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2-Amino-4-deoxychorismate synthase
Class of enzymes
Class of enzymes
| Field | Value |
|---|---|
| Name | 2-amino-4-deoxychorismate synthase |
| EC_number | 2.6.1.86 |
2-amino-4-deoxychorismate synthase (, ADIC synthase, 2-amino-2-deoxyisochorismate synthase, SgcD) is an enzyme with systematic name (2S)-2-amino-4-deoxychorismate:2-oxoglutarate aminotransferase. This enzyme catalyses the following chemical reaction
This reaction is an early part of the biosynthesis of the benzoxazolinate fragment of the enediyne antitumour antibiotic C-1027 from Streptomyces globisporus. 2-amino-2-deoxyisochorismic acid is produced from chorismic acid by transamination using glutamine as the source of the amino group:
The enzyme requires Mg2+.
References
References
- (January 2008). "Biosynthesis of the enediyne antitumor antibiotic C-1027 involves a new branching point in chorismate metabolism". Proceedings of the National Academy of Sciences of the United States of America.
- (1995). "The benzoxazolinate of C-1027 confers intercalative DNA binding". J. Am. Chem. Soc..
- (September 2001). "Phenazine biosynthesis in Pseudomonas fluorescens: branchpoint from the primary shikimate biosynthetic pathway and role of phenazine-1,6-dicarboxylic acid". Journal of the American Chemical Society.
- (March 2004). "Phenazine natural products: biosynthesis, synthetic analogues, and biological activity". Chemical Reviews.
- {{KEGG enzyme. 2.6.1.86
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