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Literature summary for 4.1.1.11 extracted from

  • 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 (2002), Acta Crystallogr. Sect. D, 58, 861-863.
    View publication on PubMed
Search for more literature for 4.1.1.11

Cloned(Commentary)

Cloned (Comment) Organism
panD gene, overexpression in Escherichia coli C41(DE3) Helicobacter pylori

Crystallization (Commentary)

Crystallization (Comment) Organism
recombinant enzyme in the presence of the substrate analogue isoasparagine, hanging-drop vapour-diffusion method, X-ray analysis Helicobacter pylori

Localization

Localization Comment Organism GeneOntology No. Textmining
soluble recombinant enzyme Helicobacter pylori
-
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-aspartate Helicobacter pylori step in the major route of beta-alanine production for pantothenate biosynthesis in bacteria beta-alanine + CO2
-
 ?

Organism

Organism UniProt Comment Textmining
Helicobacter pylori
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme Helicobacter pylori

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-aspartate alpha-decarboxylation Helicobacter pylori beta-alanine + CO2
-
 ?
L-aspartate step in the major route of beta-alanine production for pantothenate biosynthesis in bacteria Helicobacter pylori beta-alanine + CO2
-
 ?

Synonyms

Synonyms Comment Organism
PanD
-
 Helicobacter pylori