Structural studies of natural product biosynthetic proteins

Chemistry and Biology

Volumn 4, Issue 10, 1997, Pages 721-730

  Townsend, Craig A ^a  

^a JOHNS HOPKINS UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANIMALIA;

EID: 0031259902     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1074-5521(97)90310-0     Document Type: Review

References (10)

1. Roach, P.L, et al., & Baldwin, J.E. (1997). Structure of isopenicillin N synthase complexed with substrate and the mechanism of penicillin formation. Nature 387, 827-830.
2. Baldwin, J.E., Adlington, R.M., Moroney, S.E., Field, L.D. & Ting, H.-H. (1984). Stepwise ring closure in penicillin biosynthesis. Initial β-lactam formation. J. Chem. Soc., Chem. Commun., 984-986.
3. White, R.L., John, E.-M.M., Baldwin, J.E. & Abraham, E.P. (1982). Stoichiometry of oxygen consumption in the biosynthesis of isopenicillin from atripeptide. Biochem. J. 203, 791-793.
4. Kleinkauf, H. & Von Döhren, H. (1996). A nonribosomal system of peptide biosynthesis. Eur. J. Biochem. 236, 335-351.
5. Stachelhaus, T. & Marahiel, M.A. (1995). Modular structure of genes encoding multifunctional peptide synthetases required for nonribosomal peptide synthesis. FEMS Microbiol. Lett. 125, 3-14.
6. Roach, P.L., et al., & Baldwin, J.E. (1995). Crystal structure of isopenicillin N synthase is the first from a new structural family of enzymes. Nature 375, 700-704.
7. 2+ of isopenicillin N synthase derives from substrate rather than endogenous cysteine: spectroscopic studies of site-specific Cys→Ser mutated enzymes. Biochemistry 31, 4602-4612.
8. Que, J., L. & Ho, R.Y.N. (1996). Dioxygen activation by enzymes with mononuclear non-heme iron active sites. Chem. Rev. 96, 2607-2624.
9. Baldwin, J.E. & Abraham, E. (1988). The biosynthesis of penicillins and cephalosporins. Nat. Prod. Reports 5, 129-145.
10. Krol, W.J., Basak, A., Salowe, S.P. & Townsend, C.A. (1989). Oxidative cyclization chemistry catalyzed by clavaminate synthase. J. Am. Chem. Soc. 111, 7625-7627.