4.1.1.11: aspartate 1-decarboxylase
This is an abbreviated version!
For detailed information about aspartate 1-decarboxylase, go to the full flat file.
Word Map on EC 4.1.1.11
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4.1.1.11
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pantothenate
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pyrazinamide
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pyrazinoic
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self-processing
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pza-resistant
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synthesis
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drug development
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pharmacology
- 4.1.1.11
- pantothenate
- pyrazinamide
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pyrazinoic
-
self-processing
-
pza-resistant
- synthesis
- drug development
- pharmacology
Reaction
Synonyms
ACD, ADC, ADCBs, ADCC.g, ADCCg, ADCE, Aspartate alpha-decarboxylase, aspartate decarboxylase, aspartate-alpha-decarboxylase, Aspartic alpha-decarboxylase, AspDC, BmADC, BsADC, CgADC, Dgad2, GcADC, L-Aspartate alpha-decarboxylase, L-Aspartate-alpha-decarboxylase, MfnA, MJ0050, More, MtbADC, PanD, PF1159, PLP-dependent L-aspartate decarboxylase, pyruvoyl-dependent l-aspartate alpha-decarboxylase, TK1814
ECTree
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Posttranslational Modification
Posttranslational Modification on EC 4.1.1.11 - aspartate 1-decarboxylase
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proteolytic modification
additional information
bacterial ADC is usually translated into an inactive zymogen. The initially inactive recombinant Pi-protein ADC of approximately 14 kDa self-cleaves to form an active enzyme consisting of alpha-protein (approximately 11 kDa) and beta-protein (approximately 3 kDa). The enzyme completely self-cleaves and self-maturates, zymogen is proteolytically cleaved at the Gly24-Ser25 site
proteolytic modification
the ADC protein is initially translated as an inactive Pi-protein and then proteolytically cleaved at a site to generate the active species comprising the pyruvoyl-containing alpha-subunit and a smaller beta-subunit. The cleavage of the recombinant ADC protein from Bacillus subtilis after expression in Escherichia coli is almost complete
proteolytic modification
the enzyme performs self-cleavage posttranslationally
proteolytic modification
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the ADC protein is initially translated as an inactive Pi-protein and then proteolytically cleaved at a site to generate the active species comprising the pyruvoyl-containing alpha-subunit and a smaller beta-subunit. The cleavage of the recombinant ADC protein from Bacillus subtilis after expression in Escherichia coli is almost complete
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proteolytic modification
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the enzyme performs self-cleavage posttranslationally
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proteolytic modification
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bacterial ADC is usually translated into an inactive zymogen. The initially inactive recombinant Pi-protein ADC of approximately 14 kDa self-cleaves to form an active enzyme consisting of alpha-protein (approximately 11 kDa) and beta-protein (approximately 3 kDa). The enzyme completely self-cleaves and self-maturates, zymogen is proteolytically cleaved at the Gly24-Ser25 site
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proteolytic modification
the panD gene product is efficiently proteolytically processed into two subunits, an 11 kDa alpha-subunit and a 2.7 kDa beta-subunit, Gly-24/Ser-25 may be the processing site of the initially translated pi-protein
proteolytic modification
bacterial ADC is usually translated into an inactive zymogen. The initially inactive recombinant Pi-protein ADC of approximately 14 kDa self-cleaves to form an active enzyme consisting of alpha-protein (approximately 11 kDa) and beta-protein (approximately 3 kDa). The enzyme completely self-cleaves and self-maturates, zymogen is proteolytically cleaved at the Gly24-Ser25 site
proteolytic modification
the ADC protein is initially translated as an inactive Pi-protein and then proteolytically cleaved at a site to generate the active species comprising the pyruvoyl-containing alpha-subunit and a smaller beta-subunit. The cleavage of the recombinant ADC protein from Corynebacterium glutamicum after expression in Escherichia coli is almost complete
proteolytic modification
the enzyme performs self-cleavage posttranslationally
proteolytic modification
Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025
