Please use this identifier to cite or link to this item:
|Title:||The invariant F283 and its strategic position in the hydrophobic cleft of streptomyces jumonjinensis isopenicillin N synthase active site are functionally important|
|Keywords:||Deacetoxycephalosporin C synthase|
Isopenicillin N synthase
|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|
|Appears in Collections:||Staff Publications|
Show full item record
Files in This Item:
There are no files associated with this item.
checked on Sep 19, 2018
WEB OF SCIENCETM
checked on Sep 3, 2018
checked on Feb 25, 2018
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.