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Literature summary for 4.1.1.11 extracted from

  • Nozaki, S.; Webb, M.E.; Niki, H.
    An activator for pyruvoyl-dependent l-aspartate alpha-decarboxylase is conserved in a small group of the gamma-proteobacteria including Escherichia coli (2012), MicrobiologyOpen, 1, 298-310.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.1.1.11

Activating Compound

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(Commentary)

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

Protein Variants Comment Organism
additional information generation of diverse panD deletion mutant strains, overview Escherichia coli

Natural Substrates/ Products (Substrates)

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

Organism UniProt Comment Textmining
Escherichia coli
-
 gene panD
-
Escherichia coli MG1655
-
 gene panD
-

Posttranslational Modification

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 (Commentary)

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 and Products (Substrate)

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

Synonyms Comment Organism
PanD
-
 Escherichia coli
pyruvoyl-dependent l-aspartate alpha-decarboxylase
-
 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Escherichia coli

Cofactor

Cofactor Comment Organism Structure
pyruvoyl cofactor dependent on, the enzyme contains a covalently-bound pyruvoyl cofactor Escherichia coli

General Information

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