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the ADC protein is initially translated as an inactive Pi-protein and then proteolytically cleaved at a site to generate the active species comprising the pyruvoyl-containing alpha-subunit and a smaller beta-subunit. The cleavage of the recombinant ADC protein from Corynebacterium glutamicum after expression in Escherichia coli is almost complete
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proteolytic modification
Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025
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bacterial ADC is usually translated into an inactive zymogen. The initially inactive recombinant Pi-protein ADC of approximately 14 kDa self-cleaves to form an active enzyme consisting of alpha-protein (approximately 11 kDa) and beta-protein (approximately 3 kDa). The enzyme completely self-cleaves and self-maturates, zymogen is proteolytically cleaved at the Gly24-Ser25 site
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proteolytic modification
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the enzyme performs self-cleavage posttranslationally
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proteolytic modification
ADC, which is translated as inactive pro-protein, i.e. pi-protein, undergoes intramolecular self-cleavage at Gly-24/Ser-25 producing the alpha- and beta-subunit, molecular mechanism of self-processing, slow process
proteolytic modification
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an integral pyruvoyl group is formed by an autocatalytic posttranslational modification which cleaves the Gly-24/Ser-25 bond and converts Ser-25 into the pyruvoyl group
proteolytic modification
panD is initially translated as inactive precursor pi-protein which is slowly proteolytically cleaved at a specific Gly-Ser bond producing two dissimilar subunits, autocatalytic mechanism
proteolytic modification
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PanD is activated by the putative acetyltransferase YhhK, termed PanZ. Activation of PanD both in vivo and in vitro is PanZ-dependent. PanZ binds to PanD, cleavage of the recombinant FLAG-tag PanD by recombinant His-tagged PanZ
proteolytic modification
role for Thr57 in the activation of the enzyme, while neither Tyr58 nor Tyr22 is required for the activation reaction, overview
proteolytic modification
bacterial ADC is usually translated into an inactive zymogen. The zymogen is proteolytically cleaved at the Gly24-Ser25 site. The Escherichia coli ADC requires a Gcn5-like N-acetyltransferase, named PanM (also called PanZ), to help it reach complete maturation
proteolytic modification
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PanZ promotes the activation of the zymogen of PanD to form aspartate alpha-decarboxylase (ADC) in a CoA-dependent manner. Binding of PanZ promotes PanD processing, catalytic mechanism, detailed overview. Before binding of PanZ, the carbonyl of Gly24 forms a hydrogen bond to the side chain of Thr57. Binding of PanZ induces a conformation change in the peptide chain rotating the carbonyl of Gly24 to hydrogen bond to Tyr58 and shifting the hydroxyl of Ser25 to a position where reaction is possible. Following attack of the Ser25 hydroxyl on the carbonyl of Gly24 to form the oxyoxazolidine intermediate III, the side chain of Thr57 donates a proton to facilitate cleavage of the C-N bond to form the ester intermediate IV. The deprotonated Thr57 residue is then able to remove the a proton from Ser25 to cleave the peptide chain and generate a dehydroalanine residue V, which hydrolyzes to form the active enzyme
proteolytic modification
the ADC protein is initially translated as an inactive Pi-protein (14 kDa) and then proteolytically cleaved at the Gly24-Ser25 site to generate the active species comprising the pyruvoyl-containing alpha-subunit (11 kDa) and a smaller beta-subunit (3 kDa). The enzyme requires PanZ as an activator involved in the cleavage of ADCE. The recombinant ADC protein expressed from Escherichia coli strain BL21(DE3) is mainly in its inactive uncleaved form, possibly because of insufficience of panZ, an activator involved in the cleavage of ADCE
proteolytic modification
the enzyme requires activation by PanZ to be posttranslationally cleaved
proteolytic modification
Escherichia coli K-12 / DH5alpha
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the ADC protein is initially translated as an inactive Pi-protein (14 kDa) and then proteolytically cleaved at the Gly24-Ser25 site to generate the active species comprising the pyruvoyl-containing alpha-subunit (11 kDa) and a smaller beta-subunit (3 kDa). The enzyme requires PanZ as an activator involved in the cleavage of ADCE. The recombinant ADC protein expressed from Escherichia coli strain BL21(DE3) is mainly in its inactive uncleaved form, possibly because of insufficience of panZ, an activator involved in the cleavage of ADCE
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proteolytic modification
