| IED ID | IndEnz0002016503 |
| Enzyme Type ID | protease016503 |
| Protein Name |
7-dimethylallyltryptophan synthase 7-DMATS EC 2.5.1.80 Tryptophan aminopeptidase EC 3.4.11.17 |
| Gene Name | etpPT AFUA_3G12930 |
| Organism | Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Fumigati Neosartorya fumigata (Aspergillus fumigatus) Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) |
| Enzyme Sequence | MSIGAEIDSLVPAPPGLNGTAAGYPAKTQKELSNGDFDAHDGLSLAQLTPYDVLTAALPLPAPASSTGFWWRETGPVMSKLLAKANYPLYTHYKYLMLYHTHILPLLGPRPPLENSTHPSPSNAPWRSFLTDDFTPLEPSWNVNGNSEAQSTIRLGIEPIGFEAGAAADPFNQAAVTQFMHSYEATEVGATLTLFEHFRNDMFVGPETYAALRAKIPEGEHTTQSFLAFDLDAGRVTTKAYFFPILMSLKTGQSTTKVVSDSILHLALKSEVWGVQTIAAMSVMEAWIGSYGGAAKTEMISVDCVNEADSRIKIYVRMPHTSLRKVKEAYCLGGRLTDENTKEGLKLLDELWRTVFGIDDEDAELPQNSHRTAGTIFNFELRPGKWFPEPKVYLPVRHYCESDMQIASRLQTFFGRLGWHNMEKDYCKHLEDLFPHHPLSSSTGTHTFLSFSYKKQKGVYMTMYYNLRVYST |
| Enzyme Length | 472 |
| Uniprot Accession Number | Q4WYG3 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=dimethylallyl diphosphate + L-tryptophan = 7-(3-methylbut-2-enyl)-L-tryptophan + diphosphate; Xref=Rhea:RHEA:30563, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:57912, ChEBI:CHEBI:62497; EC=2.5.1.80; Evidence={ECO:0000269|PubMed:17906140, ECO:0000269|PubMed:18481055}; CATALYTIC ACTIVITY: Reaction=Preferential release of N-terminal tryptophan.; EC=3.4.11.17; Evidence={ECO:0000269|PubMed:18635009}; |
| DNA Binding | |
| EC Number | 2.5.1.80; 3.4.11.17 |
| Enzyme Function | FUNCTION: Catalyzes the prenylation of L-tryptophan at the C-7 position of the indole moiety. The enzyme is specific for dimethylallyl diphosphate (DMAPP) as prenyl donor. Accepts also D-tryptophan, typtophan-derivatives with modifications at the side chain or the indole ring, and linear and cyclic dipeptides such as H-L-Trp-L-Gly-OH or cyclo-L-Trp-L-Gly as substrates, however with lower efficiency. Also has tryptophan aminopeptidase activity towards linear peptides with a tryptophanyl moiety at the N-terminus. Dipeptides are better substrates than peptides with 3 or more amino acids. Enzymatic rate constants however are much higher for the prenyltransferase activity than for the aminopeptidase activity. {ECO:0000269|PubMed:17906140, ECO:0000269|PubMed:18481055, ECO:0000269|PubMed:18635009}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Natural variant (2) |
| Keywords | Aminopeptidase;Hydrolase;Protease;Reference proteome;Transferase |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 52,688 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=67 uM for dimethylallyl diphosphate {ECO:0000269|PubMed:17906140}; KM=137 uM for L-tryptophan {ECO:0000269|PubMed:17906140}; KM=350 uM for H-L-Trp-L-Gly-OH (for aminopeptidase activity) {ECO:0000269|PubMed:17906140}; Vmax=0.21 umol/min/mg enzyme {ECO:0000269|PubMed:17906140}; |
| Metal Binding | |
| Rhea ID | RHEA:30563 |
| Cross Reference Brenda | 2.5.1.80; |