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Molecular and biochemical characterization of Paragonimus westermani tyrosinase

Published online by Cambridge University Press:  26 January 2015

Y.-A. BAE ,
S.-H. KIM ,
C.-S. AHN ,
J.-G. KIM  and
Y. KONG
Y.-A. BAE
Affiliation:
Department of Microbiology, Gachon University Graduate School of Medicine, Incheon 406-799, Korea
S.-H. KIM
Affiliation:
Department of Microbiology, Gachon University Graduate School of Medicine, Incheon 406-799, Korea
C.-S. AHN
Affiliation:
Department of Molecular Parasitology, Sungkyunkwan University School of Medicine, and Center for Molecular Medicine, Samsung Biomedical Research Institute, Suwon 440-746, Korea
J.-G. KIM
Affiliation:
Department of Molecular Parasitology, Sungkyunkwan University School of Medicine, and Center for Molecular Medicine, Samsung Biomedical Research Institute, Suwon 440-746, Korea
Y. KONG*
Affiliation:
Department of Molecular Parasitology, Sungkyunkwan University School of Medicine, and Center for Molecular Medicine, Samsung Biomedical Research Institute, Suwon 440-746, Korea
*
* Corresponding author. Department of Molecular Parasitology, Sungkyunkwan University School of Medicine, Suwon 440-746, Korea. E-mail: [email protected]
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Summary

Trematode tyrosinases (TYRs) play a major role in the tanning process during eggshell formation. We investigated the molecular and biochemical features of Paragonimus westermani TYR (PwTYR). The PwTYR cDNA was composed of 1568-bp encompassing a 1422-bp-long open reading frame (474-amino acid polypeptide). A strong phylogenetic relationship with Platyhelminthes and Deuterostomian orthologues was evident. The recombinant PwTYR expressed in prokaryotic cells promptly oxidized diphenol substrates, with a preferential affinity toward ortho-positioned hydroxyl groups. It demonstrated fairly weak activity for monophenol compounds. Diphenol oxidase activity was augmented with an increase of pH from 5·0 to 8·0, while monophenol oxidase activity was highest at an acidic pH and gradually decreased as pH increased. Transcription profile of PwTYR was temporally upregulated along with worm development. PwTYR was specifically localized in vitellocytes and eggs. The results suggested that conversion of tyrosine to L-dihydroxyphenylalanine by PwTYR monophenol oxidase activity might be rate-limiting step during the sclerotization process of P. westermani eggs. The pH-dependent pattern of monophenol and diphenol oxidase activity further proposes that the initial hydroxylation might slowly but steadily progress in acidic secreted vesicles of vitellocytes and the second oxidation process might be rapidly accelerated by neural or weak alkaline pH environments within the ootype.

Keywords

Paragonimus westermanityrosinaserecombinant enzymepH-dependent tyrosinase activityeggshellvitellocyte
Type
Research Article
Information
Parasitology , Volume 142 , Issue 6 , May 2015 , pp. 807 - 815
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Copyright
Copyright © Cambridge University Press 2015 

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