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Information on EC 4.1.1.11 - aspartate 1-decarboxylase and Organism(s) Methanocaldococcus jannaschii and UniProt Accession Q60358

for references in articles please use BRENDA:EC4.1.1.11
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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:
Methanocaldococcus jannaschii
UNIPROT: Q60358
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Word Map
The taxonomic range for the selected organisms is: Methanocaldococcus jannaschii
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
aspartate decarboxylase, aspartate 1-decarboxylase, adcbs, l-aspartate-alpha-decarboxylase, aspartate-alpha-decarboxylase, tk1814, bmadc, mj0050, mtbadc, l-aspartate alpha-decarboxylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PLP-dependent L-aspartate decarboxylase
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Aspartate alpha-decarboxylase
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-
-
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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
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
the product beta-alanine is required for the biosynthesis of coenzyme A
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.8
L-aspartate
pH 8.0, 70°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.09
pH 8.0, 70°C, recombinant enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the MJ0050 gene complements the Escherichia coli panD deletion mutant cells, in which panD encoding aspartate decarboxylase in Escherichia coli has been knocked out, thus confirming the function of this gene in vivo
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wang, Y.; Xu, H.; White, R.H.
beta-Alanine biosynthesis in Methanocaldococcus jannaschii
J. Bacteriol.
196
2869-2875
2014
Methanocaldococcus jannaschii (Q60358), Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661 (Q60358)
Manually annotated by BRENDA team