2-Amino-4-deoxychorismate synthase
(Redirected from 2-amino-4-deoxychorismate synthase)
2-amino-4-deoxychorismate synthase (EC 2.6.1.86, ADIC synthase, 2-amino-2-deoxyisochorismate synthase, SgcD) is an enzyme with systematic name (2S)-2-amino-4-deoxychorismate:2-oxoglutarate aminotransferase.[1][2][3][4] This enzyme catalyses the following chemical reaction
2-amino-4-deoxychorismate synthase | |||||||||
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Identifiers | |||||||||
EC no. | 2.6.1.86 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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- (2S)-2-amino-4-deoxychorismate + L-glutamate chorismate + L-glutamine
This enzyme requires Mg2+. The reaction occurs in the reverse direction.
References
edit- ^ Van Lanen SG, Lin S, Shen B (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. 105 (2): 494–9. Bibcode:2008PNAS..105..494V. doi:10.1073/pnas.0708750105. PMC 2206564. PMID 18182490.
- ^ Yu, L.; Mah, S.; Otani, T.; Dedon, P. (1995). "The benzoxazolinate of C-1027 confers intercalative DNA binding". J. Am. Chem. Soc. 117 (34): 8877–8878. doi:10.1021/ja00139a032.
- ^ McDonald M, Mavrodi DV, Thomashow LS, Floss HG (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. 123 (38): 9459–60. doi:10.1021/ja011243. PMID 11562236.
- ^ Laursen JB, Nielsen J (March 2004). "Phenazine natural products: biosynthesis, synthetic analogues, and biological activity". Chemical Reviews. 104 (3): 1663–86. doi:10.1021/cr020473j. PMID 15008629.
External links
edit- 2-amino-4-deoxychorismate+synthase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)