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Information on EC 4.1.1.11 - aspartate 1-decarboxylase and Organism(s) Drosophila melanogaster

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.11 aspartate 1-decarboxylase
IUBMB Comments
The Escherichia coli enzyme contains a pyruvoyl group.
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This record set is specific for:
Drosophila melanogaster
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Word Map
The taxonomic range for the selected organisms is: Drosophila melanogaster
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
aspartate decarboxylase, adcbs, aspartate 1-decarboxylase, l-aspartate-alpha-decarboxylase, aspartate-alpha-decarboxylase, tk1814, bmadc, mj0050, mtbadc, aspdc, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Aspartate alpha-decarboxylase
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aspartate-alpha-decarboxylase
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Aspartic alpha-decarboxylase
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-
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L-Aspartate alpha-decarboxylase
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-
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L-Aspartate-alpha-decarboxylase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
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SYSTEMATIC NAME
IUBMB Comments
L-aspartate 1-carboxy-lyase (beta-alanine-forming)
The Escherichia coli enzyme contains a pyruvoyl group.
CAS REGISTRY NUMBER
COMMENTARY hide
9024-58-2
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-aspartate
beta-alanine + CO2
show the reaction diagram
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-
-
-
?
additional information
?
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the enzyme also shows cysteine sulfinic acid decarboxylase activity, EC 4.1.1.29, catalyzing the decarboxylation of cysteine sulfinic acid and cysteic acid
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-
?
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
beta-alanine + CO2
show the reaction diagram
-
-
-
-
?
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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?
X2J8B3_DROME
514
0
58477
TrEMBL
other Location (Reliability: 2)
Q24062_DROME
575
0
64796
TrEMBL
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
58000
-
x * 58000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 58000, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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black1 mutant flies have significantly reduced enzyme activity in adults and at purpuration formation, and no enzyme protein
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Phillips, A.M.; Smart, R.; Strauss, R.; Brembs, B.; Kelly, L.E.
The Drosophila black enigma: The molecular and behavioural characterization of the black1 mutant allele
Gene
351
131-142
2005
Drosophila melanogaster
Manually annotated by BRENDA team
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
Insect Biochem. Mol. Biol.
42
396-403
2012
Aedes aegypti, Drosophila melanogaster
Manually annotated by BRENDA team