Please use this identifier to cite or link to this item: https://doi.org/10.1006/bbrc.2001.4781
Title: The invariant F283 and its strategic position in the hydrophobic cleft of streptomyces jumonjinensis isopenicillin N synthase active site are functionally important
Authors: Wong, E.
Sim, J. 
Sim, T.-S. 
Keywords: Deacetoxycephalosporin C synthase
Hydrophobic cavity
Isopenicillin N synthase
Phenylalanine
Site-directed mutagenesis
Issue Date: 2001
Citation: Wong, E., Sim, J., Sim, T.-S. (2001). The invariant F283 and its strategic position in the hydrophobic cleft of streptomyces jumonjinensis isopenicillin N synthase active site are functionally important. Biochemical and Biophysical Research Communications 283 (3) : 621-626. ScholarBank@NUS Repository. https://doi.org/10.1006/bbrc.2001.4781
Abstract: Isopenicillin N synthase (IPNS) and related non-haem iron-binding enzymes including deacetoxycephalosporin C synthase (DAOCS) are proposed to have structurally similar active centers. Sequence alignment and computational structural analyses of predicted structures revealed 11 highly conserved hydrophobic amino acid residues in 134 IPNS-related enzymes form a contiguous hydrophobic patch in the IPNS active center, wherein F283 is strategically positioned. The investigation of single and double mutations at F283, adjacent (L284) and proximal sites (N285 and S216) of Streptomyces jumonjinensis IPNS advocate the explicit importance of the phenyl ring at position 283. A similarly placed phenylalanine (F264) in DAOCS was found to be also crucial for its enzyme activity. © 2001 academic Press.
Source Title: Biochemical and Biophysical Research Communications
URI: http://scholarbank.nus.edu.sg/handle/10635/130346
ISSN: 0006291X
DOI: 10.1006/bbrc.2001.4781
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