Structural basis of enzymatic S-norcoclaurine biosynthesis. (Articolo in rivista)

Type
Label
  • Structural basis of enzymatic S-norcoclaurine biosynthesis. (Articolo in rivista) (literal)
Anno
  • 2008-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1074/jbc.M803738200 (literal)
Alternative label
  • Ilari A, Franceschini S, Bonamore A, Arenghi F, Botta B, Macone A, Pasquo A, Bellucci L, Boffi A (2008)
    Structural basis of enzymatic S-norcoclaurine biosynthesis.
    in The Journal of biological chemistry (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Ilari A, Franceschini S, Bonamore A, Arenghi F, Botta B, Macone A, Pasquo A, Bellucci L, Boffi A (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 284 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • 1. Univ Roma La Sapienza, Dipartimento Sci Biochim, I-00185 Rome, Italy 2. Univ Roma La Sapienza, Ist Biol & Patol Mol, CNR, I-00185 Rome, Italy 3. CPC Biotech Srl, I-80121 Naples, Italy 4. Univ Roma La Sapienza, Dipartimento Chim & Tecnol Farmaco, I-00185 Rome, Italy 5. ENEA Casaccia Res Ctr, Dipartimento BIOTEC, Sez Genet & Genom Vegetale, I-00100 Rome, Italy 6. Univ Siena, Ist Tecn Chim Farmacol, I-53110 Siena, Italy (literal)
Titolo
  • Structural basis of enzymatic S-norcoclaurine biosynthesis. (literal)
Abstract
  • The enzyme norcoclaurine synthase (NCS) catalyzes the stereospecific Pictet-Spengler cyclization between dopamine and 4-hydroxyphenylacetaldehyde, the key step in the benzylisoquinoline alkaloid biosynthetic pathway. The crystallographic structure of norcoclaurine synthase from Thalictrum flavum in its complex with dopamine substrate and the nonreactive substrate analogue 4-hydroxybenzaldehyde has been solved at 2.1 angstrom resolution. NCS shares no common features with the functionally correlated \"Pictet-Spenglerases\" that catalyze the first step of the indole alkaloids pathways and conforms to the overall fold of the Bet v1-like protein. The active site of NCS is located within a 20-angstrom-long catalytic tunnel and is shaped by the side chains of a tyrosine, a lysine, an aspartic, and a glutamic acid. The geometry of the amino acid side chains with respect to the substrates reveals the structural determinants that govern the mechanism of the stereoselective Pictet-Spengler cyclization, thus establishing an excellent foundation for the understanding of the finer details of the catalytic process. Site-directed mutations of the relevant residues confirm the assignment based on crystallographic findings. (literal)
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