Biology:2-Amino-4-deoxychorismate dehydrogenase
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Short description: Class of enzymes
2-amino-4-deoxychorismate dehydrogenase | |||||||||
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Identifiers | |||||||||
EC number | 1.3.99.24 | ||||||||
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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2-Amino-4-deoxychorismate dehydrogenase (EC 1.3.99.24, ADIC dehydrogenase, 2-amino-2-deoxyisochorismate dehydrogenase, SgcG) is an enzyme with systematic name (2S)-2-amino-4-deoxychorismate:FMN oxidoreductase.[1][2] This enzyme catalyses the following chemical reaction
- (2S)-2-amino-4-deoxychorismate + FMN [math]\displaystyle{ \rightleftharpoons }[/math] 3-(1-carboxyvinyloxy)anthranilate + FMNH2
This enzyme participates in the formation of the benzoxazolinate moiety of the enediyne antitumour antibiotic C-1027].
References
- ↑ "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. January 2008. doi:10.1073/pnas.0708750105. PMID 18182490. Bibcode: 2008PNAS..105..494V.
- ↑ "The benzoxazolinate of C-1027 confers intercalative DNA binding". J. Am. Chem. Soc. 117 (34): 8877–8878. 1995. doi:10.1021/ja00139a032.
External links
- 2-amino-4-deoxychorismate+dehydrogenase at the US National Library of Medicine Medical Subject Headings (MeSH)
Original source: https://en.wikipedia.org/wiki/2-Amino-4-deoxychorismate dehydrogenase.
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