NascB

Evidence from

Substrate reaction site Product reaction site MCS substructure diff highlighting · RDKit atom mapping

Substrate

cyclo-(L-tryptophan-L-proline)

PubChem ↗ N1[C@@H](CCC1)C(=O)O.N[C@@H](CC1=CNC2=CC=CC=C12)C(=O)O

NascB

ΔMass: no_smiles Missing dual SMILES or RDKit not validated

Product

(-)-naseseazine C

PubChem ↗ Crowdsource product structure

Evidence trail

Excerpts are machine-extracted plain text for biochemical provenance. Follow DOI / PubMed links for the primary literature; publisher figures and PDF images are not displayed here.

Source text excerpt Other; Other; P450 NascB catalyzes dimerization of cyclo-(L-tryptophan-L-proline) to (-)-naseseazine C via intramolecular C-N bond formation and intermolecular C-C coupling. Evidence from experimental characterization (refs 27-30) and computational validation. Source organism not specified in abstract or methods; likely from a bacterial or fungal source, not plant.

Reaction & quality gates

Mechanism: Other
Evidence type: In vitro
Confidence: High
Data tier: Silver
mass=no_smiles; incomplete_SMILES
Substrate class: Other
Product class: Other

Literature & public identifiers

PubMed: PMID:38665654 ↗
DOI: 10.1021/jacsau.4c00075 ↗
UniProt: —
GenBank: —
NCBI TaxID: —

Substrate Conformational Switch Enables the Stereoselective Dimerization in P450 NascB: Insights from Molecular Dynamics Simulations and Quantum Mechanical/Molecular Mechanical Calculations.