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PanD is activated by the putative acetyltransferase YhhK, termed PanZ. Activation of PanD both in vivo and in vitro is PanZ-dependent. PanZ binds to PanD, cleavage of the recombinant FLAG-tag PanD by recombinant His-tagged PanZ
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proteolytic modification
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panD is initially translated as inactive precursor pi-protein which is slowly proteolytically cleaved at a specific Gly-Ser bond producing two dissimilar subunits, autocatalytic mechanism
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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
proteolytic modification
the ancillary protein PanM (formerly YhhK) is required in vitro and in vivo for cleavage of the L-aspartate-alpha-decarboxylase zymogen. Conserved regions of PanM form a domain where putative interactions with L-aspartate-alpha-decarboxylases may interact, PanD and PanM structure comparisons, overview
proteolytic modification
Klebsiella pneumoniae ATCC 700721 / MGH 78578
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the ancillary protein PanM (formerly YhhK) is required in vitro and in vivo for cleavage of the L-aspartate-alpha-decarboxylase zymogen. Conserved regions of PanM form a domain where putative interactions with L-aspartate-alpha-decarboxylases may interact, PanD and PanM structure comparisons, overview
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proteolytic modification
bacterial ADC is usually translated into an inactive zymogen. The initially inactive recombinant Pi-protein ADC of approximately 14 kDa self-cleaves to form an active enzyme consisting of alpha-protein (approximately 11 kDa) and beta-protein (approximately 3 kDa). The enzyme completely self-cleaves and self-maturates, zymogen is proteolytically cleaved at the Gly24-Ser25 site
proteolytic modification
Lactiplantibacillus plantarum ATCC BAA-793 / NCIMB 8826 / WCFS1
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bacterial ADC is usually translated into an inactive zymogen. The initially inactive recombinant Pi-protein ADC of approximately 14 kDa self-cleaves to form an active enzyme consisting of alpha-protein (approximately 11 kDa) and beta-protein (approximately 3 kDa). The enzyme completely self-cleaves and self-maturates, zymogen is proteolytically cleaved at the Gly24-Ser25 site
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proteolytic modification
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incubation of panD at 37°C for several hours results in a complete cleavage of the inactive pi-form into the two subunits alpha and beta, optimal cleavage at 37°C for 48 h, cleavage mechanism
proteolytic modification
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the enzyme is autocatalytically self-processing, overview
proteolytic modification
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incubation of panD at 37°C for several hours results in a complete cleavage of the inactive pi-form into the two subunits alpha and beta, optimal cleavage at 37°C for 48 h, cleavage mechanism
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proteolytic modification
the ancillary protein PanM (formerly YhhK) is required in vitro and in vivo for cleavage of the L-aspartate-alpha-decarboxylase zymogen. Conserved regions of PanM form a domain where putative interactions with L-aspartate-alpha-decarboxylases may interact, PanD and PanM structure comparisons, overview
proteolytic modification
Pseudomonas aeruginosa ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1
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the ancillary protein PanM (formerly YhhK) is required in vitro and in vivo for cleavage of the L-aspartate-alpha-decarboxylase zymogen. Conserved regions of PanM form a domain where putative interactions with L-aspartate-alpha-decarboxylases may interact, PanD and PanM structure comparisons, overview
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proteolytic modification
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PanD is a pyruvoyl enzyme that is synthesized by the cell as an inactive precursor, pro-PanD. Maturation of pro-PanD into PanD occurs via a self-cleavage event at residue Ser25, which forms the catalytic pyruvoyl moiety. Salmonella enterica PanM, a Gcn5-like N-acetyltransferase, is necessary for pro-PanD maturation, both in vitro and in vivo
proteolytic modification
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the enzyme PanD is synthesized as pro-PanD, which undergoes an auto-proteolytic cleavage at residue Ser25 to yield the catalytic pyruvoyl moiety of the enzyme, interaction with YhhK, i.e. PanM, accelerates the maturation process
proteolytic modification
