African Journal of
Microbiology Research

  • Abbreviation: Afr. J. Microbiol. Res.
  • Language: English
  • ISSN: 1996-0808
  • DOI: 10.5897/AJMR
  • Start Year: 2007
  • Published Articles: 5211

Full Length Research Paper

Predicting the catalytic sites of Streptomyces clavuligerus deacetylcephalosporin c synthase and clavaminate synthase 2

  Hong Soon Chin1*, Khang Wen Goh1, Kah Cheng Teo1, Mun Yee Chan1, Seong Wei Lee2 and Lisa Gaik Ai Ong1
  1Faculty of Science, Universiti Tunku Abdul Rahman, Kampar, Malaysia. 2Faculty of Agro Industry and Nature Resources, University Malaysia Kelantan, Kota Bharu, Malaysia.
Email: [email protected]

  •  Accepted: 30 July 2011
  •  Published: 09 October 2011



Enzymes categorized under the 2OG-Fe (II) oxygenase superfamily and Taurine catabolism dioxygenase TauD family demonstrated a striking structural conserveness even with low protein sequence homology. It is evident that these enzymes have an architecturally similar to catalytic centre with active ligands lining the reactive pocket. Deacetoxycephalosporin C synthase (DAOCS), isopenicillin N synthase (IPNS), deacetylcephalosporin C synthase (DACS), clavaminate synthase 1 and 2 (CAS1 and 2) are important bacterial enzymes that catalyze the formation of β-lactam antibiotics. With the advancement of protein structural analysis software, it is possible to predict the catalytic sites of protein that shared a structural resemblance. By exploiting the superimposition model of DAOCS-IPNS, DAOCS-CAS1 and IPNS-CAS1, a computational protocol for predicting the catalytic sites of proteins is now made available. This study shows that without the crystallized or NMR structures of DACS and CAS2, the plausible catalytic sites of protein can be forecasted using this structural bioinformatics approach.


Key words: Isopenicillin N synthase (IPNS), deacetoxycephalosporin C synthase (DAOCS),  deacetylcephalosporin C synthase (DACS), clavaminate synthase (CAS), 2OG-Fe (II) oxygenase superfamily.