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Information on EC 4.1.1.11 - aspartate 1-decarboxylase
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4.1.1.11 aspartate 1-decarboxylaseIUBMB Comments
The Escherichia coli enzyme contains a pyruvoyl group.
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Word Map
- 4.1.1.11
- pantothenate
- pyrazinamide
-
pyrazinoic
-
self-processing
-
pza-resistant
- synthesis
- drug development
- pharmacology
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
aspartate decarboxylase, aspartate 1-decarboxylase, adcbs, l-aspartate-alpha-decarboxylase, aspartate-alpha-decarboxylase, tk1814, bmadc, mj0050, mtbadc, bsadc, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ACD
ADC
ADCBs
ADCC.g
ADCCg
ADCE
Aspartate alpha-decarboxylase
aspartate decarboxylase
aspartate-alpha-decarboxylase
Aspartic alpha-decarboxylase
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-
-
-
BsADC
CgADC
L-Aspartate alpha-decarboxylase
L-Aspartate-alpha-decarboxylase
MfnA
MJ0050
PanD
PLP-dependent L-aspartate decarboxylase
pyruvoyl-dependent l-aspartate alpha-decarboxylase
TK1814
additional information
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the enzyme belongs to a small class of self-cleaving and pyruvoyl-dependent amino acid decarboxylases
Aspartate 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
Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025
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-
L-Aspartate-alpha-decarboxylase
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-
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L-Aspartate-alpha-decarboxylase
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L-Aspartate-alpha-decarboxylase
Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025
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L-Aspartate-alpha-decarboxylase
Halalkalibacterium halodurans ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125
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L-Aspartate-alpha-decarboxylase
Pseudomonas aeruginosa ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1
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L-Aspartate-alpha-decarboxylase
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L-Aspartate-alpha-decarboxylase
Salmonella enterica subsp. enterica serovar Typhimurium LT2 / SGSC1412 / ATCC 700720
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PanD
Halalkalibacterium halodurans ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125
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-
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PanD
Pseudomonas aeruginosa ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1
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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-aspartate = beta-alanine + CO2
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-
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L-aspartate = beta-alanine + CO2
in the apo structure, N-terminal Ser25 of alpha chain is converted to pyruvoyl group. Substrate analogue isoasparagine becomes covalently attached to the pyruvoyl group forming the Schiff base intermediate prior to decarboxylation
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
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SYSTEMATIC NAME
IUBMB Comments
L-aspartate 1-carboxy-lyase (beta-alanine-forming)
The Escherichia coli enzyme contains a pyruvoyl group.
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CAS REGISTRY NUMBER
COMMENTARY
9024-58-2
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-aspartate
beta-alanine + CO2
-
-
-
?
L-aspartate
beta-alanine + CO2
essential for beta-alanine synthesis, involved in pantothenate biosynthesis
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?
L-aspartate
beta-alanine + CO2
-
-
-
?
L-aspartate
beta-alanine + CO2
Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025
-
-
-
?
L-aspartate
beta-alanine + CO2
-
-
-
?
L-aspartate
beta-alanine + CO2
-
reaction occurs with retention of configuration, Tyr58 acts as proton donor in the decarboxylation mechanism, the active sites are between subunits, mechanism involves formation of an imine between the amino group of aspartate and an integral pyruvoyl group formed by an autocatalytic posttranslational modification
-
?
L-aspartate
beta-alanine + CO2
Thr-57 and a water molecule are probable catalytic residues able to support acid-base catalysis, enzyme structure
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?
L-aspartate
beta-alanine + CO2
involved in pantothenate biosynthesis
-
?
L-aspartate
beta-alanine + CO2
-
involved in the biosynthesis of pantothenate
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?
L-aspartate
beta-alanine + CO2
major route of beta-alanine production essential for the biosynthesis of pantothenate
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?
L-aspartate
beta-alanine + CO2
alpha-decarboxylation
-
?
L-aspartate
beta-alanine + CO2
involved in pantothenate biosynthesis
-
?
L-aspartate
beta-alanine + CO2
Halalkalibacterium halodurans ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125
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-
-
-
?
L-aspartate
beta-alanine + CO2
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step in the major route of beta-alanine production for pantothenate biosynthesis in bacteria
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?
L-aspartate
beta-alanine + CO2
Lactiplantibacillus plantarum ATCC BAA-793 / NCIMB 8826 / WCFS1
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-
-
?
L-aspartate
beta-alanine + CO2
the product beta-alanine is required for the biosynthesis of coenzyme A
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-
?
L-aspartate
beta-alanine + CO2
the product beta-alanine is required for the biosynthesis of coenzyme A
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?
L-aspartate
beta-alanine + CO2
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one of the most crucial steps in the pantothenate synthesis pathway
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?
L-aspartate
beta-alanine + CO2
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the enzyme is a critical regulatory enzyme in the pantothenate biosynthetic pathway
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?
