EC 2.6.1.86 - 2-amino-4-deoxychorismate synthase

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IntEnz Enzyme Nomenclature
EC 2.6.1.86

Names

Accepted name:
2-amino-4-deoxychorismate synthase
Other names:
ADIC synthase
2-amino-2-deoxyisochorismate synthase
SgcD
Systematic name:
(2S)-2-amino-4-deoxychorismate:2-oxoglutarate aminotransferase

Reaction

Cofactor

Comments:

Requires Mg2+. The reaction occurs in the reverse direction to that shown above. In contrast to most anthranilate-synthase I (ASI) homologues, this enzyme is not inhibited by tryptophan. In Streptomyces globisporus, the sequential action of this enzyme and EC 1.3.99.24, 2-amino-4-deoxychorismate dehydrogenase, leads to the formation of the benzoxazolinate moiety of the enediyne antitumour antibiotic C-1027 [1,2]. In certain Pseudomonads the enzyme participates in the biosynthesis of phenazine, a precursor for several compounds with antibiotic activity [3,4].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot:

References

  1. Van Lanen, S.G., Lin, S. and Shen, B.
    Biosynthesis of the enediyne antitumor antibiotic C-1027 involves a new branching point in chorismate metabolism.
    Proc. Natl. Acad. Sci. USA 105: 494-499 (2008). [PMID: 18182490]
  2. Yu, L., Mah, S., Otani, T. and Dedon, P.
    The benzoxazolinate of C-1027 confers intercalative DNA binding.
    J. Am. Chem. Soc. 117: 8877-8878 (1995).
  3. McDonald, M., Mavrodi, D.V., Thomashow, L.S. and Floss, H.G.
    Phenazine biosynthesis in Pseudomonas fluorescens: branchpoint from the primary shikimate biosynthetic pathway and role of phenazine-1,6-dicarboxylic acid.
    J. Am. Chem. Soc. 123: 9459-9460 (2001). [PMID: 11562236]
  4. Laursen, J.B. and Nielsen, J.
    Phenazine natural products: biosynthesis, synthetic analogues, and biological activity.
    Chem. Rev. 104: 1663-1686 (2004). [PMID: 15008629]

[EC 2.6.1.86 created 2008]