenes faecalis CCRC 11585
J. Ind. Microbiol. Biotechnol.
25
132-140
2000
Comamonas testosteroni (Q93QX0)
-
Manually annotated by BRENDA team
Chen, H.J.; Ko, T.P.; Lee, C.Y.; Wang, N.C.; Wang, A.H.
Structure, assembly, and mechanism of a PLP-dependent dodecameric L-aspartate beta-decarboxylase
Structure
17
517-529
2009
Pseudomonas sp., Comamonas testosteroni (Q93QX0), Comamonas testosteroni CCRC 11585 (Q93QX0)
Manually annotated by BRENDA team