Cloned (Comment) | Organism |
---|---|
gene panD, sequence comparisons and phylogenetic analysis, recombinant expression of the Bacillus halodurans enzyme in DELTApanD as well as DELTApanM mutant Samonella enterica strains can functionally complement both mutant strains and restore growth on minimal medium | Halalkalibacterium halodurans |
gene panD, sequence comparisons and phylogenetic analysis, recombinant expression of the Bacillus halodurans enzyme in DELTApanD as well as DELTApanM mutant Samonella enterica strains can functionally complement both mutant strains and restore growth on minimal medium | Bordetella pertussis |
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 | Helicobacter pylori |
gene panD, sequence comparisons and phylogenetic analysis, recombinant expression of the Klebsiella pneumoniae enzyme in DELTApanD as well as DELTApanM mutant Samonella enterica strains can functionally complement only the DELTApanD strain, but fails to restore growth on minimal medium in the DELTApanM strain | Klebsiella pneumoniae |
gene panD, sequence comparisons and phylogenetic analysis, recombinant expression of the Legionella phneumophila enzyme in DELTApanD as well as DELTApanM mutant Samonella enterica strains can functionally complement both mutant strains and restore growth on minimal medium | Legionella pneumophila |
gene panD, sequence comparisons and phylogenetic analysis, recombinant expression of the Magnetospirillum magneticum enzyme in DELTApanD as well as DELTApanM mutant Samonella enterica strains can functionally complement both mutant strains and restore growth on minimal medium | Magnetospirillum magneticum |
gene panD, sequence comparisons and phylogenetic analysis, recombinant expression of the Moorella thermoacetica enzyme in DELTApanD as well as DELTApanM mutant Samonella enterica strains can functionally complement both mutant strains and restore growth on minimal medium | Moorella thermoacetica |
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 | Neisseria gonorrhoeae |
gene panD, sequence comparisons and phylogenetic analysis, recombinant expression of the Pseudomonas aeruginosa enzyme in DELTApanD as well as DELTApanM mutant Samonella enterica strains can functionally complement only the DELTApanD strain, but fails to restore growth on minimal medium in the DELTApanM strain | Pseudomonas aeruginosa |
gene panD, sequence comparisons and phylogenetic analysis, recombinant expression of the Ralstonia solanacearum enzyme in DELTApanD as well as DELTApanM mutant Samonella enterica strains can functionally complement both mutant strains and restore growth on minimal medium | Ralstonia solanacearum |
gene panD, sequence comparisons and phylogenetic analysis, recombinant expression of the Samonella enterica enzyme in DELTApanD as well as DELTApanM mutant Samonella enterica strains can functionally complement only the DELTApanD strain, but fails to restore growth on minimal medium in the DELTApanM strain | Salmonella enterica subsp. enterica serovar Typhimurium |
gene panD, sequence comparisons and phylogenetic analysis, the recombinant expression of the Corynabacterium glutamicum enzyme in DELTApanD as well as DELTApanM mutant Samonella enterica strains can functionally complement both mutant strains and restore growth on minimal medium | Corynebacterium glutamicum |
Protein Variants | Comment | Organism |
---|---|---|
additional information | generation of knockout mutants DELTApanD (JE13233) and DELTApanM (JE12555) strains | Salmonella enterica subsp. enterica serovar Typhimurium |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-aspartate | Legionella pneumophila | - |
beta-alanine + CO2 | - |
? | |
L-aspartate | Halalkalibacterium halodurans | - |
beta-alanine + CO2 | - |
? | |
L-aspartate | Corynebacterium glutamicum | - |
beta-alanine + CO2 | - |
? | |
L-aspartate | Helicobacter pylori | - |
beta-alanine + CO2 | - |
? | |
L-aspartate | Magnetospirillum magneticum | - |
beta-alanine + CO2 | - |
? | |
L-aspartate | Moorella thermoacetica | - |
beta-alanine + CO2 | - |
? | |
L-aspartate | Neisseria gonorrhoeae | - |
beta-alanine + CO2 | - |
? | |
L-aspartate | Ralstonia solanacearum | - |
beta-alanine + CO2 | - |
? | |
L-aspartate | Salmonella enterica subsp. enterica serovar Typhimurium | - |
beta-alanine + CO2 | - |
? | |
L-aspartate | Klebsiella pneumoniae | - |
beta-alanine + CO2 | - |
? | |
L-aspartate | Pseudomonas aeruginosa | - |
beta-alanine + CO2 | - |
? | |
L-aspartate | Bordetella pertussis | - |
beta-alanine + CO2 | - |
