| IED ID | IndEnz0005000922 |
| Enzyme Type ID | lipase000922 |
| Protein Name |
Tuliposide B-converting enzyme 1, amyloplastic TgTCEB1 EC 4.2.99.23 |
| Gene Name | TCEB1 |
| Organism | Tulipa gesneriana (Garden tulip) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae Liliopsida Petrosaviidae Liliales Liliaceae Tulipa Tulipa gesneriana (Garden tulip) |
| Enzyme Sequence | MSIVSFCSSLPAGPHGFKHGRGTRDMVHMPCIVRRTARSPAQACRLLRWNKYHCAAVPTNSSLSPSPTPLDVEIELDLEPFLIKYKSGRIERLGRFGDRTDYVEASLDPATEVTSRDAITDTGVPVRIYLPKVDDSPPNSLRVLVYFHGGAFLVEDSASPPYHNYLNNLASKANILIVSVNYRLAPEYPLPVAYDDCMEALNWVNKHSDGTGQEDWINKHGDFDHLFISGDSAGGNITHNIAMSTDAPKNIEGIALVHPYFFGKVALETELQDPTNLLLHRKLWSFITPESEGLDDPRVNPLGPTAPSLEKIKCKRAVVFVAGEDFHSERGRKYSEKLKSEFKGEVPLLCNHDGVGHVYHLSVDATEEEIESAAAWKMMTDLLKFYKDNDVVLEGSIVESLKAKTTEGIKKMKEIEKGMSERMMEQLVAFYNGKPVPYSS |
| Enzyme Length | 440 |
| Uniprot Accession Number | A0A0H5BMX5 |
| Absorption | |
| Active Site | ACT_SITE 232; /note=Acyl-ester intermediate; /evidence=ECO:0000250|UniProtKB:I4DST8; ACT_SITE 325; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:I4DST8; ACT_SITE 357; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:I4DST8 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by Ag(+), Cu(2+), Fe(2+), Hg(2+), V(3+) and phenylmethylsulfonyl fluoride (PMSF). {ECO:0000269|PubMed:25997073}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=6-tuliposide B = D-glucose + tulipalin B; Xref=Rhea:RHEA:38655, ChEBI:CHEBI:4167, ChEBI:CHEBI:87123, ChEBI:CHEBI:87124; EC=4.2.99.23; Evidence={ECO:0000269|PubMed:25997073}; |
| DNA Binding | |
| EC Number | 4.2.99.23 |
| Enzyme Function | FUNCTION: Lactone-forming carboxylesterase, specifically catalyzing intramolecular transesterification, but not hydrolysis. Involved in the biosynthesis of tulipalins, defensive chemicals that show antimicrobial activities against a broad range of strains of bacteria and fungi. Substrates are 6-tuliposide B > 6-tuliposide A. {ECO:0000269|PubMed:25997073}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30-40 degrees Celsius. {ECO:0000269|PubMed:25997073}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0-7.5. {ECO:0000269|PubMed:25997073}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Transit peptide (1) |
| Keywords | Amyloplast;Direct protein sequencing;Lyase;Plant defense;Plastid;Transit peptide |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Plastid {ECO:0000269|PubMed:25997073}. Plastid, amyloplast {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | PTM: Not glycosylated. {ECO:0000269|PubMed:25997073}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 49,023 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.0 mM for 6-tuliposide A {ECO:0000269|PubMed:25997073}; KM=6.8 mM for 6-tuliposide B {ECO:0000269|PubMed:25997073}; Note=kcat is 8.7 sec(-1) with 6-tuliposide A as substrate. kcat is 2000 sec(-1) with 6-tuliposide B as substrate. {ECO:0000269|PubMed:25997073}; |
| Metal Binding | |
| Rhea ID | RHEA:38655 |
| Cross Reference Brenda |