Please use this identifier to cite or link to this item: https://doi.org/10.1016/0378-1097(94)90478-2
DC FieldValue
dc.titleHistidine-272 of isopenicillin N synthase of Cephalosporium acremonium, which is possibly involved in iron binding, is essential for its catalytic activity
dc.contributor.authorTiow-Suan, S.
dc.contributor.authorTan, D.S.H.
dc.date.accessioned2016-11-28T10:17:57Z
dc.date.available2016-11-28T10:17:57Z
dc.date.issued1994
dc.identifier.citationTiow-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
dc.identifier.issn03781097
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/131247
dc.description.abstractAmino 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.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1016/0378-1097(94)90478-2
dc.sourceScopus
dc.subjectCephalosporium acremonium
dc.subjectIron binding
dc.subjectIsopenicillin N synthase
dc.subjectSite-directed mutagenesis
dc.typeArticle
dc.contributor.departmentMICROBIOLOGY
dc.description.doi10.1016/0378-1097(94)90478-2
dc.description.sourcetitleFEMS Microbiology Letters
dc.description.volume120
dc.description.issue3
dc.description.page241-248
dc.description.codenFMLED
dc.identifier.isiutA1994NX64000005
Appears in Collections:Staff Publications

Show simple item record
Files in This Item:
There are no files associated with this item.

WEB OF SCIENCETM
Citations

1
checked on Sep 27, 2022

Page view(s)

99
checked on Sep 22, 2022

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.