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Literature summary for 4.1.1.11 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

Activating Compound Comment Organism Structure
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
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)

Cloned (Comment) Organism
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
gene panD, heterologous expression in panM-deficient Salmonella enterica strain JE13153, functional complementation in PanD activity Corynebacterium glutamicum

Protein Variants

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Corynebacterium glutamicum
-
gene panD
-
Salmonella enterica
-
gene panD
-

Posttranslational Modification

Posttranslational Modification Comment Organism
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)

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

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
tetramer
-
Salmonella enterica

Synonyms

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

Cofactor

Cofactor Comment Organism Structure
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
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

General Information Comment Organism
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