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Cyclopeptine synthase

From Wikipedia, the free encyclopedia

Cyclopeptine synthase (EC 6.3.2.40) is an enzyme that catalyzes the chemical reaction

anthranilate + L-phenylalanine + S-adenosyl-L-methionine + 2 ATP cyclopeptine + 2 AMP + S-adenosyl-L-homocysteine + 2 diphosphate + 2 H(+)

In Penicillium cyclopium, cyclopeptine synthase is important for benzodiazepine alkaloid biosynthesis.[1]

Enzyme Classification History

Formerly, cyclopentine synthase activity was classified under two separate enzymes.

  • anthranilate adenylyltransferase (EC 2.7.7.55) catalyzes the partial reaction
ATP + anthranilate diphosphate + N-adenylylanthranilate
  • phenylalanine adenylyltransferase (EC 2.7.7.54) catalyzes the partial reaction
ATP + L-phenylalanine diphosphate + N-adenylyl-L-phenylalanine

EC 2.7.7.54 and EC 2.7.7.55 were reclassified and merged into EC 6.3.2.40.

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