Ergocryptine

alpha-Ergocryptine

Identifiers
CAS Number	511-09-1 Y
PubChem CID	134551
IUPHAR/BPS	271
ChemSpider	118591 N
ChEMBL	CHEMBL1403281 N
ECHA InfoCard	100.007.384
Chemical and physical data
Formula	C32H41N5O5
Molar mass	575.698 g/mol
3D model (Jmol)	Interactive image
SMILES O=C3N1CCC[C@H]1[C@]2(O)O[C@](C(=O)N2[C@H]3CC(C)C)(NC(=O)[C@@H]7/C=C6/c4cccc5c4c(cn5)C[C@H]6N(C)C7)C(C)C
InChI InChI=1S/C32H41N5O5/c1-17(2)12-25-29(39)36-11-7-10-26(36)32(41)37(25)30(40)31(42-32,18(3)4)34-28(38)20-13-22-21-8-6-9-23-27(21)19(15-33-23)14-24(22)35(5)16-20/h6,8-9,13,15,17-18,20,24-26,33,41H,7,10-12,14,16H2,1-5H3,(H,34,38)/t20-,24-,25+,26+,31-,32+/m1/s1 N Key:YDOTUXAWKBPQJW-NSLWYYNWSA-N N
NY (what is this?)

Ergocryptine is an ergopeptine and one of the ergot alkaloids. It is isolated from ergot or fermentation broth and it serves as starting material for the production of bromocriptine.

Ergocryptine is a mixture of two very similar compounds, alpha- and beta-ergocryptine. The beta differs from the alpha form only in the position of a single methyl group, which is a consequence of the biosynthesis in which the proteinogenic amino acid leucine is replaced by isoleucine.

The biosynthetic pathways to ergocryptine starts with the prenylation of L-tryptophan in an SN1 fashion with Dimethylallylpyrophosphate (DMAPP). The DMAPP is derived from Mevalonic Acid. This reaction is catalyzed by a prenyltransferase enzyme (Prenyltransferase 4-dimethylallyltryptophan synthase) named FgaPT2 in A. fumigatus. An X-ray structure of the prenyltransferase FgaPT2 and tryptophan has been reported, and used to propose a three step mechanism (formation of allylic carbocation, nucleophilic attack of tryptophan on the carbocation, then deprotonation to restore aromaticity and generate the product, 4-dimethylallyltryptophan (DMAT)). DMAT is then N-methylated at the amino of the tryptophan backbone with the EasF enzyme, named FgaMT in A. fumigatus. S-adenosylmethionine (SAM) being the methyl source.

The next step in the biosynthesis of ergocryptine is the transformation of 4-dimethylallyl abrine to Chanoclavine-I. It has been shown that the enzymes EasE and EasC (FgaOx1 and FgaCat in A. fumigatus, respectively) are both required to generate Chanoclavine-I from 4-DMA abrine. Mutation experiments altering these enzymes independently stopped the pathway at abrine. This indicates that cooperation between EasE and EasC is necessary.