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PanD is a pyruvoyl enzyme that is synthesized by the cell as an inactive precursor, pro-PanD. Maturation of pro-PanD into PanD occurs via a self-cleavage event at residue Ser25, which forms the catalytic pyruvoyl moiety. Salmonella enterica PanM, a Gcn5-like N-acetyltransferase, is necessary for pro-PanD maturation, both in vitro and in vivo
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proteolytic modification
the ancillary protein PanM (formerly YhhK) is required in vitro and in vivo for cleavage of the L-aspartate-alpha-decarboxylase zymogen. Conserved regions of PanM form a domain where putative interactions with L-aspartate-alpha-decarboxylases may interact, PanD and PanM structure comparisons, overview
proteolytic modification
Salmonella enterica subsp. enterica serovar Typhimurium LT2 / SGSC1412 / ATCC 700720
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the ancillary protein PanM (formerly YhhK) is required in vitro and in vivo for cleavage of the L-aspartate-alpha-decarboxylase zymogen. Conserved regions of PanM form a domain where putative interactions with L-aspartate-alpha-decarboxylases may interact, PanD and PanM structure comparisons, overview
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the L-aspartate-alpha-decarboxylase zymogen from Bacillus halodurans does not require PanM to process its own maturation
additional information
Bordetella pertussis Tohama I / ATCC BAA-589 / NCTC 13251
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the L-aspartate-alpha-decarboxylase zymogen from Bacillus halodurans does not require PanM to process its own maturation
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additional information
the L-aspartate-alpha-decarboxylase zymogen from Corynebacterium glutamicum does not require PanM to process its own maturation
additional information
Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025
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the L-aspartate-alpha-decarboxylase zymogen from Corynebacterium glutamicum does not require PanM to process its own maturation
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additional information
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the Escherichia coli enzyme requires the regulatroy factor PanZ for proteolytic cleavage of the zymogen to form the mature enzyme
additional information
Halalkalibacterium halodurans
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the L-aspartate-alpha-decarboxylase zymogen from Bacillus halodurans does not require PanM to process its own maturation
additional information
Halalkalibacterium halodurans ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125
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the L-aspartate-alpha-decarboxylase zymogen from Bacillus halodurans does not require PanM to process its own maturation
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additional information
the L-aspartate-alpha-decarboxylase zymogen from Helicobacter pylori does not require PanM to process its own maturation
additional information
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the L-aspartate-alpha-decarboxylase zymogen from Helicobacter pylori does not require PanM to process its own maturation
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additional information
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the L-aspartate-alpha-decarboxylase zymogen from Legionella phneumophila does not require PanM to process its own maturation
additional information
the L-aspartate-alpha-decarboxylase zymogen Magnetospirillum magneticum does not require PanM to process its own maturation
additional information
Magnetospirillum magneticum AMB-1 / ATCC 700264
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the L-aspartate-alpha-decarboxylase zymogen Magnetospirillum magneticum does not require PanM to process its own maturation
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additional information
the L-aspartate-alpha-decarboxylase zymogen from Moorella thermoacetica does not require PanM to process its own maturation
additional information
Moorella thermoacetica ATCC 39073 / JCM 9320
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the L-aspartate-alpha-decarboxylase zymogen from Moorella thermoacetica does not require PanM to process its own maturation
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additional information
the L-aspartate-alpha-decarboxylase zymogen from Neisseria gonorrhoeae does not require PanM to process its own maturation
additional information
Neisseria gonorrhoeae ATCC 700825 / FA 1090
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the L-aspartate-alpha-decarboxylase zymogen from Neisseria gonorrhoeae does not require PanM to process its own maturation
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additional information
the L-aspartate-alpha-decarboxylase zymogen from Ralstonia solanacearum does not require PanM to process its own maturation