IED ID | IndEnz0010001872 |
Enzyme Type ID | esterase001872 |
Protein Name |
Dehydrogenase mokE EC 1.-.-.- Enoyl reductase Monacolin K biosynthesis protein E |
Gene Name | mokE |
Organism | Monascus pilosus (Red mold) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Monascus Monascus pilosus (Red mold) |
Enzyme Sequence | MTITFTLPPHQTALTVDEHDKVTIWDVAPCPSLPPDQVCVRVEAVALNPSDTKMRGQFATPYAFLGTDYAGTVVAVGSQVTHIQVGDRVYGAQNEMCPRTPDQGAFSQYTVTRGRIWATVPEGWSFEQAASLPAGISTAGLAMKLLGLPLPDPNATTAPALPKPVYVLVYGGSTATATIVMQMLRLSGYIPIATCSPHNFDLAKKHGAEDVFDYRDAGLAQTIRTYTKNNLRYALDCITNVESTTLCFAAIGRAGGRYVSLNPFPEHAATRKMVTADWTLGPTIFGEGSTWPAPYGRPGSEKDRAFGEELWRVAARLVEDGKIVHHPLRVIPGGFEAIKQGMELVRTGQLSGEKVVVKLG |
Enzyme Length | 360 |
Uniprot Accession Number | Q3S2U1 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | BINDING 214; /note=NADP; /evidence=ECO:0000250|UniProtKB:Q9Y7D0; BINDING 279; /note=NADP; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q9Y7D0 |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 1.-.-.- |
Enzyme Function | FUNCTION: Dehydrogenase; part of the gene cluster that mediates the biosynthesis of monakolin K, also known as lovastatin, and which acts as a potent competitive inhibitor of HMG-CoA reductase (PubMed:18578535). Monakolin K biosynthesis is performed in two stages (PubMed:19693441). The first stage is catalyzed by the nonaketide synthase mokA, which belongs to type I polyketide synthases and catalyzes the iterative nine-step formation of the polyketide (PubMed:18578535, PubMed:19693441). This PKS stage is completed by the action of dehydrogenase mokE, which catalyzes the NADPH-dependent reduction of the unsaturated tetra-, penta- and heptaketide intermediates that arise during the mokA-mediated biosynthesis of the nonaketide chain and leads to dihydromonacolin L (PubMed:19693441). Covalently bound dihydromonacolin L is released from mokA by the mokD esterase (By similarity). Conversion of dihydromonacolin L into monacolin L and then monacolin J is subsequently performed with the participation of molecular oxygen and P450 monoogygenase mokC (PubMed:19693441). Finally, mokF performs the conversion of monacoline J to monacoline K through the addition of the side-chain diketide moiety (2R)-2-methylbutanoate produced by the diketide synthase mokB (PubMed:19693441). {ECO:0000250|UniProtKB:Q0C8M2, ECO:0000303|PubMed:18578535, ECO:0000303|PubMed:19693441}. |
Temperature Dependency | |
PH Dependency | |
Pathway | PATHWAY: Polyketide biosynthesis; lovastatin biosynthesis. {ECO:0000250|UniProtKB:Q9Y7D0}. |
nucleotide Binding | NP_BIND 50..53; /note=NADP; /evidence=ECO:0000250|UniProtKB:Q9Y7D0; NP_BIND 173..176; /note=NADP; /evidence=ECO:0000250|UniProtKB:Q9Y7D0; NP_BIND 196..199; /note=NADP; /evidence=ECO:0000250|UniProtKB:Q9Y7D0; NP_BIND 261..262; /note=NADP; /evidence=ECO:0000250|UniProtKB:Q9Y7D0; NP_BIND 350..351; /note=NADP; /evidence=ECO:0000250|UniProtKB:Q9Y7D0 |
Features | Binding site (2); Chain (1); Nucleotide binding (5); Region (2) |
Keywords | NADP;Nucleotide-binding;Oxidoreductase |
Interact With | |
Induction | INDUCTION: Expression is controlled by the monacolin K cluster transcription regulator mokH (PubMed:19968298). {ECO:0000269|PubMed:19968298}. |
Subcellular Location | |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 38,845 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |