Natural Diels-Alderases: Elusive and Irresistable.
Eight examples of biosynthetic pathways wherein a natural enzyme has been identified and claimed to function as a catalyst for the [4 + 2] cycloaddition reaction, namely, Diels-Alderases, are briefly reviewed. These are discussed in the context of the mechanistic challenges associated with the technical difficulty of proving that the net formal [4 + 2] cycloaddition under study indeed proceeds through a synchronous mechanism and that the putative biosynthetic enzyme deploys the pericyclic transition state required for a Diels-Alder cycloaddition reaction.
Department of Chemistry, Colorado State University , Fort Collins, Colorado 80524, United States.
Kimberly
K
Klas
Graduate School of Pharmaceutical Sciences, Kumamoto University , 5-1 Oe-honmachi, Kumamoto 862-0973, Japan.
Sachiko
S
Tsukamoto
Life Sciences Institute and Departments of Medicinal Chemistry, Microbiology & Immunology, and Chemistry, University of Michigan , Ann Arbor, Michigan 48109, United States.
David H
DH
Sherman
Department of Chemistry, Colorado State University , Fort Collins, Colorado 80524, United States.|University of Colorado Cancer Center , Aurora, Colorado 80045, United States.
Robert M
RM
Williams
D055162:Biocatalysis; D001688:Biological Products / Q000138:chemical synthesis* / Q000737:chemistry / Q000378:metabolism; D018360:Crystallography, X-Ray; D061565:Cycloaddition Reaction; D009281:Naphthalenes / Q000138:chemical synthesis* / Q000737:chemistry / Q000378:metabolism; D011753:Pyrones / Q000138:chemical synthesis* / Q000737:chemistry / Q000378:metabolism
D001688:Biological Products; D009281:Naphthalenes; D011753:Pyrones; C113269:solanapyrone B; C113266:solanapyrone A