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Literature summary extracted from

  • Stuecker, T.N.; Hodge, K.M.; Escalante-Semerena, J.C.
    The missing link in coenzyme A biosynthesis: PanM (formerly YhhK), a yeast GCN5 acetyltransferase homologue triggers aspartate decarboxylase (PanD) maturation in Salmonella enterica (2012), Mol. Microbiol., 84, 608-619.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
4.1.1.11 additional information the enzyme does not require activation by an endogenous PanM-like protein, incontrast to other species like Escherichia coli or Salmonella enterica Corynebacterium glutamicum
4.1.1.11 YhhK or PanM, the protein interacts directly with PanD, such interactions accelerate pro-PanD maturation, analysis by yeast two hybrid system. One PanM monomer (14.5 kDa) interacts with one PanD tetramer (55.6 kDa) Salmonella enterica

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.1.11 gene panD, expression of Corynebacterium glutamicum panD in Salmonella enterica panM deficient strain JE13233 shows functional complementation, thus the Corynebacterium glutamicum enzyme does not required panM activation Salmonella enterica
4.1.1.11 gene panD, heterologous expression in panM-deficient Salmonella enterica strain JE13153, functional complementation in PanD activity Corynebacterium glutamicum

Protein Variants

EC Number Protein Variants Comment Organism
4.1.1.11 additional information the PanM-deficient Salmonella enterica strain JE13153 is inactive due to impaired activation of PanD Salmonella enterica

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.1.1.11 55600
-
-
 Salmonella enterica

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.1.11 L-aspartate Corynebacterium glutamicum
-
 beta-alanine + CO2
-
 ?
4.1.1.11 L-aspartate Salmonella enterica
-
 beta-alanine + CO2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.11 Corynebacterium glutamicum
-
 gene panD
-
4.1.1.11 Salmonella enterica
-
 gene panD
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
4.1.1.11 proteolytic modification 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 Salmonella enterica

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.1.11 native enzyme from Salmonella enterica strain JE13153 lacking panM by anion exchange chromatography Salmonella enterica

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.11 L-aspartate
-
 Corynebacterium glutamicum beta-alanine + CO2
-
 ?
4.1.1.11 L-aspartate
-
 Salmonella enterica beta-alanine + CO2
-
 ?

Subunits

EC Number Subunits Comment Organism
4.1.1.11 tetramer
-
 Salmonella enterica

Synonyms

EC Number Synonyms Comment Organism
4.1.1.11 aspartate decarboxylase
-
 Corynebacterium glutamicum
4.1.1.11 aspartate decarboxylase
-
 Salmonella enterica
4.1.1.11 L-Aspartate-alpha-decarboxylase
-
 Corynebacterium glutamicum
4.1.1.11 L-Aspartate-alpha-decarboxylase
-
 Salmonella enterica
4.1.1.11 PanD
-
 Corynebacterium glutamicum
4.1.1.11 PanD
-
 Salmonella enterica

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.1.11 pyruvoyl cofactor 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 Corynebacterium glutamicum
4.1.1.11 pyruvoyl cofactor 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 Salmonella enterica

General Information

EC Number General Information Comment Organism
4.1.1.11 additional information 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 Salmonella enterica