6895-64-3Relevant academic research and scientific papers
The substrate specificity of β,β-carotene 15,15′-monooxygenase
Wirtz, Gabriele M.,Bornemann, Claus,Giger, Alfred,Mueller, Robert K.,Schneider, Heinz,Schlotterbeck, Goetz,Schiefer, Gerhard,Woggon, Wolf-Dietrich
, p. 2301 - 2315 (2007/10/03)
The synthesis of several substrate analogues of the enzyme β,β-carotene 15,15′-monooxygenase is reported. The substrate specificity of enriched enzyme fractions isolated from chicken intestinal mucosa was investigated. Regarding substrate binding/cleavage, these experiments demonstrate that i) any deviation from the rod-like β,β-carotene structure is not tolerated, ii) one 'natural', unsubstituted β-ionone ring is required, iii) the position and presence of the Me groups attached to the polyene chain is significant. These results suggest a hydrophobic barrel-like substrate binding site in which the protein's amino acid residues through interaction with the Me groups, direct the central C=C bond in binding distance to the active site's metal-oxo center, supporting the unique regiospecificity of cleavage to retinal (provitamin A).
