Activating Compound | Comment | Organism | Structure |
---|---|---|---|
PanZ | 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. Gene panZ is conserved only in Escherichia coli-related enterobacterial species including Shigella, Salmonella, Klebsiella and Yersinia | Escherichia coli |
Cloned (Comment) | Organism |
---|---|
gene panD, phylogenetic tree, expression of nontagged enzyme in Escherichia coli panZ-deficient strain SN227, expression of His-tagged wild-type and mutant enzymes in Escherichia coli, expression of flag3-tagged enzyme from gene panD with the cat gene inserted between frt sites in Escherichia coli strain MG1655 | Escherichia coli |
Protein Variants | Comment | Organism |
---|---|---|
additional information | generation of diverse panD deletion mutant strains, overview | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-aspartate | Escherichia coli | - |
beta-alanine + CO2 | - |
? | |
L-aspartate | Escherichia coli MG1655 | - |
beta-alanine + CO2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
gene panD | - |
Escherichia coli MG1655 | - |
gene panD | - |
Posttranslational Modification | Comment | Organism |
---|---|---|
proteolytic modification | 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 | Escherichia coli |
Purification (Comment) | Organism |
---|---|
recombinant nontagged enzyme in Escherichia coli panZ-deficient strain SN227 by ultrafiltration, ammonium sulfate fractionation, dialysis, and anionexchange chromatography, recombinant His-tagged wild-type and mutant enzymes and flag3-tagged enzyme from Escherichia coli strain MG1655 by affinity chromatography and dialysis | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-aspartate | - |
Escherichia coli | beta-alanine + CO2 | - |
? | |
L-aspartate | - |
Escherichia coli MG1655 | beta-alanine + CO2 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
PanD | - |
Escherichia coli |
pyruvoyl-dependent l-aspartate alpha-decarboxylase | - |
Escherichia coli |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
pyruvoyl cofactor | dependent on, the enzyme contains a covalently-bound pyruvoyl cofactor | Escherichia coli |
General Information | Comment | Organism |
---|---|---|
evolution | the enzyme is a member of the small class of pyruvoyl-dependent enzymes, which contain a covalently-bound pyruvoyl cofactor | Escherichia coli |
metabolism | the enzyme catalyzes the first step in the biosynthetic pathway of pantothenate and coenzyme A, overview | Escherichia coli |
physiological function | regulation of PanD by PanZ allows these organisms to closely regulate production of beta-alanine and hence pantothenate in response to metabolic demand in host gut flora, where pantothenate is abundant | Escherichia coli |