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Information on EC 4.1.1.11 - aspartate 1-decarboxylase and Organism(s) Neisseria gonorrhoeae and UniProt Accession Q5F8Y9

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:
Neisseria gonorrhoeae
UNIPROT: Q5F8Y9
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Word Map
The taxonomic range for the selected organisms is: Neisseria gonorrhoeae
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
aspartate decarboxylase, adcbs, aspartate 1-decarboxylase, l-aspartate-alpha-decarboxylase, tk1814, aspartate-alpha-decarboxylase, bmadc, mj0050, mtbadc, bsadc, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
L-Aspartate-alpha-decarboxylase
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Aspartate alpha-decarboxylase
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Aspartic alpha-decarboxylase
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L-Aspartate alpha-decarboxylase
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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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?
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
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?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
Salmonella enterica and Corynebacterium glutamicum L-aspartate-alpha-decarboxylases represent two different classes of homologues of these enzymes. Class I homologues require PanM for activation, while class II self cleave in the absence of PanM. Computer modeling of conserved amino acids using structure coordinates of PanM and L-aspartate-alpha-decarboxylase available in the protein data bank (RCSB PDB) reveal a putative site of interactions, analysis of self-cleavage mechanism of L-aspartate-alpha-decarboxylases. Phylogenetic distribution of prokaryotic L-aspartate-alpha-decarboxylase and PanM proteins, distribution of the two classes of PanD in the prokaryotes, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
the L-aspartate-alpha-decarboxylase zymogen from Neisseria gonorrhoeae does not require PanM to process its own maturation
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene panD, sequence comparisons and phylogenetic analysis, recombinant expression of the Neisseria gonorrhoeae enzyme in DELTApanD as well as DELTApanM mutant Samonella enterica strains can functionally complement both mutant strains and restore growth on minimal medium
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Stuecker, T.N.; Bramhacharya, S.; Hodge-Hanson, K.M.; Suen, G.; Escalante-Semerena, J.C.
Phylogenetic and amino acid conservation analyses of bacterial L-aspartate-alpha-decarboxylase and of its zymogen-maturation protein reveal a putative interaction domain
BMC Res. Notes
8
354
2015
Bordetella pertussis (Q7VXF8), Bordetella pertussis Tohama I / ATCC BAA-589 / NCTC 13251 (Q7VXF8), Corynebacterium glutamicum (Q9X4N0), Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025 (Q9X4N0), Halalkalibacterium halodurans, Halalkalibacterium halodurans ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125, Helicobacter pylori (P56065), Helicobacter pylori 26695 (P56065), Klebsiella pneumoniae (A6T4S8), Klebsiella pneumoniae ATCC 700721 / MGH 78578 (A6T4S8), Legionella pneumophila, Magnetospirillum magneticum (Q2VZZ9), Magnetospirillum magneticum AMB-1 / ATCC 700264 (Q2VZZ9), Moorella thermoacetica (Q2RM59), Moorella thermoacetica ATCC 39073 / JCM 9320 (Q2RM59), Neisseria gonorrhoeae (Q5F8Y9), Neisseria gonorrhoeae ATCC 700825 / FA 1090 (Q5F8Y9), Pseudomonas aeruginosa (Q9HV68), Pseudomonas aeruginosa ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1 (Q9HV68), Ralstonia solanacearum (Q8XVU6), Salmonella enterica subsp. enterica serovar Typhimurium (P65662), Salmonella enterica subsp. enterica serovar Typhimurium LT2 / SGSC1412 / ATCC 700720 (P65662)
Manually annotated by BRENDA team