African Journal of
Pharmacy and Pharmacology

  • Abbreviation: Afr. J. Pharm. Pharmacol.
  • Language: English
  • ISSN: 1996-0816
  • DOI: 10.5897/AJPP
  • Start Year: 2007
  • Published Articles: 2218

Full Length Research Paper

Molecular cloning and characterization of a new cDNA encoding a trypsin-like serine protease from the venom gland of Scolopendra subspinipes mutilans

Junli Guo1,2, Ruhong Zhang3, Junfu Wang4 and Lixia Miao1*
1School of Basic Medical Sciences, Wuhan University, Wuhan 430072, China. 2College of Life Sciences, Henan Normal University, Xinxiang 453007, China. 3Renmin Hospital of Wuhan University, Wuhan, Hubei 430060, China. 4Department of Life Sciences and Technology, Xinxiang University, Xinxiang 453003, China.
Email: [email protected]

  •  Accepted: 24 April 2013
  •  Published: 08 May 2013


A cDNA encoding a new putative serine protease, named Ssmase, was cloned and characterized from the venom gland of the centipede Scolopendra subspinipes mutilans. The cDNA sequence was 1029 bp length, including a 780 bp open reading frame (ORF), a 105 bp 5 untranslated region, and a 144 bp 3 untranslated region. The precursor nucleotide sequence of Ssmase was deduced to encode a prepro-peptide of 19 residues and a mature protein of 240 residues. The 19 amino acid residues prepro-peptide of Ssmase putatively composed of 14 amino acids of pre-peptide and 5 amino acids of propeptide (QGSSA). The mature protein of Ssmase contained the typical domain of a trypsin-like serine protease, where His61, Asp108 and Ser208 were the principal residues of the catalytic center. The cysteine residues at 46 to 62, 141 to 214, 180 to 195 and 204 to 233 possibly formed four pairs of disulfide bridges. Ssmase was found to have five N-glycosylation sites (N-Xaa-T/S). To the best of our knowledge, Ssmase was a trypsin-like serine protease firstly characterized from centipede venoms. Ssmase represented a new family of trypsin-like serine protease with four disulfide bridge motif.


Key words: Centipede, Scolopendra subspinipes mutilans, trypsin-like serine protease, cysteine motif.