? | |
L-aspartate | Neisseria gonorrhoeae ATCC 700825 / FA 1090 | - |
beta-alanine + CO2 | - |
? | |
L-aspartate | Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025 | - |
beta-alanine + CO2 | - |
? | |
L-aspartate | Magnetospirillum magneticum AMB-1 / ATCC 700264 | - |
beta-alanine + CO2 | - |
? | |
L-aspartate | Helicobacter pylori 26695 | - |
beta-alanine + CO2 | - |
? | |
L-aspartate | Pseudomonas aeruginosa ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1 | - |
beta-alanine + CO2 | - |
? | |
L-aspartate | Salmonella enterica subsp. enterica serovar Typhimurium LT2 / SGSC1412 / ATCC 700720 | - |
beta-alanine + CO2 | - |
? | |
L-aspartate | Halalkalibacterium halodurans ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125 | - |
beta-alanine + CO2 | - |
? | |
L-aspartate | Klebsiella pneumoniae ATCC 700721 / MGH 78578 | - |
beta-alanine + CO2 | - |
? | |
L-aspartate | Moorella thermoacetica ATCC 39073 / JCM 9320 | - |
beta-alanine + CO2 | - |
? | |
L-aspartate | Bordetella pertussis Tohama I / ATCC BAA-589 / NCTC 13251 | - |
beta-alanine + CO2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
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 | - |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
additional information | the L-aspartate-alpha-decarboxylase zymogen from Bacillus halodurans does not require PanM to process its own maturation | Halalkalibacterium halodurans |
additional information | the L-aspartate-alpha-decarboxylase zymogen from Bacillus halodurans does not require PanM to process its own maturation | Bordetella pertussis |
additional information | the L-aspartate-alpha-decarboxylase zymogen from Corynebacterium glutamicum does not require PanM to process its own maturation | Corynebacterium glutamicum |
additional information | the L-aspartate-alpha-decarboxylase zymogen from Helicobacter pylori does not require PanM to process its own maturation | Helicobacter pylori |
additional information | the L-aspartate-alpha-decarboxylase zymogen from Legionella phneumophila does not require PanM to process its own maturation | Legionella pneumophila |
additional information | the L-aspartate-alpha-decarboxylase zymogen from Moorella thermoacetica does not require PanM to process its own maturation | Moorella thermoacetica |
additional information | the L-aspartate-alpha-decarboxylase zymogen from Neisseria gonorrhoeae does not require PanM to process its own maturation | Neisseria gonorrhoeae |
additional information | the L-aspartate-alpha-decarboxylase zymogen from Ralstonia solanacearum does not require PanM to process its own maturation | Ralstonia solanacearum |
additional information | the L-aspartate-alpha-decarboxylase zymogen Magnetospirillum magneticum does not require PanM to process its own maturation | Magnetospirillum magneticum |
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 | Salmonella enterica subsp. enterica serovar Typhimurium |
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 | Klebsiella pneumoniae |
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 | Pseudomonas aeruginosa |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
additional information | 37°C is the optimal growth temperature of the bacterium | Salmonella enterica subsp. enterica serovar Typhimurium | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-aspartate | - |
Legionella pneumophila | beta-alanine + CO2 | - |
? | |
L-aspartate | - |
Halalkalibacterium halodurans | beta-alanine + CO2 | - |
? | |
L-aspartate | - |
Corynebacterium glutamicum | beta-alanine + CO2 | - |
? | |
L-aspartate | - |
Helicobacter pylori | beta-alanine + CO2 | - |
? | |
L-aspartate | - |
Magnetospirillum magneticum | beta-alanine + CO2 | - |
? | |
L-aspartate | - |
Moorella thermoacetica | beta-alanine + CO2 | - |
? | |
L-aspartate | - |
Neisseria gonorrhoeae | beta-alanine + CO2 | - |
? | |
L-aspartate | - |
Ralstonia solanacearum | beta-alanine + CO2 | - |
? | |
L-aspartate | - |
Salmonella enterica subsp. enterica serovar Typhimurium | beta-alanine + CO2 | - |
? | |
L-aspartate | - |
Klebsiella pneumoniae | beta-alanine + CO2 | - |
? | |
L-aspartate | - |
Pseudomonas aeruginosa | beta-alanine + CO2 | - |
? | |
L-aspartate | - |
Bordetella pertussis | beta-alanine + CO2 | - |
? | |
L-aspartate | - |
Neisseria gonorrhoeae ATCC 700825 / FA 1090 | beta-alanine + CO2 | - |
? | |
L-aspartate | - |
Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025 | beta-alanine + CO2 | - |
? | |
L-aspartate | - |
Magnetospirillum magneticum AMB-1 / ATCC 700264 | beta-alanine + CO2 | - |
