|Family type peptidase||M77.001 - tryptophanyl aminopeptidase 7-DMATS-type peptidase (Aspergillus fumigatus), MEROPS Accession MER0066227 (peptidase unit: 1-472)|
|Content of family||Family M77 contains aminopeptidases.|
Identifier created: MEROPS 8.3 (22 December 2008)|
The dimethylallyltryptophan synthase 7-DMATS (M77.001) catalyzes the prenylation of L-tryptophan at position C7 of the indole ring. In a study of potential substrates, it was discovered that 7-DMATS could also accept tryptophan-containing cyclic dipeptides and linear dipeptides such as Trp-Gly. Two products were detected using Trp-Gly, 7-dimethylallyltryptophan and 7-dimethylallyltryptophan-Gly, which implied that 7-DMATS was also acting as a peptidase (Kremer & Li, 2008). Release of modified Trp from tetrapeptides by the prenyltransferase CdpNPT (M77.003) confirmed that the enzyme was acting as an aminopeptidase (Kremer & Li, 2008). A tryptophanyl aminopeptidase from the fungus Trichosporon cutaneum (##M9A.008##) was biochemically characterized in 1983, but has never been sequenced (Iwayama et al., 1983) and may be a homologue.
|Active site||No active site residues or metal ligands have been identified. The tryptophanyl aminopeptidase from Trichosporon cutaneum is dependent on manganese (Iwayama et al., 1983).|
|Inhibitors||Both 7-DMATS and FgaPT1(M77.002) are inhibited by EDTA (Kremer & Li, 2008).|
|Molecular structure||No tertiary structure has been solved for any member of the family.|