Cyclopeptine synthase

Cyclopeptine synthase
Identifiers
EC no.	6.3.2.40
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / QuickGO
Search PMC articles PubMed articles NCBI proteins

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

anthranilate + L-phenylalanine + S-adenosyl-L-methionine + 2 ATP ${\displaystyle \rightleftharpoons }$ 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 ${\displaystyle \rightleftharpoons }$ diphosphate + N-adenylylanthranilate

• phenylalanine adenylyltransferase (EC 2.7.7.54) catalyzes the partial reaction

ATP + L-phenylalanine ${\displaystyle \rightleftharpoons }$ 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.

References

1. Lerbs, W.; Luckner, M. (1985). "Cyclopeptine synthetase activity in surface cultures of Penicillium cyclopium". Journal of Basic Microbiology. 25 (6): 387–391. doi:10.1002/jobm.3620250611. ISSN   0233-111X.