Please use this identifier to cite or link to this item: https://doi.org/10.1016/0378-1097(94)90478-2
Title: Histidine-272 of isopenicillin N synthase of Cephalosporium acremonium, which is possibly involved in iron binding, is essential for its catalytic activity
Authors: Tiow-Suan, S. 
Tan, D.S.H. 
Keywords: Cephalosporium acremonium
Iron binding
Isopenicillin N synthase
Site-directed mutagenesis
Issue Date: 1994
Citation: Tiow-Suan, S., Tan, D.S.H. (1994). Histidine-272 of isopenicillin N synthase of Cephalosporium acremonium, which is possibly involved in iron binding, is essential for its catalytic activity. FEMS Microbiology Letters 120 (3) : 241-248. ScholarBank@NUS Repository. https://doi.org/10.1016/0378-1097(94)90478-2
Abstract: Amino acid sequence alignment of the Cephalosporium acremonium isopenicillin N synthase (cIPNS) to similar non-heme Fe2+-containing enzymes from 28 different sources (bacterial, fungal, plant and animals) revealed a homologous region of high sequence conservation containing an invariant histidine residue at position 272 in cIPNS. The importance of this histidine residue in cIPNS was investigated through site-directed mutagenesis by replacing the histidine residue with leucine. The mutated gene was verified by DNA sequence analysis and expressed in Escherichia coli. When analyzed by denaturing gel electrophoresis and immunoblotting, the mutant cIPNS had identical mobility as that of the wild-type enzyme. Enzyme studies on the mutant enzyme showed loss of enzymatic activity indicating that His272 is essential for the catalytic function of cIPNS, possibly as a ligand for iron binding.
Source Title: FEMS Microbiology Letters
URI: http://scholarbank.nus.edu.sg/handle/10635/131247
ISSN: 03781097
DOI: 10.1016/0378-1097(94)90478-2
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