Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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)

EC Number Cloned (Comment) Organism
4.3.3.7 from pETSA1, overexpressed Clostridium botulinum

Organism

EC Number Organism UniProt Comment Textmining
4.3.3.7 Clostridium botulinum
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.3.3.7
-
 Clostridium botulinum

Substrates and Products (Substrate)

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

Synonyms

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

Cofactor

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

General Information

EC Number General Information Comment Organism
4.3.3.7 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