? | |
L-aspartate | - |
Helicobacter pylori 26695 | beta-alanine + CO2 | - |
? | |
L-aspartate | - |
Pseudomonas aeruginosa ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1 | beta-alanine + CO2 | - |
? | |
L-aspartate | - |
Salmonella enterica subsp. enterica serovar Typhimurium LT2 / SGSC1412 / ATCC 700720 | beta-alanine + CO2 | - |
? | |
L-aspartate | - |
Halalkalibacterium halodurans ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125 | beta-alanine + CO2 | - |
? | |
L-aspartate | - |
Klebsiella pneumoniae ATCC 700721 / MGH 78578 | beta-alanine + CO2 | - |
? | |
L-aspartate | - |
Moorella thermoacetica ATCC 39073 / JCM 9320 | beta-alanine + CO2 | - |
? | |
L-aspartate | - |
Bordetella pertussis Tohama I / ATCC BAA-589 / NCTC 13251 | beta-alanine + CO2 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
L-Aspartate-alpha-decarboxylase | - |
Legionella pneumophila |
L-Aspartate-alpha-decarboxylase | - |
Halalkalibacterium halodurans |
L-Aspartate-alpha-decarboxylase | - |
Corynebacterium glutamicum |
L-Aspartate-alpha-decarboxylase | - |
Helicobacter pylori |
L-Aspartate-alpha-decarboxylase | - |
Magnetospirillum magneticum |
L-Aspartate-alpha-decarboxylase | - |
Moorella thermoacetica |
L-Aspartate-alpha-decarboxylase | - |
Neisseria gonorrhoeae |
L-Aspartate-alpha-decarboxylase | - |
Ralstonia solanacearum |
L-Aspartate-alpha-decarboxylase | - |
Salmonella enterica subsp. enterica serovar Typhimurium |
L-Aspartate-alpha-decarboxylase | - |
Klebsiella pneumoniae |
L-Aspartate-alpha-decarboxylase | - |
Pseudomonas aeruginosa |
L-Aspartate-alpha-decarboxylase | - |
Bordetella pertussis |
PanD | - |
Legionella pneumophila |
PanD | - |
Halalkalibacterium halodurans |
PanD | - |
Corynebacterium glutamicum |
PanD | - |
Helicobacter pylori |
PanD | - |
Magnetospirillum magneticum |
PanD | - |
Moorella thermoacetica |
PanD | - |
Neisseria gonorrhoeae |
PanD | - |
Ralstonia solanacearum |
PanD | - |
Salmonella enterica subsp. enterica serovar Typhimurium |
PanD | - |
Klebsiella pneumoniae |
PanD | - |
Pseudomonas aeruginosa |
PanD | - |
Bordetella pertussis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
additional information | the ancillary protein PanM (formerly YhhK) is required in vitro and in vivo for cleavage of the L-aspartate-alpha-decarboxylase zymogen | Salmonella enterica subsp. enterica serovar Typhimurium | |
additional information | the ancillary protein PanM (formerly YhhK) is required in vitro and in vivo for cleavage of the L-aspartate-alpha-decarboxylase zymogen | Klebsiella pneumoniae | |
additional information | the ancillary protein PanM (formerly YhhK) is required in vitro and in vivo for cleavage of the L-aspartate-alpha-decarboxylase zymogen | Pseudomonas aeruginosa |
General Information | Comment | Organism |
---|---|---|
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 | Legionella pneumophila |
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 | Halalkalibacterium halodurans |
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 | Corynebacterium glutamicum |
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 | Helicobacter pylori |
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 | Magnetospirillum magneticum |
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 | Moorella thermoacetica |
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 | Neisseria gonorrhoeae |
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 | Ralstonia solanacearum |
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 | Salmonella enterica subsp. enterica serovar Typhimurium |
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 | Klebsiella pneumoniae |
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 | Pseudomonas aeruginosa |
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 | Bordetella pertussis |
malfunction | when expressed in the Salmonella enterica DELTApanM strain, all panD homologues from bacteria that also contain a panM gene (Salmonella enterica, Klebsiella pneumoniae, Pseudomonas aeruginosa) fail to restore growth on minimal medium | Salmonella enterica subsp. enterica serovar Typhimurium |
additional information | the ancillary protein PanM (formerly YhhK) is required in vitro and in vivo for cleavage of the L-aspartate-alpha-decarboxylase zymogen | Salmonella enterica subsp. enterica serovar Typhimurium |
additional information | the L-aspartate-alpha-decarboxylase zymogen from Corynebacterium glutamicum does not require PanM to process its own maturation | Corynebacterium glutamicum |