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Literature summary for 4.3.3.7 extracted from

  • Orsburn, B.C.; Melville, S.B.; Popham, D.L.
    EtfA catalyses the formation of dipicolinic acid in Clostridium perfringens (2010), Mol. Microbiol., 75, 178-186.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
from pETSA1, overexpressed Clostridium botulinum

Organism

Organism UniProt Comment Textmining
Clostridium botulinum
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Clostridium botulinum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-aspartate 4-semialdehyde + pyruvate
-
Clostridium botulinum dihydrodipicolinate + 2 H2O
-
?

Synonyms

Synonyms Comment Organism
DapA
-
Clostridium botulinum
DHDPA synthase
-
Clostridium botulinum
dihydro-dipicolinic acid synthase
-
Clostridium botulinum

Cofactor

Cofactor Comment Organism Structure
FAD produces a 5fold increase in dipicolinic acid production Clostridium botulinum
FMN results in a 3fold increase in dipicolinic acid production Clostridium botulinum
additional information neither NAD+ nor NADP+ are involved in the production of dipicolinic acid Clostridium botulinum

General Information

General Information Comment Organism
metabolism sequential production of dihydrodipicolinate and dipicolinic acid appears to be catalysed by DHDPA synthase followed by an electron transfer flavoprotein, EtfA from Clostridium perfringens. Spontaneous dipicolinic acid formation in the presence of high concentrations of DapA Clostridium botulinum