L-aspartate
beta-alanine + CO2
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Ser25 is the catalytic residue, self-processing and catalytic mechanism, overview
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?
L-aspartate
beta-alanine + CO2
-
one of the most crucial steps in the pantothenate synthesis pathway
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?
L-aspartate
beta-alanine + CO2
Pseudomonas aeruginosa ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1
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-
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?
L-aspartate
beta-alanine + CO2
the enzyme also catalyzes the decarboxylation of L-glutamate with slightly lower efficiency. No activity with D-aspartate
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?
L-aspartate
beta-alanine + CO2
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-
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?
L-aspartate
beta-alanine + CO2
Salmonella enterica subsp. enterica serovar Typhimurium LT2 / SGSC1412 / ATCC 700720
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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. 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
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?
additional information
?
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fluorometric method for beta-alanine determination, development of a high-throughput screening method for beta-alanine detection
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?
additional information
?
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fluorometric method for beta-alanine determination, development of a high-throughput screening method for beta-alanine detection
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?
additional information
?
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large-scale enzymatic production of beta-alanine from L-aspartate by pH-stat directed, fed-batch-feeding strategy, method development and evaluation, overview
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?
additional information
?
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the enzyme performs self-cleavage for catalytic activition
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?
additional information
?
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fluorometric method for beta-alanine determination, development of a high-throughput screening method for beta-alanine detection
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?
additional information
?
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the enzyme performs self-cleavage for catalytic activition
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?
additional information
?
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large-scale enzymatic production of beta-alanine from L-aspartate by pH-stat directed, fed-batch-feeding strategy, method development and evaluation, overview
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?
additional information
?
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Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025
fluorometric method for beta-alanine determination, development of a high-throughput screening method for beta-alanine detection
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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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?
additional information
?
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(2R,3R)-3-fluoroaspartic acid and (2R,3S)-3-fluoroaspartic acid can act as substrates of ADC enzymes for single turnover, but not catalytic, reactions
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?
additional information
?
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fluorometric method for beta-alanine determination, development of a high-throughput screening method for beta-alanine detection
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?
additional information
?
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Escherichia coli K-12 / DH5alpha
fluorometric method for beta-alanine determination, development of a high-throughput screening method for beta-alanine detection
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?
additional information
?
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(2R,3R)-3-fluoroaspartic acid and (2R,3S)-3-fluoroaspartic acid can act as substrates of ADC enzymes for single turnover, but not catalytic, reactions
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?
additional information
?
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the enzyme is a glutamate decarboxylase (GAD) homologue encoded by gene TK1814. The recombinant bifunctional TK1814 protein displays not only GAD activity but also ADC activity using pyridoxal 5'-phosphate as a cofactor
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?
additional information
?
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the enzyme is a glutamate decarboxylase (GAD) homologue encoded by gene TK1814. The recombinant bifunctional TK1814 protein displays not only GAD activity but also ADC activity using pyridoxal 5'-phosphate as a cofactor
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?
additional information
?
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the kcat/Km value with Asp is much higher than that with Glu, suggesting that Asp is the preferred substrate of the TK1814 protein
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?
additional information
?
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the kcat/Km value with Asp is much higher than that with Glu, suggesting that Asp is the preferred substrate of the TK1814 protein
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?
additional information
?
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Thermococcus kodakarensis ATCC BAA-918 / JCM 12380 / KOD1
the enzyme is a glutamate decarboxylase (GAD) homologue encoded by gene TK1814. The recombinant bifunctional TK1814 protein displays not only GAD activity but also ADC activity using pyridoxal 5'-phosphate as a cofactor
-
-
?
additional information
?
-
Thermococcus kodakarensis ATCC BAA-918 / JCM 12380 / KOD1
the kcat/Km value with Asp is much higher than that with Glu, suggesting that Asp is the preferred substrate of the TK1814 protein
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-aspartate
beta-alanine + CO2
-
-
-
?
L-aspartate
beta-alanine + CO2
essential for beta-alanine synthesis, involved in pantothenate biosynthesis
-
?
L-aspartate
beta-alanine + CO2
-
-
-
?
L-aspartate
beta-alanine + CO2
Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025
-
-
-
?
L-aspartate
beta-alanine + CO2
-
-
-
?
L-aspartate
beta-alanine + CO2
involved in pantothenate biosynthesis
-
?
L-aspartate
beta-alanine + CO2
-
involved in the biosynthesis of pantothenate
-
?
L-aspartate
beta-alanine + CO2
major route of beta-alanine production essential for the biosynthesis of pantothenate
-
?
L-aspartate
beta-alanine + CO2
involved in pantothenate biosynthesis
-
?
L-aspartate
beta-alanine + CO2
Halalkalibacterium halodurans ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125
-
-
-
-
?
L-aspartate
beta-alanine + CO2
-
step in the major route of beta-alanine production for pantothenate biosynthesis in bacteria
-
?