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Information on EC 4.1.1.11 - aspartate 1-decarboxylase and Organism(s) Helicobacter pylori and UniProt Accession P56065

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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:
Helicobacter pylori
UNIPROT: P56065
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Word Map
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The taxonomic range for the selected organisms is: Helicobacter pylori
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
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L-aspartate
=
beta-alanine
+
CO2
=
+
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
L-Aspartate-alpha-decarboxylase
-
Aspartate alpha-decarboxylase
-
-
-
-
Aspartic alpha-decarboxylase
-
-
-
-
L-Aspartate alpha-decarboxylase
-
-
-
-
L-Aspartate-alpha-decarboxylase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-aspartate = beta-alanine + CO2
show the reaction diagram
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
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
-
-
-
-
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
-
-
-
?
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
-
-
-
?
L-aspartate
beta-alanine + CO2
show the reaction diagram
-
step in the major route of beta-alanine production for pantothenate biosynthesis in bacteria
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
recombinant enzyme
-
Manually annotated by BRENDA team
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
proteolytic modification
self-processing of subunits at Gly24-Ser25 producing beta-chain with residues 1-24 and alpha chain with residues 25-117. In the apo structure, Ser25, which forms the N-terminus of alpha chain, is converted to a pyruvoyl group
additional information
the L-aspartate-alpha-decarboxylase zymogen from Helicobacter pylori does not require PanM to process its own maturation
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
both apo form and in complex with isoasparagine
recombinant enzyme in the presence of the substrate analogue isoasparagine, hanging-drop vapour-diffusion method, X-ray analysis
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene panD, sequence comparisons and phylogenetic analysis, recombinant expression of the Helicobacter pylori enzyme in DELTApanD as well as DELTApanM mutant Samonella enterica strains can functionally complement both mutant strains and restore growth on minimal medium
panD gene, overexpression in Escherichia coli C41(DE3)
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kwon, A.R.; Lee, B.I.; Han, B.W.; Ahn, H.J.; Yang, J.K.; Yoon, H.J.; Suh, S.W.
Crystallization and preliminary X-ray crystallographic analysis of aspartate 1-decarboxylase from Helicobacter pylori
Acta Crystallogr. Sect. D
58
861-863
2002
Helicobacter pylori
Manually annotated by BRENDA team
Lee, B.I.; Suh, S.W.
Crystal structure of the Schiff base intermediate prior to decarboxylation in the catalytic cycle of aspartate alpha-decarboxylase
J. Mol. Biol.
340
1-7
2004
Helicobacter pylori (P56065), Helicobacter pylori
Manually annotated by BRENDA team
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